The EMBO Journal
 
Advanced search
Journal home
Current issue
Advance Online Publication
Web Focuses
Archive
Browse by subject
Free online sample issue
Aims and scope
Press releases
ToC by email
Authors & Referees
Guide for authors
Submit an Article
Guide for referees
Editorial Team, Senior Advisors and Advisory Editorial Board
Contact Editorial office
Customer services
Subscribe
Order sample copy
Purchase articles
Reprints and permissions
Contact NPG
Advertising
EMBO
www.embo.org
Article
Subject Categories: Signal Transduction | Immunology
The EMBO Journal (2006) 25, 774–784, doi:10.1038/sj.emboj.7600978
Published online 9 February 2006
Recruitment and activation of PLCgamma1 in T cells: a new insight into old domains
Alex Braiman, Mira Barda-Saad, Connie L Sommers and Lawrence E Samelson
Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA

To whom correspondence should be addressed
Lawrence E Samelson, Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Building 37, Room 2066, Bethesda, MD 20892-4254, USA. Tel.: +1 301 496 9683; Fax: +1 301 496 8479; E-mail: samelson@helix.nih.gov

Received 25 August 2005; Accepted 9 January 2006; Published online 9 February 2006.
Abstract
Engagement of the T-cell antigen receptor leads to recruitment of phospholipase Cgamma1 (PLCgamma1) to the LAT-nucleated signaling complex and to PLCgamma1 activation in a tyrosine phosphorylation-dependent manner. The mechanism of PLCgamma1 recruitment and the role of PLCgamma1 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 PLCgamma1 is necessary but not sufficient for its recruitment. Either the SH3 or C-terminal SH2 domain of PLCgamma1, with the participation of Vav1, c-Cbl and Slp76, are required to stabilize PLCgamma1 recruitment. All three PLCgamma1 SH domains are required for phosphorylation of PLCgamma1 Y783, which is critical for enzyme activation. These novel findings entailed revision of the currently accepted model of PLCgamma1 recruitment and activation in T lymphocytes.
Keywords: calcium, confocal microscopy, FRET, protein–protein interaction, TCR
Top

MORE ARTICLES LIKE THIS

Send to a friendEmail link to a friend
PDFDownload PDF
Full textFull text
Next article
Previous article
Table of contents
rights and permissionsRights and permissions
order commercial reprintsReprints
ToC alertRegister for table of contents by email
  Privacy policy Copyright © 2006 by the European Molecular Biology Organization