| Literature DB >> 20610546 |
Lakshmi Balagopalan1, Nathan P Coussens, Eilon Sherman, Lawrence E Samelson, Connie L Sommers.
Abstract
The adapter molecule LAT is a nucleating site for multiprotein signaling complexes that are vital for the function and differentiation of T cells. Extensive investigation of LAT in multiple experimental systems has led to an integrated understanding of the formation, composition, regulation, dynamic movement, and function of LAT-nucleated signaling complexes. This review discusses interactions of signaling molecules that bind directly or indirectly to LAT and the role of cooperativity in stabilizing LAT-nucleated signaling complexes. In addition, it focuses on how imaging studies visualize signaling assemblies as signaling clusters and demonstrate their dynamic nature and cellular fate. Finally, this review explores the function of LAT based on the interpretation of mouse models using various LAT mutants.Entities:
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Year: 2010 PMID: 20610546 PMCID: PMC2908767 DOI: 10.1101/cshperspect.a005512
Source DB: PubMed Journal: Cold Spring Harb Perspect Biol ISSN: 1943-0264 Impact factor: 10.005