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Vol. 10, Issue 8, 2669-2685, August 1999
and§
*Laboratory of Environmental Biochemistry, Department of
Environmental Biology, Graduate School of Agricultural Sciences, Tohoku
University, Sendai 981-8555, Japan; Activation of human platelets with thrombin transiently
increases phosphorylation at 558threonine of moesin as
determined with phosphorylation state-specific antibodies. This
specific modification is completely inhibited by the kinase inhibitor
staurosporine and maximally promoted by the phosphatase inhibitor
calyculin A, making it possible to purify the two forms of moesin to
homogeneity. Blot overlay assays with F-actin probes labeled with
either [32P]ATP or 125I show that only
phosphorylated moesin interacts with F-actin in total platelet lysates,
in moesin antibody immunoprecipitates, and when purified. In the
absence of detergents, both forms of the isolated protein are
aggregated. Phosphorylated, purified moesin co-sediments with Molecular Mechanisms
of Disease Laboratories, Department of Pathology, Stanford University
School of Medicine, Stanford, California 94305-5324; and
Department of Cell Biology, University of Massachusetts
Medical School, Worcester, Massachusetts 016055
- or
/
-actin filaments in cationic, but not in anionic, nonionic, or
amphoteric detergents. The interaction affinity is high
(Kd, ~1.5 nM), and the maximal moesin:actin
stoichiometry is 1:1. This interaction is also observed in platelets
extracted with cationic but not with nonionic detergents. In 0.1%
Triton X-100, F-actin interacts with phosphorylated moesin only in the presence of polyphosphatidylinositides. Thus, both
polyphosphatidylinositides and phosphorylation can activate moesin's
high-affinity F-actin binding site in vitro. Dual regulation by both
mechanisms may be important for proper cellular control of
moesin-mediated linkages between the actin cytoskeleton and the plasma membrane.
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