Tyrosine phosphorylation of myosin heavy chain during skeletal muscle differentiation: An integrated bioinformatics approach

D. F. Harney, R. K. Butler, R. J. Edwards

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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 tyrosines 163 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.

Original languageEnglish (US)
JournalTheoretical Biology and Medical Modelling
Volume2
DOIs
StatePublished - Mar 25 2005
Externally publishedYes

Fingerprint

Phosphorylation
Skeletal muscle
Myosin
Myosin Heavy Chains
Bioinformatics
Computational Biology
Tyrosine
Muscle
Skeletal Muscle
Platelets
Insulin
Blood Platelets
Phosphor
Functional analysis
Cell
Functional Analysis
Phosphors
Muscle Cells
Phosphotransferases
Cells

ASJC Scopus subject areas

  • Modeling and Simulation
  • Health Informatics

Cite this

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T1 - Tyrosine phosphorylation of myosin heavy chain during skeletal muscle differentiation

T2 - An integrated bioinformatics approach

AU - Harney, D. F.

AU - Butler, R. K.

AU - Edwards, R. J.

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N2 - 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 tyrosines 163 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.

AB - 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 tyrosines 163 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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