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ID 46920
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Author
Sekiguchi, Takeshi
Sasaki, Toru
Funakoshi, Minoru
Ishii, Takashi
Saitoh, Yoh-hei
Kaneko, Shu-ichi
Abstract
Ubiquitin-like (UBL)-ubiquitin-associated (UBA) proteins, including Dsk2 and Rad23, act as delivery factors that target polyubiquitinated substrates to the proteasome. We report here that the Dsk2 UBL domain is ubiquitinated in yeast cells and that Dsk2 ubiquitination of the UBL domain is involved in Dsk2 stability, depending on the Dsk2 UBA domain. Also, Dsk2 lacking ubiquitin chains impaired ubiquitin-dependent protein degradation and decreased the interaction of Dsk2 with polyubiquitinated proteins in cells. Moreover, Dsk2 ubiquitination affected ability to restore the temperature-sensitive growth defect of dsk2 Delta. These results indicate that ubiquitination in the UBL domain of Dsk2 has in vivo functions in the ubiquitin-proteasome pathway in yeast.
Keywords
UBL–UBA protein
Dsk2
UBL domain
UBA domain
Ubiquitin
Proteasome
Published Date
2011-08-05
Publication Title
Biochemical and Biophysical Research Communications
Volume
volume411
Issue
issue3
Publisher
Academic Press Inc Elsevier Science
Start Page
555
End Page
561
ISSN
0006-291X
NCID
AA00564395
Content Type
Journal Article
language
英語
Copyright Holders
© 2011 Elsevier Inc. All rights reserved.
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Refereed
True
DOI
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Web of Sience KeyUT