GRAIL: a unique mediator of CD4 T-lymphocyte unresponsiveness

被引：51

作者：

Whiting, Chan C. ^{[1
]}

Su, Leon L. ^{[1
]}

Lin, Jack T. ^{[1
]}

Fathman, C. Garrison ^{[1
]}

机构：

[1] Stanford Univ, Dept Med, Div Rheumatol & Immunol, Stanford, CA 94305 USA

来源：

FEBS JOURNAL | 2011年 / 278卷 / 01期

关键词：

anergy; cell cycle; de-ubiquitinating enzymes (DUBs); E3; GRAIL; RNF128; T-cell unresponsiveness; tolerance; ubiquitination; ubiquitin-protein ligase; E3 UBIQUITIN LIGASE; CELL TOLERANCE; CUTTING EDGE; CBL-B; UP-REGULATION; ANERGY; INDUCTION; ACTIVATION; MECHANISMS; CD151;

D O I：

10.1111/j.1742-4658.2010.07922.x

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：

GRAIL (gene related to anergy in lymphocytes, also known as RNF128), an ubiquitin-protein ligase (E3), utilizes a unique single transmembrane protein with a split-function motif, and is an important gatekeeper of T-cell unresponsiveness. Although it may play a role in other CD4 T-cell functions including activation, survival and differentiation, GRAIL is most well characterized as a negative regulator of T-cell receptor responsiveness and cytokine production. Here, we review the recent literature on this remarkable E3 in the regulation of human and mouse CD4 T-cell unresponsiveness.

引用

页码：47 / 58

页数：12

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