Journal article
Cooperative interactions at the SLP-76 complex are critical for actin polymerization
The EMBO journal, Vol.29(14), pp.2315-2328
07/21/2010
DOI: 10.1038/emboj.2010.133
PMCID: PMC2910278
PMID: 20562827
Abstract
T-cell antigen receptor (TCR) engagement induces formation of multi-protein signalling complexes essential for regulating T-cell functions. Generation of a complex of SLP-76, Nck and VAV1 is crucial for regulation of the actin machinery. We define the composition, stoichiometry and specificity of interactions in the SLP-76, Nck and VAV1 complex. Our data reveal that this complex can contain one SLP-76 molecule, two Nck and two VAV1 molecules. A direct interaction between Nck and VAV1 is mediated by binding between the C-terminal SH3 domain of Nck and the VAV1 N-terminal SH3 domain. Disruption of the VAV1:Nck interaction deleteriously affected actin polymerization. These novel findings shed new light on the mechanism of actin polymerization after T-cell activation.
Details
- Title: Subtitle
- Cooperative interactions at the SLP-76 complex are critical for actin polymerization
- Creators
- Mira Barda-Saad - Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan, Israel. bardasm@mail.biu.ac.ilNaoto ShirasuMaor H PaukerNirit HassanOrly PerlAndrea BalboHiroshi YamaguchiJon C D HoutmanEttore AppellaPeter SchuckLawrence E Samelson
- Resource Type
- Journal article
- Publication Details
- The EMBO journal, Vol.29(14), pp.2315-2328
- DOI
- 10.1038/emboj.2010.133
- PMID
- 20562827
- PMCID
- PMC2910278
- ISSN
- 0261-4189
- eISSN
- 1460-2075
- Grant note
- Intramural NIH HHS
- Language
- English
- Date published
- 07/21/2010
- Academic Unit
- Microbiology and Immunology; Internal Medicine
- Record Identifier
- 9984094556302771
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