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Oncoprotein 18 (Op18) is a conserved cytosolic protein that is a
target for both cell cycle and cell surface receptor-regulated
phosphorylation events. The four residues Ser
Volume 270,
Number 23,
Issue of June 9, pp. 14175-14183, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Ser
, Ser
, and Ser
are all
subject to cell cycle-regulated phosphorylation. Ser
and
Ser
are targets for cyclin dependent kinases (CDKs), while
Ser
and Ser
are phosphorylated by an
unidentified protein kinase. We have recently shown that induced
expression of a CDK target site-deficient mutant, Op18-S25A,S38A,
blocks human cell lines during G2/M transition. In the present report
we show that mitosis is associated with complete phosphorylation of the
two Op18 CDK target sites Ser
and Ser
and
that Ser
and Ser
are also phosphorylated to a
high stoichiometry. To evaluate the function of multisite
phosphorylation of Op18, we expressed and analyzed the cell cycle
phenotype of different kinase target site-deficient mutants. The data
showed that induced expression of the S16A,S63A, S25A,S38A, and
S16A,S25A,S38A,S63A mutants all resulted in an indistinguishable
phenotype, i.e. immediate G2/M block and subsequent
endoreduplication, a given fraction of G2 versus M-phase
blocked cells, and a characteristic nuclear morphology of M-blocked
cells. This result was unexpected; however, a likely explanation was
provided by analysis of Op18 phosphoisomers, which revealed that
mutations of the CDK sites interfere with phosphorylation of Ser
and Ser
. The simplest interpretation of our results
is that phosphorylation of Ser
and Ser
is
essential during G2/M transition and that the phenotype of the
S25A,S38A mutant is mediated by the observed block of
Ser
/Ser
phosphorylation.
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