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The C‐terminus of MIP‐T3 protein is required for ubiquitin–proteasome‐mediated degradation in human cells
Author(s) -
Guo Chao-Wan,
Liu Ge,
Xiong Sheng,
Ge Feng,
Fuse Takayuki,
Wang Yi-Fei,
Kitazato Kaio
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.04.015
Subject(s) - proteasome , intraflagellar transport , ubiquitin , microbiology and biotechnology , protein degradation , cilium , chemistry , protein aggregation , microtubule , biology , biochemistry , flagellum , gene
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.