@article{oai:nagasaki-u.repo.nii.ac.jp:00013387,
 author = {Guo, Chao-Wan and Liu, Ge and Xiong, Sheng and Ge, Feng and Fuse, Takayuki and Wang, Yi-Fei and Kitazato, Kaio},
 issue = {9},
 journal = {FEBS Letters},
 month = {May},
 note = {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., FEBS Letters, 585(6), pp.1350-1356; 2011},
 pages = {1350--1356},
 title = {The C-terminus of MIP-T3 protein is required for ubiquitin-proteasome-mediated degradation in human cells.},
 volume = {585},
 year = {2011}
}