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J. Biol. Chem., Vol. 276, Issue 18, 14704-14709, May 4, 2001
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From the Department of Biochemistry and Molecular Biology, School
of Medicine, University of Louisville, Louisville, Kentucky
40292
The plasma membrane Ca2+-ATPase
(PMCA) plays an essential role in maintaining low cytosolic
Ca2+ in resting platelets. During platelet activation PMCA
is phosphorylated transiently on tyrosine residues resulting in
inhibition of the pump that enhances elevation of Ca2+.
Tyrosine phosphorylation of many proteins during platelet activation results in their association with the cytoskeleton. Consequently, in
the present study we asked if PMCA interacts with the platelet cytoskeleton. We observed that very little PMCA is associated with the
cytoskeleton in resting platelets but that ~80% of total PMCA
(PMCA1b + PMCA4b) is redistributed to the cytoskeleton upon activation
with thrombin. Tyrosine phosphorylation of PMCA during activation was
not associated with the redistribution because tyrosine-phosphorylated
PMCA was not translocated specifically to the cytoskeleton. Because
PMCA b-splice isoforms have C-terminal PSD-95/Dlg/ZO-1 homology
domain (PDZ)-binding domains, a C-terminal peptide was used to
disrupt potential PDZ domain interactions. Activation of
saponin-permeabilized platelets in the presence of the peptide led to a
significant decrease of PMCA in the cytoskeleton. PMCA associated with
the cytoskeleton retained Ca2+-ATPase activity. These
results suggest that during activation active PMCA is recruited to the
cytoskeleton by interaction with PDZ domains and that this association
provides a microenvironment with a reduced Ca2+ concentration.
Plasma Membrane Ca2+-ATPase Associates with the
Cytoskeleton in Activated Platelets through a PDZ-binding Domain*
*
This work was supported by Grant-in-aid 9750039N from the
American Heart Association (to W. L. D.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 502-852-5227;
Fax: 502-852-6222; E-mail: bill.dean@louisville.edu.
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