The Cdc48 protein and its cofactor Vms1 are involved in Cdc13 protein degradation

Guem Hee Baek, Haili Cheng, Ikjin Kim, Hai Rao

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)26788-26795
Number of pages8
JournalJournal of Biological Chemistry
Volume287
Issue number32
DOIs
StatePublished - Aug 3 2012
Externally publishedYes

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Autophagy
Proteolysis
Degradation
Fungal Proteins
Proteasome Endopeptidase Complex
Toxicity
Carrier Proteins
Proteins
Telomere

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

The Cdc48 protein and its cofactor Vms1 are involved in Cdc13 protein degradation. / Baek, Guem Hee; Cheng, Haili; Kim, Ikjin; Rao, Hai.

In: Journal of Biological Chemistry, Vol. 287, No. 32, 03.08.2012, p. 26788-26795.

Research output: Contribution to journalArticle

Baek, Guem Hee ; Cheng, Haili ; Kim, Ikjin ; Rao, Hai. / The Cdc48 protein and its cofactor Vms1 are involved in Cdc13 protein degradation. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 32. pp. 26788-26795.
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