A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts
A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts
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DOI：
10.1016/s0092-8674(00)81608-6
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发表时间：
1998-09-04
期刊：
影响因子：
64.5
通讯作者：
Shaw, AS
中科院分区：
文献类型：
--
作者：
Dustin, ML;Olszowy, MW;Shaw, AS
T细胞识别抗原需要在T细胞和抗原提呈细胞之间形成一个特殊的连接。这种连接是通过从接触区招募和排除特定蛋白质而产生的。监管这些事件的机制尚不清楚。在这里，我们证明了黏附分子CD2的配体结合启动了蛋白质分离、CD2聚集和细胞骨架极化的过程。虽然蛋白质的分离不依赖于CD2的胞质结构域，但CD2的聚集和细胞骨架的极化需要CD2胞质结构域与一种新的含SH3的蛋白质相互作用。这种新的蛋白质被称为CD2AP，可能通过将特定的黏附受体连接到细胞骨架来促进接触区域的受体模式。
Recognition of antigen by T cells requires the formation of a specialized junction between the T cell and the antigen-presenting cell. This junction is generated by the recruitment and the exclusion of specific proteins from the contact area. The mechanisms that regulate these events are unknown. Here we demonstrate that ligand engagement of the adhesion molecule, CD2, initiates a process of protein segregation, CD2 clustering, and cytoskeletal polarization. Although protein segregation was not dependent on the cytoplasmic domain of CD2, CD2 clustering and cytoskeletal polarization required an interaction of the CD2 cytoplasmic domain with a novel SH3-containing protein. This novel protein, called CD2AP, is likely to facilitate receptor patterning in the contact area by linking specific adhesion receptors to the cytoskeleton.