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Recent genetic and functional evidence suggests that the amino
terminus of the retinoblastoma (Rb) protein plays an important role in
Rb-mediated growth suppression. To explore the mechanism(s) by which
this portion of Rb may regulate cell growth, we have sought to
characterize cellular proteins that associate with the Rb amino
terminus using an in vitro protein-binding assay. Here we
report that at least one such protein is a cell cycle-regulated
Rb/histone H1 kinase (RbK) whose enzymatic and/or Rb association
activity is most prevalent in G
Volume 270,
Number 16,
Issue of April 21, pp. 9281-9288, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
/M Phases
/M phases of cells. In
contrast to previously characterized cyclin-dependent and Rb-associated
kinases, such as cdk1 (cdc2) and cdk2, G/M RbK 1) is not
depleted by incubation with p13-beads, 2) is not detected
with antisera against several Rb-associated cyclins-cdks, and 3)
associates with Rb via the Rb amino terminus, a region that is
dispensable for interaction with other Rb-associated kinases. RbK is
clearly distinct from previously characterized mitotic cdks since
cyclin A-cdc2, cyclin A-cdk2, cyclin B-cdc2, and cyclin B-cdk2 did not
associate with the Rb amino terminus. Coprecipitation experiments with
Rb antisera confirmed the association of Rb with a RbK-like kinase in
metaphase-arrested cells in vivo. Interestingly,
G
/M RbK did not appreciably associate with an analogous
portion of p107, a Rb-related protein. Taken together, these data
indicate that the Rb amino terminus specifically associates with a
novel cell cycle-regulated kinase in late cell cycle stages.
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