Cooperative interactions at the SLP-76 complex are critical for actin polymerization

被引：88

作者：

Barda-Saad, Mira ^{[1
]}

Shirasu, Naoto ^{[2
]}

Pauker, Maor H. ^{[1
]}

Hassan, Nirit ^{[1
]}

Perl, Orly ^{[1
]}

Balbo, Andrea ^{[3
]}

Yamaguchi, Hiroshi ^{[4
]}

Houtman, Jon C. D. ^{[5
]}

Appella, Ettore ^{[4
]}

Schuck, Peter ^{[3
]}

Samelson, Lawrence E. ^{[2
]}

机构：

[1] Bar Ilan Univ, Mina & Everard Goodman Fac Life Sci, IL-52900 Ramat Gan, Israel

[2] NCI, Cellular & Mol Biol Lab, Ctr Canc Res, Bethesda, MD 20892 USA

[3] NIH, Lab Bioengn & Phys Sci, NIBIB, Bethesda, MD 20892 USA

[4] NCI, Cell Biol Lab, Bethesda, MD 20892 USA

[5] Univ Iowa, Dept Microbiol, Iowa City, IA 52242 USA

来源：

EMBO JOURNAL | 2010年 / 29卷 / 14期

基金：

以色列科学基金会;

关键词：

actin polymerization; lymphocyte activation; signalling complexes; SLP-76; T-CELL-RECEPTOR; APC CONTACT SITE; SIGNAL-TRANSDUCTION; ANTIGEN RECEPTOR; ADAPTER PROTEIN; PHOSPHOLIPASE C-GAMMA-1; IMMUNOLOGICAL SYNAPSE; IMMUNE SYNAPSE; ACTIVATION; CYTOSKELETON;

D O I：

10.1038/emboj.2010.133

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

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. The EMBO Journal (2010) 29, 2315-2328. doi:10.1038/emboj.2010.133; Published online 18 June 2010

引用

页码：2315 / 2328

页数：14

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