C-terminal COOH of integrin β1 is necessary for β1 association with the kindlin-2 adapter protein.

ABSTRACT: Protein-protein interactions are driving forces in cellular processes. As a prime example, transmembrane integrins link extracellular matrix and intracellular proteins, resulting in bidirectional signaling that regulates cell migration, proliferation, differentiation, and survival. Here we provide the first evidence that interaction between the integrin β1 cytoplasmic tail and kindlin-2, a member of a family of adapters implicated in human disease pathogenesis, is mainly governed by the β1 C-terminal carboxylate moiety and is required for laterality organ development in zebrafish. Affinity measurements indicate that this unusual protein-protein interaction mode is coordinated by a putative carboxylate-binding motif in the kindlin-2 FERM subdomain F3. Contrary to the C terminus of proteins

SUBMITTER: Fitzpatrick P 

PROVIDER: S-EPMC4036257 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature