The C-terminus of MIP-T3 protein is required for ubiquitin-proteasome-mediated degradation in human cells

被引：4

作者：

Guo, Chao-Wan ^{[1
]}

Liu, Ge ^{[1
]}

Xiong, Sheng ^{[1
,2
]}

Ge, Feng ^{[1
]}

Fuse, Takayuki ^{[1
,3
]}

Wang, Yi-Fei ^{[2
]}

Kitazato, Kaio ^{[1
]}

机构：

[1] Nagasaki Univ, Grad Sch Biomed Sci, Dept Mol Microbiol & Immunol, Div Mol Pharmacol Infect Agents, Nagasaki 8528521, Japan

[2] Jinan Univ, Natl Engn Res Ctr Genet Med, Guangdong Prov Key Lab Bioengn Med, Biomed R&D Ctr, Guangzhou, Guangdong, Peoples R China

[3] Nagasaki Univ, Grad Sch Biomed Sci, Dept Mol Microbiol & Immunol, Div Cellular & Mol Biol, Nagasaki 8528521, Japan

来源：

FEBS LETTERS | 2011年 / 585卷 / 09期

基金：

日本学术振兴会;

关键词：

MIP-T3; Intraflagellar transport; Polyubiquitination; Proteasome; Protein ability; INTRAFLAGELLAR TRANSPORT; CILIA; AUTOPHAGY;

D O I：

10.1016/j.febslet.2011.04.015

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The intraflagellar transport (IFT) complex is essential for the formation and functional maintenance of eukaryotic cilia which play a vital role in development and tissue homeostasis. However, the biochemical characteristics and precise functions of IFT proteins remain unknown. Here, we report that MIP-T3, a human microtubule-interacting protein recently identified as a novel conserved component of the IFT complex, is an easily degradable protein in human cell lines. Protein degradation is mediated by the ubiquitin-proteasome system, and the C-terminus is required for ubiquitination and proteasome-mediated degradation of MIP-T3 protein. This study provides the first evidence for regulation of IFT protein stability. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1350 / 1356

页数：7

共 20 条

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