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Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band.
Max-Planck-Institute for Biophysical Chemistry, Department of Biochemistry, D-37077 Göttingen, Germany.
The myofibrils of cross-striated muscle fibers contain in their M bands cytoskeletal proteins whose main function seems to be the stabilization of the three-dimensional arrangement of thick filaments. We identified two immunoglobin domains (Mp2-Mp3) of M-protein as a site binding to the central region of light meromyosin. This binding is regulated in vitro by phosphorylation of a single serine residue (Ser76) in the immediately adjacent amino-terminal domain Mp1. M-protein phosphorylation by cAMP-dependent kinase A inhibits binding to myosin LMM. Transient transfection studies of cultured cells revealed that the myosin-binding site seems involved in the targeting of M-protein to its location in the myofibril. Using the same method, a second myofibril-binding site was uncovered in domains Mp9-Mp13. These results support the view that specific phosphorylation events could be also important for the control of sarcomeric M band formation and remodeling.
PMID: 9529381 [PubMed - indexed for MEDLINE]
PMCID: PMC25310
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Cited by 8 PubMed Central articles
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Woods S, Farrall A, Procko C, Whitelaw ML.
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[Nucleic Acids Res. 2008]
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Regulation of skeletal muscle sarcomere integrity and postnatal muscle function by Mef2c.
Potthoff MJ, Arnold MA, McAnally J, Richardson JA, Bassel-Duby R, Olson EN.
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[Mol Cell Biol. 2007]
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A mutation in the dimerization domain of filamin c causes a novel type of autosomal dominant myofibrillar myopathy.
Vorgerd M, van der Ven PF, Bruchertseifer V, Löwe T, Kley RA, Schröder R, Lochmüller H, Himmel M, Koehler K, Fürst DO, et al.
Am J Hum Genet. 2005 Aug; 77(2):297-304. Epub 2005 May 31.
[Am J Hum Genet. 2005]
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