UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1

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초록

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.

키워드

ataxin-1; ubiquitination; UbcH6; AXH domain; RING-FINGER PROTEINS; CONJUGATING ENZYME; LIGASE ACTIVITY; DEGRADATION; PATHWAY; DISEASE; CLONING; REPEAT; TYPE-1; E6-AP
제목
UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1
저자
Hong, Sunghoi; Lee, Soyeon; Cho, Ssang-Goo; Kang, Seongman
DOI
10.1016/j.bbrc.2008.04.066
발행일
2008-06
유형
Article
저널명
Biochemical and Biophysical Research Communications
권
371
호
2
페이지
256 ~ 260