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

Sunghoi Hong; Soyeon Lee; Ssang Goo Cho; Seongman Kang

doi:10.1016/j.bbrc.2008.04.066

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

Sunghoi Hong, Soyeon Lee, Ssang Goo Cho, Seongman Kang

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

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.

Original language	English
Pages (from-to)	256-260
Number of pages	5
Journal	Biochemical and biophysical research communications
Volume	371
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2008.04.066
Publication status	Published - 2008 Jun 27

Bibliographical note

Funding Information:
This work was supported by the Korea Research Foundation Grant funded by the Korean Government (MOEHRD) (KRF-2005-C00350) and by a grant of Ministry of Health and Welfare (A06-00043398).

Keywords

AXH domain
Ataxin-1
UbcH6
Ubiquitination

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2008.04.066

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title = "UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1",

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.",

keywords = "AXH domain, Ataxin-1, UbcH6, Ubiquitination",

author = "Sunghoi Hong and Soyeon Lee and Cho, {Ssang Goo} and Seongman Kang",

note = "Funding Information: This work was supported by the Korea Research Foundation Grant funded by the Korean Government (MOEHRD) (KRF-2005-C00350) and by a grant of Ministry of Health and Welfare (A06-00043398).",

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AU - Cho, Ssang Goo

AU - Kang, Seongman

N1 - Funding Information: This work was supported by the Korea Research Foundation Grant funded by the Korean Government (MOEHRD) (KRF-2005-C00350) and by a grant of Ministry of Health and Welfare (A06-00043398).

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N2 - 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.

AB - 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.

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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