Ataxin-10 interacts with O-GlcNAc transferase OGT in pancreatic β cells

被引:18
作者
Andrali, SS
März, P
Özcan, S
机构
[1] Univ Kentucky, Coll Med, Dept Mol & Cellular Biochem, Lexington, KY 40536 USA
[2] Univ Basel, Inst Physiol, CH-4051 Basel, Switzerland
关键词
MIN6; beta cells; SCA10; OGT; glucose; diabetes; ataxia; O-GlcNAc; ataxin-10;
D O I
10.1016/j.bbrc.2005.09.026
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Several nuclear and cytoplasmic proteins in metazoans are modified by O-linked N-acetylglucosamine (O-GlcNAc). This modification is dynamic and reversible similar to phosphorylation and is catalyzed by the O-linked GlcNAc transferase (OGT), Hyperglycemia has been shown to increase O-GlcNAc levels in pancreatic beta cells, which appears to interfere with beta-cell function. To obtain a better understanding of the role of O-linked GlcNAc modification in beta cells, we have isolated OGT interacting proteins from a cDNA library made from the mouse insulinoma MIN6 cell line. We describe here the identification of Ataxin-10, encoded by the SCA10 (spinocerebellar ataxia type 10) gene as an OGT interacting protein. Mutations in the SCA10 gene cause progressive cerebellar ataxias and seizures. We demonstrate that SCA10 interacts with OGT in vivo and is modified by O-linked glycosylation in MIN6 cells, suggesting a novel role for the Ataxin-10 protein in pancreatic beta cells. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:149 / 153
页数:5
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