Balagopalan Lakshmi, Kortum Robert L, Coussens Nathan P, Barr Valarie A, Samelson Lawrence E
From the Laboratory of Cellular and Molecular Biology, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892-4256.
the Department of Pharmacology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, and.
J Biol Chem. 2015 Oct 30;290(44):26422-9. doi: 10.1074/jbc.R115.665869. Epub 2015 Sep 9.
Since the cloning of the critical adapter, LAT (linker for activation of T cells), more than 15 years ago, a combination of multiple scientific approaches and techniques continues to provide valuable insights into the formation, composition, regulation, dynamics, and function of LAT-based signaling complexes. In this review, we will summarize current views on the assembly of signaling complexes nucleated by LAT. LAT forms numerous interactions with other signaling molecules, leading to cooperativity in the system. Furthermore, oligomerization of LAT by adapter complexes enhances intracellular signaling and is physiologically relevant. These results will be related to data from super-resolution microscopy studies that have revealed the smallest LAT-based signaling units and nanostructure.
自15年多前关键衔接蛋白LAT(T细胞活化连接蛋白)克隆成功以来,多种科学方法和技术的结合持续为基于LAT的信号复合物的形成、组成、调控、动力学及功能提供了有价值的见解。在本综述中,我们将总结关于由LAT引发的信号复合物组装的当前观点。LAT与其他信号分子形成众多相互作用,从而导致系统中的协同作用。此外,衔接蛋白复合物使LAT寡聚化可增强细胞内信号传导,且具有生理相关性。这些结果将与超分辨率显微镜研究的数据相关联,这些研究揭示了最小的基于LAT的信号单元和纳米结构。
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