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(Received for publication, October 1, 1996, and in revised form, November 18, 1996)
From the pRb controls cell proliferation by restricting
inappropriate entry of cells into the cell division cycle. As
dephosphorylation of pRb during mitotic exit activates its growth
suppressive function, identification of the protein phosphatase that
dephosphorylates pRb, and characterization of the mechanism of its
regulation, are essential to elucidating the mechanisms of cell growth
control. By fractionating mitotic CV-1P cell extracts, we identify the protein phosphatase which dephosphorylates pRb as a type 1 serine/threonine phosphoprotein phosphatase (PP1). Molecular sizing
analyses indicate that the catalytic enzyme (PP1c) is present in a high
molecular weight complex, with a predicted molecular mass of 166 kDa.
PP1-interacting proteins in the mitotic cell extracts are identified.
Two PP1-interacting proteins (41 and 110 kDa) are shown to form
distinct complexes with PP1c from fractions of separated mitotic cell
extracts containing phosphorylase phosphatase activity. However, only
the 110-kDa PP1-interacting protein is present in fractions containing
pRb-directed phosphatase activity, identifying this protein as a
putative activator of PP1 function toward pRb during mitosis.
Volume 272, Number 7,
Issue of February 14, 1997
pp. 4528-4535
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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