Recruitment and activation of PLCγ1 in T cells:: a new insight into old domains

被引:98
作者
Braiman, A [1 ]
Barda-Saad, M [1 ]
Sommers, CL [1 ]
Samelson, LE [1 ]
机构
[1] NCI, Cellular & Mol Biol Lab, NIH, Bethesda, MD 20892 USA
关键词
calcium; confocal microscopy; FRET; protein-protein interaction; TCR;
D O I
10.1038/sj.emboj.7600978
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
Engagement of the T- cell antigen receptor leads to recruitment of phospholipase C gamma 1 ( PLC gamma 1) to the LAT- nucleated signaling complex and to PLC gamma 1 activation in a tyrosine phosphorylation- dependent manner. The mechanism of PLC gamma 1 recruitment and the role of PLC gamma 1 Src homology ( SH) domains in this process remain incompletely understood. Using a combination of biochemical methods and real- time fluorescent imaging, we show here that the N- terminal SH2 domain of PLC gamma 1 is necessary but not sufficient for its recruitment. Either the SH3 or C- terminal SH2 domain of PLC gamma 1, with the participation of Vav1, c- Cbl and Slp76, are required to stabilize PLC gamma 1 recruitment. All three PLC gamma 1 SH domains are required for phosphorylation of PLC gamma 1 Y783, which is critical for enzyme activation. These novel findings entailed revision of the currently accepted model of PLC gamma 1 recruitment and activation in T lymphocytes.
引用
收藏
页码:774 / 784
页数:11
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