LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation

被引：748

作者：

Zhang, WG ^{[1
]}

Trible, RP ^{[1
]}

Samelson, LE ^{[1
]}

机构：

[1] National Institute Child Health & Human Dev, Cell Biol & Metab Branch, Sect Lymphocyte Signaling, NIH, Bethesda, MD 20892 USA

来源：

IMMUNITY | 1998年 / 9卷 / 02期

关键词：

D O I：

10.1016/S1074-7613(00)80606-8

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

The linker molecule LAT is a critical substrate of the tyrosine kinases activated upon TCR engagement. Phosphorylated LAT binds Grb2, PLC-gamma 1, and other signaling molecules. We demonstrate that human LAT is palmitoylated and that palmitoylated LAT predominantly localizes into glycolipid-enriched microdomains (GEMs). Although the LAT transmembrane domain is sufficient for membrane localization, palmitoylation at C26 and C29 is essential for efficient partitioning into GEMs. LAT palmitoylation is necessary for its tyrosine phosphorylation. After T cell activation, most tyrosine-phosphorylated LAT molecules and a fraction of PLC-gamma 1 and other signaling molecules are present in GEMs. LAT is central to T cell activation and is a novel linker molecule shown to require targeting to membrane microdomains for signaling.

引用

页码：239 / 246

页数：8

共 39 条

[11] FC-EPSILON-RI-MEDIATED RECRUITMENT OF P53/56(LYN) TO DETERGENT-RESISTANT MEMBRANE DOMAINS ACCOMPANIES CELLULAR SIGNALING [J].