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(Received for publication, August 21, 1997, and in revised form, September 5, 1997)
,
and
From the § Department of Biochemistry and Molecular
Biology, Mayo Foundation, Rochester, Minnesota 55905 and the
Phosphorylation by protein kinase C of the
"a" and "b" variants of plasma membrane Ca2+
pump isoforms 2 and 3 was studied. Full-length versions of these isoforms were assembled and expressed in COS cells. Whereas the "a"
forms were phosphorylated easily with PKC, isoform 2b was phosphorylated only a little, and isoform 3b was not phosphorylated at
all. Phosphorylation of isoforms 2a and 3a did not affect their basal
activity, but prevented the stimulation of their activity by calmodulin
and their binding to calmodulin-Sepharose. This indicated that
phosphorylation prevented activation of these isoforms by preventing
calmodulin binding. Based on these results, phosphorylation of the pump
with PKC would be expected to increase free intracellular Ca2+ levels in those cells where isoforms 2a and 3a are
expressed.
National Institute of Haematology and Immunology, Daroczi
ut 24, 1113 Budapest, Hungary
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