Ubiquitination status does not affect Vps34 degradation

Jing Tang; Fei Sun; Xiao-Juan Deng; Yuan-Lin Ma; Kun-Yi Li; Ying Tang; Guo-Jun Chen

doi:10.1016/j.gendis.2019.05.003

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Ubiquitination status does not affect Vps34 degradation

Full-length article | 更新时间：2022-06-24

- Ubiquitination status does not affect Vps34 degradation
- Ubiquitination status does not affect Vps34 degradation
- Genes & Diseases 2020年7卷第3期
- 作者机构：
  
  1. Department of Neurology, The First Affiliated Hospital of Chongqing Medical University, Chongqing Key Laboratory of Neurology, 1 Youyi Road,Chongqing,China,400016
  2. Department of Physiology, Wayne State University School of Medicine,MI,Detroit,USA,48201
- 作者简介：
- 基金信息：
- DOI：10.1016/j.gendis.2019.05.003
  中图分类号：
- 纸质出版日期：2020，
  
  网络出版日期：2020-9-1，
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Jing Tang, Fei Sun, Xiao-Juan Deng, 等. Ubiquitination status does not affect Vps34 degradation[J]. Genes & Diseases, 2020,7(3).

Jing Tang, Fei Sun, Xiao-Juan Deng, et al. Ubiquitination status does not affect Vps34 degradation[J]. Genes & Diseases, 2020,7(3).
Jing Tang, Fei Sun, Xiao-Juan Deng, 等. Ubiquitination status does not affect Vps34 degradation[J]. Genes & Diseases, 2020,7(3). DOI： 10.1016/j.gendis.2019.05.003.

Jing Tang, Fei Sun, Xiao-Juan Deng, et al. Ubiquitination status does not affect Vps34 degradation[J]. Genes & Diseases, 2020,7(3). DOI： 10.1016/j.gendis.2019.05.003.

摘要

Abstract

Vps34 (vacuolar protein-sorting 34) plays important role in autophagy and endosomal trafficking. These processes are closely associated protein ubiquitination and degradation. We have hypothesized that Vps34 ubiquitination status would also control its degradation. Here

we report that our results did not support this assumption. In cells transiently transfected with ubiquitin (UB) constructs contained different lysine residues (Ks)

Vps34 ubiquitination could occur regardless of the presence of any Ks in UB. However

Vps34 protein levels were not significantly altered in cells transiently transfected with these UB mutants. We further found that Vps34 protein was altered by pharmacological manipulation of E2/E3 activity; yet this effect was not significantly affected by UB overexpression. In vivo experiments revealed that in APP/PS1 mice

an animal model of Alzheimer's disease (AD)

although ubiquitination of Vps34 was significantly reduced

Vps34 protein levels remained unchanged. Vps34 indeed was subjected to proteasomal or lysosomal degradation

as prolonged treatment of proteasomal inhibitor MG132 or lysosomal inhibitor chloroquine elevated Vps34 protein levels. We conclude that unlike most of other proteins

Vps34 ubiquitination is not closely associated with its degradation.

关键词

Keywords

Alzheimer's diseaseDegradationUbiquitinationUPSVPS34

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