1. Key Laboratory of Brain, Cognition and Education Sciences, Ministry of Education Institute for Brain, Science and Rehabilitation, South China Normal University,Guangdong,Guangzhou,China,510631
2. Department of Ophthalmology, Guangdong Second Provincial General Hospital,Guangdong,Guangzhou,China,510320
3. LIMES Institute, Department of Molecular Brain Physiology and Behavior, University of Bonn, Bonn,Germany,53115
4. Institute of Physiology and Pathophysiology, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen,Germany,91054
Published:2023,
Published Online:1 November 2023,
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Meilan Chen, Lu Xu, Yi Wu, et al. The organization and function of the Golgi apparatus in dendrite development and neurological disorders. [J]. Genes & Diseases 1(6):2425-2442(2023)
Meilan Chen, Lu Xu, Yi Wu, et al. The organization and function of the Golgi apparatus in dendrite development and neurological disorders. [J]. Genes & Diseases 1(6):2425-2442(2023) DOI: 10.1016/j.gendis.2022.11.009.
Dendrites are specialized neuronal compartments that sense
integrate and transfer information in the neural network. Their development is tightly controlled and abnormal dendrite morphogenesis is strongly linked to neurological disorders. While dendritic morphology ranges from relatively simple to extremely complex for a specified neuron
either requires a functional secretory pathway to continually replenish proteins and lipids to meet dendritic growth demands. The Golgi apparatus occupies the center of the secretory pathway and is regulating posttranslational modifications
sorting
transport
and signal transduction
as well as acting as a non-centrosomal microtubule organization center. The neuronal Golgi apparatus shares common features with Golgi in other eukaryotic cell types but also forms distinct structures known as Golgi outposts that specifically localize in dendrites. However
the organization and function of Golgi in dendrite development and its impact on neurological disorders is just emerging and so far lacks a systematic summary. We describe the organization of the Golgi apparatus in neurons
review the current understanding of Golgi function in dendritic morphogenesis
and discuss the current challenges and future directions.
DendriteGolgiGolgi outpostsMicrotubuleNeurodevelopmental disordersSecretory pathway
1 A.J. KoleskeMolecular mechanisms of dendrite stability Nat Rev Neurosci, 14 (8) (2013), pp. 536-550
2 M.J. Kennedy, C. HanusArchitecture and dynamics of the neuronal secretory network Annu Rev Cell Dev Biol, 35 (2019), pp. 543-566
3 S. Huang, Y. WangGolgi structure formation, function, and post-translational modifications in mammalian cells F1000Res, 6 (2017), p. 2050
4 W. ZhongGolgi during development Cold Spring Harbor Perspect Biol, 3 (9) (2011), p. a005363
5 K. Park, S. Ju, N. Kim, et al.The Golgi complex: a hub of the secretory pathway BMB Rep, 54 (5) (2021), pp. 246-252
6 A.A.W.M. Sanders, I. KaverinaNucleation and dynamics of Golgi-derived microtubules Front Neurosci, 9 (2015), p. 431
7 Y. Ravichandran, B. Goud, J.B. MannevilleThe Golgi apparatus and cell polarity: roles of the cytoskeleton, the Golgi matrix, and Golgi membranes Curr Opin Cell Biol, 62 (2020), pp. 104-113
8 L. Fourriere, A.J. Jimenez, F. Perez, et al.The role of microtubules in secretory protein transport J Cell Sci, 133 (2) (2020), p. jcs237016
9 F. Zappa, M. Failli, M.A. De MatteisThe Golgi complex in disease and therapy Curr Opin Cell Biol, 50 (2018), pp. 102-116
10 S. Passemard, F. Perez, E. Colin-Lemesre, et al.Golgi trafficking defects in postnatal microcephaly: the evidence for “Golgipathies” Prog Neurobiol, 153 (2017), pp. 46-63
11 S. Rasika, S. Passemard, A. Verloes, et al.Golgipathies in neurodevelopment: a new view of old defects Dev Neurosci, 40 (5–6) (2018), pp. 396-416
12 J.Á. Martínez-Menárguez, M. Tomás, N. Martínez-Martínez, et al.Golgi fragmentation in neurodegenerative diseases: is there a common cause? Cells, 8 (7) (2019), p. 748
13 M.G. Bexiga, J.C. SimpsonHuman diseases associated with form and function of the Golgi complex Int J Mol Sci, 14 (9) (2013), pp. 18670-18681
14 M.M. Fu, T.S. McAlear, H. Nguyen, et al.The Golgi outpost protein TPPP nucleates microtubules and is critical for myelination Cell, 179 (1) (2019), pp. 132-146 e14
15 Z. Liu, M. Yan, W. Lei, et al.Sec13 promotes oligodendrocyte differentiation and myelin repair through autocrine pleiotrophin signaling J Clin Invest, 132 (7) (2022), Article e155096
16 B. Burke, G. Griffiths, H. Reggio, et al.A monoclonal antibody against a 135-K Golgi membrane protein EMBO J, 1 (12) (1982), pp. 1621-1628
17 J.E. RothmanThe Golgi apparatus: two organelles in tandem Science, 213 (4513) (1981), pp. 1212-1219
18 M.S. Ladinsky, D.N. Mastronarde, J.R. McIntosh, et al.Golgi structure in three dimensions: functional insights from the normal rat kidney cell J Cell Biol, 144 (6) (1999), pp. 1135-1149
19 M.S. Ladinsky, J.R. Kremer, P.S. Furcinitti, et al.HVEM tomography of the trans-Golgi network: structural insights and identification of a lace-like vesicle coat J Cell Biol, 127 (1) (1994), pp. 29-38
20 W. Zhou, J. Chang, X. Wang, et al.GM130 is required for compartmental organization of dendritic Golgi outposts Curr Biol, 24 (11) (2014), pp. 1227-1233
21 F.A. Barr, N. Nakamura, G. WarrenMapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae EMBO J, 17 (12) (1998), pp. 3258-3268
22 S. GoldfischerThe internal reticular apparatus of Camillo Golgi: a complex, heterogeneous organelle, enriched in acid, neutral, and alkaline phosphatases, and involved in glycosylation, secretion, membrane flow, lysosome formation, and intracellular digestion J Histochem Cytochem, 30 (7) (1982), pp. 717-733
23 R.D. Broadwell, C. OliverGolgi apparatus, GERL, and secretory granule formation within neurons of the hypothalamo-neurohypophysial system of control and hyperosmotically stressed mice J Cell Biol, 90 (2) (1981), pp. 474-484
24 L.K. Climer, R.D. Hendrix, V.V. LupashinConserved oligomeric Golgi and neuronal vesicular trafficking Handb Exp Pharmacol, 245 (2018), pp. 227-247
25 H.H. Mollenhauer, D. James MorréThe tubular network of the Golgi apparatus Histochem Cell Biol, 109 (5–6) (1998), pp. 533-543
26 A.A. Mironov, I.S. Sesorova, E.V. Seliverstova, et al.Different Golgi ultrastructure across species and tissues: implications under functional and pathological conditions, and an attempt at classification Tissue Cell, 49 (2 Pt A) (2017), pp. 186-201
27 V. Kondylis, C. RabouilleThe Golgi apparatus: lessons from Drosophila FEBS Lett, 583 (23) (2009), pp. 3827-3838
28 G. Lavieu, M.H. Dunlop, A. Lerich, et al.The Golgi ribbon structure facilitates anterograde transport of large cargoes Mol Biol Cell, 25 (19) (2014), pp. 3028-3036
29 F. Wendler, A.K. Gillingham, R. Sinka, et al.A genome-wide RNA interference screen identifies two novel components of the metazoan secretory pathway EMBO J, 29 (2) (2010), pp. 304-314
30 S. Springer, R. SchekmanNucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs Science, 281 (5377) (1998), pp. 698-700
31 S.J. Scales, R. Pepperkok, T.E. KreisVisualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI Cell, 90 (6) (1997), pp. 1137-1148
32 J.F. Presley, N.B. Cole, T.A. Schroer, et al.ER-to-Golgi transport visualized in living cells Nature, 389 (6646) (1997), pp. 81-85
33 C. Barlowe, L. Orci, T. Yeung, et al.COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum Cell, 77 (6) (1994), pp. 895-907
34 S. Soulier, P. GayeEnzymatic O-glycosylation of ℵ-caseinomacropeptide by ovine mammary Golgi membranes Biochimie, 63 (7) (1981), pp. 619-628
35 J. Hellicar, N.L. Stevenson, D.J. Stephens, et al.Supply chain logistics - the role of the Golgi complex in extracellular matrix production and maintenance J Cell Sci, 135 (1) (2022), p. jcs258879
36 R.W. YoungThe role of the Golgi complex in sulfate metabolism J Cell Biol, 57 (1) (1973), pp. 175-189
37 N. Lane, L. Caro, L.R. Otero-Vilardebó, et al.On the site of sulfation in colonic goblet cells J Cell Biol, 21 (3) (1964), pp. 339-351
38 A.M. Ernst, S.A. Syed, O. Zaki, et al.S-palmitoylation sorts membrane cargo for anterograde transport in the Golgi Dev Cell, 47 (4) (2018), pp. 479-493 e7
39 D.F. Steiner, K. Docherty, R. CarrollGolgi/granule processing of peptide hormone and neuropeptide precursors: a minireview J Cell Biochem, 24 (2) (1984), pp. 121-130
40 M.J. Lewis, H.R.B. PelhamSNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum Cell, 85 (2) (1996), pp. 205-215
41 F. Letourneur, E.C. Gaynor, S. Hennecke, et al.Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum Cell, 79 (7) (1994), pp. 1199-1207
42 L. Orci, M. Stamnes, M. Ravazzola, et al.Bidirectional transport by distinct populations of COPI-coated vesicles Cell, 90 (2) (1997), pp. 335-349
43 L. Orci, M. Ravazzola, M.J. Storch, et al.Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles Cell, 49 (6) (1987), pp. 865-868
44 G.S. Payne, R. SchekmanA test of clathrin function in protein secretion and cell growth Science, 230 (4729) (1985), pp. 1009-1014
45 Y. Tu, L. Zhao, D.D. Billadeau, et al.Endosome-to-TGN trafficking: organelle-vesicle and organelle-organelle interactions Front Cell Dev Biol, 8 (2020), p. 163
46 S. De Tito, J.H. Hervás, A.R. van Vliet, et al.The Golgi as an assembly line to the autophagosome Trends Biochem Sci, 45 (6) (2020), pp. 484-496
47 R. Mattera, S.Y. Park, R. De Pace, et al.AP-4 mediates export of ATG9A from the trans-Golgi network to promote autophagosome formation Proc Natl Acad Sci U S A, 114 (50) (2017), pp. E10697-E10706
48 A.R.J. Young, E.Y.W. Chan, X.W. Hu, et al.Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes J Cell Sci, 119 (18) (2006), pp. 3888-3900
49 M.N. Seaman, E.G. Marcusson, J.L. Cereghino, et al.Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products J Cell Biol, 137 (1) (1997), pp. 79-92
50 R.N. Ghosh, W.G. Mallet, T.T. Soe, et al.An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells J Cell Biol, 142 (4) (1998), pp. 923-936
51 J. Gao, A. Gao, H. Zhou, et al.The role of metal ions in the Golgi apparatus Cell Biol Int, 46 (9) (2022), pp. 1309-1319
52 J. Li, Y. WangGolgi metal ion homeostasis in human health and diseases Cells, 11 (2) (2022), p. 289
53 C. Hartwig, G.M. Méndez, S. Bhattacharjee, et al.Golgi-dependent copper homeostasis sustains synaptic development and mitochondrial content J Neurosci, 41 (2) (2021), pp. 215-233
54 V. Lissandron, P. Podini, P. Pizzo, et al.Unique characteristics of Ca2+ homeostasis of the trans-Golgi compartment Proc Natl Acad Sci U S A, 107 (20) (2010), pp. 9198-9203
55 B.L. Steimle, D.K. Bailey, F.M. Smith, et al.Calcium and the Ca-ATPase SPCA1 modulate plasma membrane abundance of ZIP8 and ZIP14 to regulate Mn(II) uptake in brain microvascular endothelial cells J Biol Chem, 298 (8) (2022), Article 102211
56 C.H. George, G.V. Higgs, F.A. LaiRyanodine receptor mutations associated with stress-induced ventricular tachycardia mediate increased calcium release in stimulated cardiomyocytes Circ Res, 93 (6) (2003), pp. 531-540
57 S. Potelle, W. Morelle, E. Dulary, et al.Glycosylation abnormalities in Gdt1p/TMEM165 deficient cells result from a defect in Golgi manganese homeostasis Hum Mol Genet, 25 (8) (2016), pp. 1489-1500
58 A. Carmona, C.E. Zogzas, S. Roudeau, et al.SLC30A10 mutation involved in Parkinsonism results in Manganese accumulation within nanovesicles of the Golgi apparatus ACS Chem Neurosci, 10 (1) (2019), pp. 599-609
59 L. Huang, C.P. Kirschke, Y. Zhang, et al.The ZIP7 gene (Slc39a7) encodes a zinc transporter involved in zinc homeostasis of the Golgi apparatus J Biol Chem, 280 (15) (2005), pp. 15456-15463
60 A. Grubman, G.E. Lidgerwood, C. Duncan, et al.Deregulation of subcellular biometal homeostasis through loss of the metal transporter, Zip7, in a childhood neurodegenerative disorder Acta Neuropathol Commun, 2 (2014), p. 25
61 B.H. Bin, T. Fukada, T. Hosaka, et al.Biochemical characterization of human ZIP13 protein: a homo-dimerized zinc transporter involved in the spondylocheiro dysplastic Ehlers-Danlos syndrome J Biol Chem, 286 (46) (2011), pp. 40255-40265
62 M.L. Kennerson, G.A. Nicholson, S.G. Kaler, et al.Missense mutations in the copper transporter gene ATP7A cause X-linked distal hereditary motor neuropathy Am J Hum Genet, 86 (3) (2010), pp. 343-352
63 N. Bakkar, A. Starr, B.E. Rabichow, et al.The M1311V variant of ATP7A is associated with impaired trafficking and copper homeostasis in models of motor neuron disease Neurobiol Dis, 149 (2021), Article 105228
64 S. Watanabe, Y. Amagai, S. Sannino, et al.Zinc regulates ERp44-dependent protein quality control in the early secretory pathway Nat Commun, 10 (2019), p. 603
65 M.G. Lee, B.H. BinDifferent actions of intracellular zinc transporters ZIP7 and ZIP13 are essential for dermal development Int J Mol Sci, 20 (16) (2019), p. 3941
66 J. van de Leemput, J. Chandran, M.A. Knight, et al.Deletion at ITPR1 underlies ataxia in mice and spinocerebellar ataxia 15 in humans PLoS Genet, 3 (6) (2007), p. e108
67 Y.J. Wang, J. Wang, H.Q. Sun, et al.Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi Cell, 114 (3) (2003), pp. 299-310
68 T. Itoh, N. Fujita, E. Kanno, et al.Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation Mol Biol Cell, 19 (7) (2008), pp. 2916-2925
69 B. Guinea, J.M. Ligos, T. Laín de Lera, et al.Nucleocytoplasmic shuttling of STK16 (PKL12), a Golgi-resident serine/threonine kinase involved in VEGF expression regulation Exp Cell Res, 312 (2) (2006), pp. 135-144
70 C. Fernández-Hernando, M. Fukata, P.N. Bernatchez, et al.Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase J Cell Biol, 174 (3) (2006), pp. 369-377
71 J.G. Donaldson, R.A. Kahn, J. Lippincott-Schwartz, et al.Binding of ARF and beta-COP to Golgi membranes: possible regulation by a trimeric G protein Science, 254 (5035) (1991), pp. 1197-1199
72 J. Chia, G. Goh, V. Racine, et al.RNAi screening reveals a large signaling network controlling the Golgi apparatus in human cells Mol Syst Biol, 8 (2012), p. 629
73 F. Bard, L. Casano, A. Mallabiabarrena, et al.Functional genomics reveals genes involved in protein secretion and Golgi organization Nature, 439 (7076) (2006), pp. 604-607
74 A. Rahman, P. Lőrincz, R. Gohel, et al.GMAP is an Atg8a-interacting protein that regulates Golgi turnover in Drosophila Cell Rep, 39 (9) (2022), Article 110903
75 S. Yadav, M.A. Puthenveedu, A.D. LinstedtGolgin160 recruits the dynein motor to position the Golgi apparatus Dev Cell, 23 (1) (2012), pp. 153-165
76 K. Chabin-Brion, J. Marceiller, F. Perez, et al.The Golgi complex is a microtubule-organizing organelle Mol Biol Cell, 12 (7) (2001), pp. 2047-2060
77 C. Infante, F. Ramos-Morales, C. Fedriani, et al.GMAP-210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein J Cell Biol, 145 (1) (1999), pp. 83-98
78 K.M. Ori-McKenney, L.Y. Jan, Y.N. JanGolgi outposts shape dendrite morphology by functioning as sites of acentrosomal microtubule nucleation in neurons Neuron, 76 (5) (2012), pp. 921-930
79 P.M. Miller, A.W. Folkmann, A.R.R. Maia, et al.Golgi-derived CLASP-dependent microtubules control Golgi organization and polarized trafficking in motile cells Nat Cell Biol, 11 (9) (2009), pp. 1069-1080
80 S. Rivero, J. Cardenas, M. Bornens, et al.Microtubule nucleation at the cis-side of the Golgi apparatus requires AKAP450 and GM130 EMBO J, 28 (8) (2009), pp. 1016-1028
81 Y.K. Choi, P. Liu, S.K. Sze, et al.CDK5RAP2 stimulates microtubule nucleation by the γ-tubulin ring complex J Cell Biol, 191 (6) (2010), pp. 1089-1095
82 Z. Wang, T. Wu, L. Shi, et al.Conserved motif of CDK5RAP2 mediates its localization to centrosomes and the Golgi complex J Biol Chem, 285 (29) (2010), pp. 22658-22665
83 C. Yalgin, S. Ebrahimi, C. Delandre, et al.Centrosomin represses dendrite branching by orienting microtubule nucleation Nat Neurosci, 18 (10) (2015), pp. 1437-1445
84 R. Roubin, C. Acquaviva, V. Chevrier, et al.Myomegalin is necessary for the formation of centrosomal and Golgi-derived microtubules Biol Open, 2 (2) (2013), pp. 238-250
85 A. Efimov, A. Kharitonov, N. Efimova, et al.Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi network Dev Cell, 12 (6) (2007), pp. 917-930
86 J. Wu, C. de Heus, Q. Liu, et al.Molecular pathway of microtubule organization at the Golgi apparatus Dev Cell, 39 (1) (2016), pp. 44-60
87 A. Mukherjee, P.S. Brooks, F. Bernard, et al.Microtubules originate asymmetrically at the somatic Golgi and are guided via Kinesin2 to maintain polarity within neurons Elife, 9 (2020), Article e58943
88 M.M. Nguyen, M.C. Stone, M.M. RollsMicrotubules are organized independently of the centrosome in Drosophila neurons Neural Dev, 6 (2011), p. 38
89 P. Li, L. Li, B. Yu, et al.Doublecortin facilitates the elongation of the somatic Golgi apparatus into proximal dendrites Mol Biol Cell, 32 (5) (2021), pp. 422-434
90 A.C. Horton, B. Rácz, E.E. Monson, et al.Polarized secretory trafficking directs cargo for asymmetric dendrite growth and morphogenesis Neuron, 48 (5) (2005), pp. 757-771
91 B. Castellano, B. Gonzalez, G. PalaciosCytochemical demonstration of TPPase in myelinated fibers in the central and peripheral nervous system of the rat Brain Res, 492 (1–2) (1989), pp. 203-210
92 D.L. Griffith, W. BondareffLocalization of thiamine pyrophosphatase in synaptic vesicles Am J Anat, 136 (4) (1973), pp. 549-556
93 T.T. Merianda, A.C. Lin, J.S.Y. Lam, et al.A functional equivalent of endoplasmic reticulum and Golgi in axons for secretion of locally synthesized proteins Mol Cell Neurosci, 40 (2) (2009), pp. 128-142
94 A.C. Horton, M.D. EhlersDual modes of endoplasmic reticulum-to-Golgi transport in dendrites revealed by live-cell imaging J Neurosci, 23 (15) (2003), pp. 6188-6199
95 V.M. TennysonThe fine structure of the axon and growth cone of the dorsal root neuroblast of the rabbit embryo J Cell Biol, 44 (1) (1970), pp. 62-79
96 M.B. BungeFine structure of nerve fibers and growth cones of isolated sympathetic neurons in culture J Cell Biol, 56 (3) (1973), pp. 713-735
97 M.M. Nguyen, C.J. McCracken, E.S. Milner, et al.γ-Tubulin controls neuronal microtubule polarity independently of Golgi outposts Mol Biol Cell, 25 (13) (2014), pp. 2039-2050
98 B. Ye, Y. Zhang, W. Song, et al.Growing dendrites and axons differ in their reliance on the secretory pathway Cell, 130 (4) (2007), pp. 717-729
99 A.C. Horton, M.D. EhlersSecretory trafficking in neuronal dendrites Nat Cell Biol, 6 (7) (2004), pp. 585-591
100 E.R. Torre, O. StewardProtein synthesis within dendrites: glycosylation of newly synthesized proteins in dendrites of hippocampal neurons in culture J Neurosci, 16 (19) (1996), pp. 5967-5978
101 J.E. Kacharmina, C. Job, P. Crino, et al.Stimulation of glutamate receptor protein synthesis and membrane insertion within isolated neuronal dendrites Proc Natl Acad Sci U S A, 97 (21) (2000), pp. 11545-11550
102 W. Ju, W. Morishita, J. Tsui, et al.Activity-dependent regulation of dendritic synthesis and trafficking of AMPA receptors Nat Neurosci, 7 (3) (2004), pp. 244-253
103 A.B. Bowen, A.M. Bourke, B.G. Hiester, et al.Golgi-independent secretory trafficking through recycling endosomes in neuronal dendrites and spines Elife, 6 (2017), Article e27362
104 C. Hanus, L. Kochen, S. Tom Dieck, et al.Synaptic control of secretory trafficking in dendrites Cell Rep, 7 (6) (2014), pp. 1771-1778
105 M. Mikhaylova, P.P. Reddy, T. Munsch, et al.Calneurons provide a calcium threshold for trans-Golgi network to plasma membrane trafficking Proc Natl Acad Sci U S A, 106 (22) (2009), pp. 9093-9098
106 S. Bera, V. Raghuram, M. Mikhaylova, et al.A plasmid-based expression system to study protein-protein interactions at the Golgi in vivo Anal Biochem, 502 (2016), pp. 50-52
107 M. Mikhaylova, S. Bera, O. Kobler, et al.A dendritic Golgi satellite between ERGIC and retromer Cell Rep, 14 (2) (2016), pp. 189-199
108 G. Quassollo, J. Wojnacki, D.A. Salas, et al.A RhoA signaling pathway regulates dendritic Golgi outpost formation Curr Biol, 25 (8) (2015), pp. 971-982
109 A.P. Govind, O. Jeyifous, T.A. Russell, et al.Activity-dependent Golgi satellite formation in dendrites reshapes the neuronal surface glycoproteome Elife, 10 (2021), Article e68910
110 K.M. Grochowska, M. Andres-Alonso, A. Karpova, et al.The needs of a synapse-How local organelles serve synaptic proteostasis EMBO J, 41 (7) (2022), Article e110057
111 M.A. Puthenveedu, C. Bachert, S. Puri, et al.GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution Nat Cell Biol, 8 (3) (2006), pp. 238-248
112 N. Nakamura, C. Rabouille, R. Watson, et al.Characterization of a cis-Golgi matrix protein, GM130 J Cell Biol, 131 (6 Pt 2) (1995), pp. 1715-1726
113 R.M. Ríos, A. Sanchís, A.M. Tassin, et al.GMAP-210 recruits gamma-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation Cell, 118 (3) (2004), pp. 323-335
114 J.S. Liu, C.R. Schubert, X. Fu, et al.Molecular basis for specific regulation of neuronal kinesin-3 motors by doublecortin family proteins Mol Cell, 47 (5) (2012), pp. 707-721
115 V. des Portes, J.M. Pinard, P. Billuart, et al.A novel CNS gene required for neuronal migration and involved in X-linked subcortical laminar heterotopia and lissencephaly syndrome Cell, 92 (1) (1998), pp. 51-61
116 J.G. Gleeson, K.M. Allen, J.W. Fox, et al.Doublecortin, a brain-specific gene mutated in human X-linked lissencephaly and double cortex syndrome, encodes a putative signaling protein Cell, 92 (1) (1998), pp. 63-72
117 A.S. Tsvetkov, A. Samsonov, A. Akhmanova, et al.Microtubule-binding proteins CLASP1 and CLASP2 interact with actin filaments Cell Motil Cytoskeleton, 64 (7) (2007), pp. 519-530
118 A. Akhmanova, C.C. Hoogenraad, K. Drabek, et al.CLASPs are CLIP-115 and-170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts Cell, 104 (6) (2001), pp. 923-935
119 U. Beffert, G.M. Dillon, J.M. Sullivan, et al.Microtubule plus-end tracking protein CLASP2 regulates neuronal polarity and synaptic function J Neurosci, 32 (40) (2012), pp. 13906-13916
120 A. di Ronza, L. Bajaj, J. Sharma, et al.CLN8 is an endoplasmic reticulum cargo receptor that regulates lysosome biogenesis Nat Cell Biol, 20 (12) (2018), pp. 1370-1377
121 L. Lonka, A. Kyttälä, S. Ranta, et al.The neuronal ceroid lipofuscinosis CLN8 membrane protein is a resident of the endoplasmic reticulum Hum Mol Genet, 9 (11) (2000), pp. 1691-1697
122 D. Jensen, R. SchekmanCOPII-mediated vesicle formation at a glance J Cell Sci, 124 (1) (2011), pp. 1-4
123 E.C. Arakel, B. SchwappachFormation of COPI-coated vesicles at a glance J Cell Sci, 131 (5) (2018), Article jcs209890
124 R. DudenER-to-Golgi transport: COP I and COP II function (review) Mol Membr Biol, 20 (3) (2003), pp. 197-207
125 F. Pesaola, G. Quassollo, A.C. Venier, et al.The neuronal ceroid lipofuscinosis-related protein CLN8 regulates endo-lysosomal dynamics and dendritic morphology Biol Cell, 113 (10) (2021), pp. 419-437
126 R. Passantino, C. Cascio, I. Deidda, et al.Identifying protein partners of CLN8, an ER-resident protein involved in neuronal ceroid lipofuscinosis Biochim Biophys Acta, 1833 (3) (2013), pp. 529-540
127 G. Haase, C. RabouilleGolgi fragmentation in ALS motor neurons. new mechanisms targeting microtubules, tethers, and transport vesicles Front Neurosci, 9 (2015), p. 448
128 D. Sengupta, A.D. LinstedtControl of organelle size: the Golgi complex Annu Rev Cell Dev Biol, 27 (2011), pp. 57-77
129 A. Mukhopadhyay, K. Funato, P.D. StahlRab7 regulates transport from early to late endocytic compartments in Xenopus oocytes J Biol Chem, 272 (20) (1997), pp. 13055-13059
130 M. Stagi, Z.A. Klein, T.J. Gould, et al.Lysosome size, motility and stress response regulated by fronto-temporal dementia modifier TMEM106B Mol Cell Neurosci, 61 (2014), pp. 226-240
131 S. PelletierSCYL pseudokinases in neuronal function and survival Neural Regen Res, 11 (1) (2016), pp. 42-44
132 J.L. Burman, L. Bourbonniere, J. Philie, et al.Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde traffic J Biol Chem, 283 (33) (2008), pp. 22774-22786
133 J.L. Burman, J.N.R. Hamlin, P.S. McPhersonScyl1 regulates Golgi morphology PLoS One, 5 (3) (2010), Article e9537
134 W.M. Schmidt, C. Kraus, H. Höger, et al.Mutation in the Scyl1 gene encoding amino-terminal kinase-like protein causes a recessive form of spinocerebellar neurodegeneration EMBO Rep, 8 (7) (2007), pp. 691-697
135 D. Lenz, P. McClean, A. Kansu, et al.SCYL1 variants cause a syndrome with lowγ-glutamyl-transferase cholestasis, acute liver failure, and neurodegeneration (CALFAN) Genet Med, 20 (10) (2018), pp. 1255-1265
136 J.N.R. Hamlin, L.K. Schroeder, M. Fotouhi, et al.Scyl1 scaffolds class II Arfs to specific subcomplexes of coatomer through the γ-COP appendage domain J Cell Sci, 127 (Pt 7) (2014), pp. 1454-1463
137 G. Amano, S. Matsuzaki, Y. Mori, et al.SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis Mol Biol Cell, 31 (18) (2020), pp. 1963-1973
138 A.C. Wolfes, C. DeanThe diversity of synaptotagmin isoforms Curr Opin Neurobiol, 63 (2020), pp. 198-209
139 O.J. Kwon, H. Gainer, S. Wray, et al.Identification of a novel protein containing two C2 domains selectively expressed in the rat brain and kidney FEBS Lett, 378 (2) (1996), pp. 135-139
140 M.Y. Lee, S.H. Choi, S.L. Shin, et al.Distribution of B/K protein in rat brain Cell Tissue Res, 303 (1) (2001), pp. 47-56
141 K. Sharma, S. Schmitt, C.G. Bergner, et al.Cell type–and brain region–resolved mouse brain proteome Nat Neurosci, 18 (12) (2015), pp. 1819-1831
142 D.A. Ruhl, E. Bomba-Warczak, E.T. Watson, et al.Synaptotagmin 17 controls neurite outgrowth and synaptic physiology via distinct cellular pathways Nat Commun, 10 (1) (2019), p. 3532
143 M. Fukuda, K. MikoshibaThe N-terminal cysteine cluster is essential for membrane targeting of B/K protein Biochem J, 360 (Pt 2) (2001), pp. 441-448
144 C. Dean, F.M. Dunning, H. Liu, et al.Axonal and dendritic synaptotagmin isoforms revealed by a pHluorin-syt functional screen Mol Biol Cell, 23 (9) (2012), pp. 1715-1727
145 Y.S. Jang, M.Y. Lee, S.H. Choi, et al.Expression of B/K protein in the hippocampus of kainate-induced rat seizure model Brain Res, 999 (2) (2004), pp. 203-211
146 N. Muschalik, S. MunroGolgins Curr Biol., 28 (8) (2018), pp. R374-R376
147 N. NakamuraEmerging new roles of GM130, a cis-Golgi matrix protein, in higher order cell functions J Pharmacol Sci, 112 (3) (2010), pp. 255-264
148 M. Lowe, C. Rabouille, N. Nakamura, et al.Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis Cell, 94 (6) (1998), pp. 783-793
149 M. Lowe, N.K. Gonatas, G. WarrenThe mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130 J Cell Biol, 149 (2) (2000), pp. 341-356
150 S. Sundaramoorthy, J.B. Goh, S. Rafee, et al.Mitotic Golgi vesiculation involves mechanisms independent of Ser25 phosphorylation of GM130 Cell Cycle, 9 (15) (2010), pp. 3100-3105
151 C. Liu, M. Mei, Q. Li, et al.Loss of the golgin GM130 causes Golgi disruption, Purkinje neuron loss, and ataxia in mice Proc Natl Acad Sci U S A, 114 (2) (2017), pp. 346-351
152 W. Huang, L. She, X.Y. Chang, et al.Protein kinase LKB1 regulates polarized dendrite formation of adult hippocampal newborn neurons Proc Natl Acad Sci U S A, 111 (1) (2014), pp. 469-474
153 T. Veenendaal, T. Jarvela, A.G. Grieve, et al.GRASP65 controls the cis Golgi integrity in vivo Biol Open, 3 (6) (2014), pp. 431-443
154 Y. Xiang, Y. WangGRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking J Cell Biol, 188 (2) (2010), pp. 237-251
155 J. Shorter, R. Watson, M.E. Giannakou, et al.GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system EMBO J, 18 (18) (1999), pp. 4949-4960
156 E.K. Scott, L. LuoHow do dendrites take their shape? Nat Neurosci, 4 (4) (2001), pp. 359-365
157 X. Wang, J.H. Kim, M. Bazzi, et al.Bimodal control of dendritic and axonal growth by the dual leucine zipper kinase pathway PLoS Biol, 11 (6) (2013), Article e1001572
158 K. Tanabe, S. Kani, T. Shimizu, et al.Atypical protein kinase C regulates primary dendrite specification of cerebellar Purkinje cells by localizing Golgi apparatus J Neurosci, 30 (50) (2010), pp. 16983-16992
159 S.M. Hapak, C.V. Rothlin, S. GhoshPAR3-PAR6-atypical PKC polarity complex proteins in neuronal polarization Cell Mol Life Sci, 75 (15) (2018), pp. 2735-2761
160 S. Rao, G.W. Kirschen, J. Szczurkowska, et al.Repositioning of somatic Golgi apparatus is essential for the dendritic establishment of adult-born hippocampal neurons J Neurosci, 38 (3) (2018), pp. 631-647
161 Y. Gao, F. Wang, B.E. Eisinger, et al.Integrative single-cell transcriptomics reveals molecular networks defining neuronal maturation during postnatal neurogenesis Cerebr Cortex, 27 (3) (2017), pp. 2064-2077
162 K.A. Orlova, W.E. Parker, G.G. Heuer, et al.STRADα deficiency results in aberrant mTORC1 signaling during corticogenesis in humans and mice J Clin Invest, 120 (5) (2010), pp. 1591-1602
163 C. Preisinger, B. Short, V. De Corte, et al.YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta J Cell Biol, 164 (7) (2004), pp. 1009-1020
164 G. D'Arcangelo, G.G. Miao, S.C. Chen, et al.A protein related to extracellular matrix proteins deleted in the mouse mutant reeler Nature, 374 (6524) (1995), pp. 719-723
165 S. Hirotsune, T. Takahara, N. Sasaki, et al.The reeler gene encodes a protein with an EGF-like motif expressed by pioneer neurons Nat Genet, 10 (1) (1995), pp. 77-83
166 M. Ogawa, T. Miyata, K. Nakajimat, et al.The reeler gene-associated antigen on Cajal-retzius neurons is a crucial molecule for laminar organization of cortical neurons Neuron, 14 (5) (1995), pp. 899-912
167 E. Ampuero, N. Jury, S. Härtel, et al.Interfering of the Reelin/ApoER2/PSD95 signaling axis reactivates dendritogenesis of mature hippocampal neurons J Cell Physiol, 232 (5) (2017), pp. 1187-1199
168 R.S. O'Dell, D.A. Cameron, W.R. Zipfel, et al.Reelin prevents apical neurite retraction during terminal translocation and dendrite initiation J Neurosci, 35 (30) (2015), pp. 10659-10674
169 T. Kohno, K. Ishii, Y. Hirota, et al.Reelin-Nrp1 interaction regulates neocortical dendrite development in a context-specific manner J Neurosci, 40 (43) (2020), pp. 8248-8261
170 M.I.K. Hamad, P. Petrova, S. Daoud, et al.Reelin restricts dendritic growth of interneurons in the neocortex Development, 148 (17) (2021), Article dev199718
171 S. Niu, A. Renfro, C.C. Quattrocchi, et al.Reelin promotes hippocampal dendrite development through the VLDLR/ApoER2-Dab1 pathway Neuron, 41 (1) (2004), pp. 71-84
172 D.S. Rice, S. Nusinowitz, A.M. Azimi, et al.The Reelin pathway modulates the structure and function of retinal synaptic circuitry Neuron, 31 (6) (2001), pp. 929-941
173 B.W. Howell, R. Hawkes, P. Soriano, et al.Neuronal position in the developing brain is regulated by mouse disabled-1 Nature, 389 (6652) (1997), pp. 733-737
174 D.S. Rice, M. Sheldon, G. D'Arcangelo, et al.Disabled-1 acts downstream of Reelin in a signaling pathway that controls laminar organization in the mammalian brain Development, 125 (18) (1998), pp. 3719-3729
175 B.W. Howell, T.M. Herrick, J.D. Hildebrand, et al.Dab1 tyrosine phosphorylation sites relay positional signals during mouse brain development Curr Biol, 10 (15) (2000), pp. 877-885
176 R.S. O'Dell, C.J.M. Ustine, D.A. Cameron, et al.Layer 6 cortical neurons require Reelin-Dab1 signaling for cellular orientation, Golgi deployment, and directed neurite growth into the marginal zone Neural Dev, 7 (2012), p. 25
177 T. Matsuki, R.T. Matthews, J.A. Cooper, et al.Reelin and Stk25 have opposing roles in neuronal polarization and dendritic Golgi deployment Cell, 143 (5) (2010), pp. 826-836
178 G.M. Dillon, W.A. Tyler, K.C. Omuro, et al.CLASP2 links Reelin to the cytoskeleton during neocortical development Neuron, 93 (6) (2017), pp. 1344-1358 e5
179 M. Yanagida, R. Miyoshi, R. Toyokuni, et al.Dynamics of the leading process, nucleus, and Golgi apparatus of migrating cortical interneurons in living mouse embryos Proc Natl Acad Sci U S A, 109 (41) (2012), pp. 16737-16742
180 A. Sakakibara, R. Ando, T. Sapir, et al.Microtubule dynamics in neuronal morphogenesis Open Biol, 3 (7) (2013), Article 130061
181 S. Etienne-Manneville, A. HallRho GTPases in cell biology Nature, 420 (6916) (2002), pp. 629-635
182 N. Mosaddeghzadeh, M.R. AhmadianThe RHO family GTPases: mechanisms of regulation and signaling Cells, 10 (7) (2021), p. 1831
183 M. Auer, B. Hausott, L. KlimaschewskiRho GTPases as regulators of morphological neuroplasticity Ann Anat, 193 (4) (2011), pp. 259-266
184 A. Debant, C. Serra-Pagès, K. Seipel, et al.The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains Proc Natl Acad Sci U S A, 93 (11) (1996), pp. 5466-5471
185 T. Tao, J. Sun, Y. Peng, et al.Golgi-resident TRIO regulates membrane trafficking during neurite outgrowth J Biol Chem, 294 (28) (2019), pp. 10954-10968
186 Y.J. Peng, W.Q. He, J. Tang, et al.Trio is a key guanine nucleotide exchange factor coordinating regulation of the migration and morphogenesis of granule cells in the developing cerebellum J Biol Chem, 285 (32) (2010), pp. 24834-24844
187 M. Meseke, G. Rosenberger, E. FörsterReelin and the Cdc42/Rac1 guanine nucleotide exchange factor αPIX/Arhgef6 promote dendritic Golgi translocation in hippocampal neurons Eur J Neurosci, 37 (9) (2013), pp. 1404-1412
188 E.H. Hong, J.Y. Kim, J.H. Kim, et al.BIG2-ARF1-RhoA-mDia1 signaling regulates dendritic Golgi polarization in hippocampal neurons Mol Neurobiol, 55 (10) (2018), pp. 7701-7716
189 N. Watanabe, T. Kato, A. Fujita, et al.Cooperation between mDia1 and ROCK in Rho-induced actin reorganization Nat Cell Biol, 1 (3) (1999), pp. 136-143
190 T. Ishizaki, Y. Morishima, M. Okamoto, et al.Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1 Nat Cell Biol, 3 (1) (2001), pp. 8-14
191 W.B. Grueber, L.Y. Jan, Y.N. JanTiling of the Drosophila epidermis by multidendritic sensory neurons Development, 129 (12) (2002), pp. 2867-2878
192 O. Papoulas, T.S. Hays, J.C. SissonThe golgin Lava lamp mediates dynein-based Golgi movements during Drosophila cellularization Nat Cell Biol, 7 (6) (2005), pp. 612-618
193 O. Jeyifous, C.L. Waites, C.G. Specht, et al.SAP97 and CASK mediate sorting of NMDA receptors through a previously unknown secretory pathway Nat Neurosci, 12 (8) (2009), pp. 1011-1019
194 S.Z. Yang, J. WildongerGolgi outposts locally regulate microtubule orientation in neurons but are not required for the overall polarity of the dendritic cytoskeleton Genetics, 215 (2) (2020), pp. 435-447
195 K. Blochlinger, R. Bodmer, L.Y. Jan, et al.Patterns of expression of cut, a protein required for external sensory organ development in wild-type and cut mutant Drosophila embryos Genes Dev, 4 (8) (1990), pp. 1322-1331
196 S. Jinushi-Nakao, R. Arvind, R. Amikura, et al.Knot/Collier and cut control different aspects of dendrite cytoskeleton and synergize to define final Arbor shape Neuron, 56 (6) (2007), pp. 963-978
197 S.C. Iyer, E.P. Ramachandran Iyer, R. Meduri, et al.Cut, via CrebA, transcriptionally regulates the COPII secretory pathway to direct dendrite development in Drosophila J Cell Sci, 126 (20) (2013), pp. 4732-4745
198 M. Martinez-Campos, R. Basto, J. Baker, et al.The Drosophila pericentrin-like protein is essential for cilia/flagella function, but appears to be dispensable for mitosis J Cell Biol, 165 (5) (2004), pp. 673-683
199 T.L. Megraw, S. Kilaru, F.R. Turner, et al.The centrosome is a dynamic structure that ejects PCM flares J Cell Sci, 115 (Pt 23) (2002), pp. 4707-4718
200 D. Satoh, D. Sato, T. Tsuyama, et al.Spatial control of branching within dendritic arbors by dynein-dependent transport of Rab5-endosomes Nat Cell Biol, 10 (10) (2008), pp. 1164-1171
201 Y. Zheng, J. Wildonger, B. Ye, et al.Dynein is required for polarized dendritic transport and uniform microtubule orientation in axons Nat Cell Biol, 10 (10) (2008), pp. 1172-1180
202 M.T. Kelliher, Y. Yue, A. Ng, et al.Autoinhibition of kinesin-1 is essential to the dendrite-specific localization of Golgi outposts J Cell Biol, 217 (7) (2018), pp. 2531-2547
203 D. Mori, M. Yamada, Y. Mimori-Kiyosue, et al.An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation by modulation of microtubule dynamics Nat Cell Biol, 11 (9) (2009), pp. 1057-1068
204 A.L. Arthur, S.Z. Yang, A.M. Abellaneda, et al.Dendrite arborization requires the dynein cofactor NudE J Cell Sci, 128 (11) (2015), pp. 2191-2201
205 D. Jaarsma, C.C. HoogenraadCytoplasmic dynein and its regulatory proteins in Golgi pathology in nervous system disorders Front Neurosci, 9 (2015), p. 397
206 H.Y.K. Kaan, D.D. Hackney, F. KozielskiThe structure of the kinesin-1 motor-tail complex reveals the mechanism of autoinhibition Science, 333 (6044) (2011), pp. 883-885
207 V.A. Kulkarni, B.L. FiresteinThe dendritic tree and brain disorders Mol Cell Neurosci, 50 (1) (2012), pp. 10-20
208 C.H. Lin, H. Li, Y.N. Lee, et al.Lrrk regulates the dynamic profile of dendritic Golgi outposts through the golgin Lava lamp J Cell Biol, 210 (3) (2015), pp. 471-483
209 C.G. Chung, M.J. Kwon, K.H. Jeon, et al.Golgi outpost synthesis impaired by toxic polyglutamine proteins contributes to dendritic pathology in neurons Cell Rep, 20 (2) (2017), pp. 356-369
210 J.H. Park, C.G. Chung, J. Seo, et al.C9orf72-associated arginine-rich dipeptide repeat proteins reduce the number of Golgi outposts and dendritic branches in Drosophila neurons Mol Cell, 43 (9) (2020), pp. 821-830
211 Q. Du, J. Chang, G. Cheng, et al.Sunday driver mediates multi-compartment Golgi outposts defects induced by amyloid precursor protein Front Neurosci, 15 (2021), Article 673684
212 T. De Wit, V. Baekelandt, E. LobbestaelLRRK2 phosphorylation: behind the scenes Neuroscientist, 24 (5) (2018), pp. 486-500
213 E. Tolosa, M. Vila, C. Klein, et al.LRRK2 in Parkinson disease: challenges of clinical trials Nat Rev Neurol, 16 (2) (2020), pp. 97-107
214 D.G. Healy, M. Falchi, S.S. O'Sullivan, et al.Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study Lancet Neurol, 7 (7) (2008), pp. 583-590
215 K. Stafa, A. Trancikova, P.J. Webber, et al.GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1 PLoS Genet, 8 (2) (2012), Article e1002526
216 F. Sambataro, M. PennutoCell-autonomous and non-cell-autonomous toxicity in polyglutamine diseases Prog Neurobiol, 97 (2) (2012), pp. 152-172
217 S.B. Lee, J.A. Bagley, H.Y. Lee, et al.Pathogenic polyglutamine proteins cause dendrite defects associated with specific actin cytoskeletal alterations in Drosophila Proc Natl Acad Sci U S A, 108 (40) (2011), pp. 16795-16800
218 J.P. Taylor, R.H. Brown Jr., D.W. ClevelandDecoding ALS: from genes to mechanism Nature, 539 (7628) (2016), pp. 197-206
219 T. Takeda, T. Uchihara, Y. Nakayama, et al.Dendritic retraction, but not atrophy, is consistent in amyotrophic lateral sclerosis-comparison between Onuf's neurons and other sacral motor neurons Acta Neuropathol Commun, 2 (2014), p. 11
220 M. Tibshirani, B. Zhao, B.J. Gentil, et al.Dysregulation of chromatin remodelling complexes in amyotrophic lateral sclerosis Hum Mol Genet, 26 (21) (2017), pp. 4142-4152
221 J.J. Herzog, M. Deshpande, L. Shapiro, et al.TDP-43 misexpression causes defects in dendritic growth Sci Rep, 7 (1) (2017), Article 15656
222 I. FerrerNeurons and their dendrites in frontotemporal dementia Dement Geriatr Cognit Disord, 10 (Suppl 1) (1999), pp. 55-60
223 M. DeJesus-Hernandez, I.R. Mackenzie, B.F. Boeve, et al.Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS Neuron, 72 (2) (2011), pp. 245-256
224 A.E. Renton, E. Majounie, A. Waite, et al.A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD Neuron, 72 (2) (2011), pp. 257-268
225 B.D. Freibaum, J.P. TaylorThe role of dipeptide repeats in C9ORF72-related ALS-FTD Front Mol Neurosci, 10 (2017), p. 35
226 A. Stieber, Z. Mourelatos, N.K. GonatasIn Alzheimer's disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic Am J Pathol, 148 (2) (1996), pp. 415-426
227 S.J. Baloyannis, S.L. Manolidis, L.S. ManolidisSynaptic alterations in the vestibulocerebellar system in Alzheimer's disease: a Golgi and electron microscope study Acta Otolaryngol, 120 (2) (2000), pp. 247-250
228 T.M. Maguire, K.C. BreenA decrease in neural sialyltransferase activity in Alzheimer's disease Dementia, 6 (4) (1995), pp. 185-190
229 A. Halim, G. Brinkmalm, U. Rüetschi, et al.Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid Proc Natl Acad Sci U S A, 108 (29) (2011), pp. 11848-11853
230 C.J. Fontaine, A.R. Patten, H.M. Sickmann, et al.Effects of pre-natal alcohol exposure on hippocampal synaptic plasticity: sex, age and methodological considerations Neurosci Biobehav Rev, 64 (2016), pp. 12-34
231 H.M. Hwang, R.Y. Ku, K. Hashimoto-ToriiPrenatal environment that affects neuronal migration Front Cell Dev Biol, 7 (2019), p. 138
232 D. Wang, B.W. Howell, E.C. OlsonMaternal ethanol exposure acutely elevates src family kinase activity in the fetal cortex Mol Neurobiol, 58 (10) (2021), pp. 5210-5223
233 J. Lee, V. Naik, M. Orzabal, et al.Morphological alteration in rat hippocampal neuronal dendrites following chronic binge prenatal alcohol exposure Brain Res, 1768 (2021), Article 147587
234 T.A. Powrozek, E.C. OlsonEthanol-induced disruption of Golgi apparatus morphology, primary neurite number and cellular orientation in developing cortical neurons Alcohol, 46 (7) (2012), pp. 619-627
235 C.W. Bird, F.T. Candelaria-Cook, C.M. Magcalas, et al.Moderate prenatal alcohol exposure enhances GluN2B containing NMDA receptor binding and ifenprodil sensitivity in rat agranular insular cortex PLoS One, 10 (3) (2015), Article e0118721
236 M.L. Brady, M.R. Diaz, A. Iuso, et al.Moderate prenatal alcohol exposure reduces plasticity and alters NMDA receptor subunit composition in the dentate gyrus J Neurosci, 33 (3) (2013), pp. 1062-1067
237 Y. Honse, K.M. Nixon, M.D. Browning, et al.Cell surface expression of NR1 splice variants and NR2 subunits is modified by prenatal ethanol exposure Neuroscience, 122 (3) (2003), pp. 689-698
238 D.A. Thayer, Y.N. Jan, L.Y. JanIncreased neuronal activity fragments the Golgi complex Proc Natl Acad Sci U S A, 110 (4) (2013), pp. 1482-1487
239 Q. Wang, Y. Wang, F. YuYif1 associates with Yip1 on Golgi and regulates dendrite pruning in sensory neurons during Drosophila metamorphosis Development, 145 (12) (2018), p. dev164475
240 Q. He, H. Liu, S. Deng, et al.The Golgi apparatus may be a potential therapeutic target for apoptosis-related neurological diseases Front Cell Dev Biol, 8 (2020), p. 830
241 M.O. Caracci, L.M. Fuentealba, M.P. MarzoloGolgi complex dynamics and its implication in prevalent neurological disorders Front Cell Dev Biol, 7 (2019), p. 75
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