The Cdc48 Protein and Its Cofactor Vms1 Are Involved in Cdc13 Protein Degradation

被引:13
作者
Baek, Guem Hee [1 ]
Cheng, Haili [1 ]
Kim, Ikjin [1 ]
Rao, Hai [1 ]
机构
[1] Univ Texas Hlth Sci Ctr San Antonio, Inst Biotechnol, Dept Mol Med, San Antonio, TX 78245 USA
基金
美国国家卫生研究院;
关键词
SACCHAROMYCES-CEREVISIAE; UBIQUITIN LIGASE; COMPLEXES; YEAST; UFD2; TURNOVER; ATPASE; SYSTEM;
D O I
10.1074/jbc.M112.351825
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
Vms1 is a newly identified Cdc48-binding protein. The biological function of Vms1 remains obscure. Here, we show that both Cdc48 and Vms1, but not Cdc48 cofactors Ufd1 and Ufd2, are crucial for the degradation of Cdc13, a telomere regulator. Interestingly, both autophagy and the proteasome are involved in Cdc13 turnover. Toxicity associated with accumulation of large amounts of Cdc13 in vms1 Delta or autophagy mutants underscores the significance of the proteolytic regulation of Cdc13. Because few ubiquitylated yeast proteins are known to be degraded by autophagy under non-stress conditions, the identification of Cdc13 as a target of autophagy provides a valuable tool to unravel the mechanism of autophagy-mediated selective protein degradation.
引用
收藏
页码:26788 / 26795
页数:8
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