Cooperative interactions at the SLP-76 complex are critical for actin polymerization
Cooperative interactions at the SLP-76 complex are critical for actin polymerization
复制标题
DOI：
10.1038/emboj.2010.133
复制
发表时间：
2010-07-21
期刊：
影响因子：
11.4
通讯作者：
Samelson, Lawrence E.
中科院分区：
文献类型：
--
作者：
Barda-Saad, Mira;Shirasu, Naoto;Samelson, Lawrence E.
t细胞抗原受体（TCR）参与诱导形成对调节t细胞功能至关重要的多蛋白信号复合物。SLP-76、Nck和VAV1复合物的产生对肌动蛋白机制的调控至关重要。我们定义了SLP-76、Nck和VAV1复合物中相互作用的组成、化学计量学和特异性。我们的数据表明，该复合物可以包含一个SLP-76分子，两个Nck分子和两个VAV1分子。Nck和VAV1之间的直接相互作用是通过Nck的c端SH3结构域和VAV1的n端SH3结构域的结合介导的。VAV1: Nck相互作用的破坏有害地影响肌动蛋白聚合。这些新发现为研究t细胞活化后肌动蛋白聚合的机制提供了新的思路。EMBO杂志（2010）29,2315-2328。doi: 10.1038 / emboj.2010.133;2010年6月18日在线发布
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