TY - JOUR
T1 - The Cdc48 protein and its cofactor Vms1 are involved in Cdc13 protein degradation
AU - Baek, Guem Hee
AU - Cheng, Haili
AU - Kim, Ikjin
AU - Rao, Hai
PY - 2012/8/3
Y1 - 2012/8/3
N2 - 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 vms1Δ 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.
AB - 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 vms1Δ 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.
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U2 - 10.1074/jbc.M112.351825
DO - 10.1074/jbc.M112.351825
M3 - Article
C2 - 22718752
AN - SCOPUS:84864565210
SN - 0021-9258
VL - 287
SP - 26788
EP - 26795
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 32
ER -