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UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1
- Authors
- Hong, Sunghoi; Lee, Soyeon; Cho, Ssang-Goo; Kang, Seongman
- Issue Date
- 27-Jun-2008
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- ataxin-1; ubiquitination; UbcH6; AXH domain
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.371, no.2, pp.256 - 260
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 371
- Number
- 2
- Start Page
- 256
- End Page
- 260
- ISSN
- 0006-291X
- Abstract
- UbcH6 is a member of an evolutionally conserved subfamily of E2 ubiquitin-conjugating enzymes. In this study, we report that UbcH6 interacts with and ubiquitinates ataxin-1, the spinocerebellar ataxia type 1 gene product. UbcH6 was identified as an ataxin-1-interacting protein using a yeast two-hybrid screen. UbcH6 co-immunoprecipitates and co-localizes with the ataxin-1 protein in the nucleus. Our binding assays showed that ataxin-1 interacts with UbcH6 through its AXH domain. Interestingly, UbcH6 could ubiquitinate ataxin-1 in the absence of an E3 ligase. The expression level of UbcH6 regulated the rate of ataxin-1 degradation. This study demonstrates that UbcH6 and ataxin-1 are E2-substrate cognate pairs in the ubiquitin-proteasome system. (C) 2008 Elsevier Inc. All rights reserved.
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Related Researcher
- KANG, Seong Man
- Department of Life Sciences