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

Content Provider	PubMed Central
Author	Alex, Braiman Mira, Barda-saad Sommers, Connie L. Samelson, Lawrence E.
Copyright Year	2006
Abstract	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.
Related Links	http://dx.doi.org/10.1038/sj.emboj.7600978
Ending Page	784
Page Count	11
Starting Page	774
File Format	PDF
ISSN	02614189
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	4
Volume Number	25
Language	English
Publisher Date	2006-02-22
Access Restriction	Open
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

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