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Recruitment and activation of PLCγ1 in T cells: a new insight into old domains
Author(s) -
Braiman Alex,
BardaSaad Mira,
Sommers Connie L,
Samelson Lawrence E
Publication year - 2006
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600978
Subject(s) - library science , experimental biology , national laboratory , biology , computational biology , computer science , physics , engineering physics
Engagement of the T‐cell antigen receptor leads to recruitment of phospholipase Cγ1 (PLCγ1) to the LAT‐nucleated signaling complex and to PLCγ1 activation in a tyrosine phosphorylation‐dependent manner. The mechanism of PLCγ1 recruitment and the role of PLCγ1 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 PLCγ1 is necessary but not sufficient for its recruitment. Either the SH3 or C‐terminal SH2 domain of PLCγ1, with the participation of Vav1, c‐Cbl and Slp76, are required to stabilize PLCγ1 recruitment. All three PLCγ1 SH domains are required for phosphorylation of PLCγ1 Y783, which is critical for enzyme activation. These novel findings entailed revision of the currently accepted model of PLCγ1 recruitment and activation in T lymphocytes.