The kinase domains of obscurin interact with intercellular adhesion proteins.

ABSTRACT: Obscurins comprise a family of giant (~870- to 600-kDa) and small (~250- to 55-kDa) proteins that play important roles in myofibrillogenesis, cytoskeletal organization, and cell adhesion and are implicated in hypertrophic cardiomyopathy and tumorigenesis. Giant obscurins are composed of tandem structural and signaling motifs, including 2 serine/threonine kinase domains, SK1 and SK2, present at the COOH terminus of giant obscurin-B. Using biochemical and cellular approaches, we show for the first time that both SK1 and SK2 possess enzymatic activities and undergo autophosphorylation. SK2 can phosphorylate the cytoplasmic domain of N-cadherin, a major component of adherens junctions, and SK1 can interact with the extracellular domain of the β1-subunit of the Na(+)/K(+)-ATPase, which also res

SUBMITTER: Hu LY 

PROVIDER: S-EPMC3633816 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature