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Vol. 9, Issue 4, 829-840, April 1998

Mapping of a Myosin-binding Domain and a Regulatory Phosphorylation Site in M-Protein, a Structural Protein of the Sarcomeric M Band

Wolfgang M.J. Obermann,* Peter F.M. van der Ven,*dagger Frank Steiner,* Klaus Weber,* and Dieter O. Fürstdagger Dagger

 *Max-Planck-Institute for Biophysical Chemistry, Department of Biochemistry, D-37077 Göttingen, Germany; and  dagger University of Potsdam, Department of Cell Biology, D-14471 Potsdam, 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.


Molecular Biology of the Cell
Vol. 9, 829-840, April 1998
Copyright © 1998 by The American Society for Cell Biology



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