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Budding yeast Dsk2 protein forms a homodimer via its C-terminal UBA domain

Lookup NU author(s): Professor Jane Endicott

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Abstract

Budding yeast Dsk2 is a family of UbL-UBA proteins that can interact with both polyubiquitin and the proteasome, and is thereby thought to function as a shuttle protein in the ubicluitin-proteasome pathway. Here we show that Dsk2 can homodimerize via its C-terminal UBA domain in the absence of ubiquitin. Dsk2 mutants defective in the UBA domain do not dimerize and do not bind polyubiquitin. The expression of Dsk2 UBA mutants fails to restore the growth defect caused by DSK2 disruption although that of wild-type Dsk2 can restore the defect. These results suggest that Dsk2 homodimerization via the UBA domain plays a role in regulating polyubiquitin binding in the ubiquitin-proteasome pathway. (c) 2005 Elsevier Inc. All rights reserved.


Publication metadata

Author(s): Sasaki T, Funakoshi M, Endicott JA, Kobayashi H

Publication type: Article

Publication status: Published

Journal: Biochemical and Biophysical Research Communications

Year: 2005

Volume: 336

Issue: 2

Pages: 530-535

ISSN (print): 0006-291X

ISSN (electronic): 1090-2104

Publisher: Academic Press

URL: http://dx.doi.org/10.1016/j.bbrc.2005.08.126

DOI: 10.1016/j.bbrc.2005.08.126

PubMed id: 16140271


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