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Cooperative interactions at the SLP‐76 complex are critical for actin polymerization
Author(s) -
BardaSaad Mira,
Shirasu Naoto,
Pauker Maor H,
Hassan Nirit,
Perl Orly,
Balbo Andrea,
Yamaguchi Hiroshi,
Houtman Jon C D,
Appella Ettore,
Schuck Peter,
Samelson Lawrence E
Publication year - 2010
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/emboj.2010.133
Subject(s) - biology , actin , polymerization , computational biology , evolutionary biology , microbiology and biotechnology , polymer , chemistry , organic chemistry
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.