Autoinhibitory interaction in the multidomain adaptor protein Nck: possible roles in improving specificity and functional diversity.

ABSTRACT: Nck is a functionally versatile multidomain adaptor protein consisting of one SH2 and three SH3 domains. In most cases, the SH2 domain mediates binding to tyrosine-phosphorylated receptors or cytosolic proteins, which leads to the formation of larger protein complexes via the SH3 domains. Nck plays a pivotal role in T-cell receptor-mediated reorganization of the actin cytoskeleton as well as in the formation of the immunological synapses. The modular domain structure and the functionality of the individual domains suggest that they might act independently. Here we report an interesting intramolecular interaction within Nck that occurs between a noncanonical yet conserved (K/R)x(K/R)RxxS sequence in the linker between the first and second SH3 domain (SH3.1/SH3.2) and the second SH3 domain (

SUBMITTER: Takeuchi K 

PROVIDER: S-EPMC2899887 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature