Key result
A combined bioinformatics approach identified tyrosines 163 and 1856 of the skeletal muscle heavy chain as the leading candidates for insulin-mediated tyrosine phosphorylation.
Bioinformatics analysis identifies tyrosines 163 and 1856 on skeletal muscle myosin heavy chain as the most likely sites for insulin-mediated tyrosine phosphorylation, providing targets for future functional studies.
Does not inform clinical practice; hypothesis-generating for functional validation of myosin phosphorylation in insulin signaling.
BACKGROUND: Previously it has been shown that insulin-mediated tyrosine phosphorylation of myosin heavy chain is concomitant with enhanced association of C-terminal SRC kinase during skeletal muscle differentiation. We sought to identify putative site(s) for this phosphorylation event. RESULTS: A combined bioinformatics approach of motif prediction and evolutionary and structural analyses identified tyrosines163 and 1856 of the skeletal muscle heavy chain as the leading candidate for the sites of insulin-mediated tyrosine phosphorylation. CONCLUSION: Our work is suggestive that tyrosine phosphorylation of myosin heavy chain, whether in skeletal muscle or in platelets, is a significant event that may initiate cytoskeletal reorganization of muscle cells and platelets. Our studies provide a good starting point for further functional analysis of MHC phosphor-signalling events within different cells.
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Harney et al. (2005) studied Skeletal muscle differentiation. Bioinformatics analysis was evaluated on Identification of putative tyrosine phosphorylation sites on myosin heavy chain. A combined bioinformatics approach identified tyrosines 163 and 1856 of the skeletal muscle heavy chain as the leading candidates for insulin-mediated tyrosine phosphorylation.
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