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


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