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Blood, 1 April 2001, Vol. 97, No. 7, pp. 2091-2097
NEOPLASIA
Cyclin A1 directly interacts with B-myb and cyclin A1/cdk2
phosphorylate B-myb at functionally important serine and threonine
residues: tissue-specific regulation of B-myb function
Carsten Müller-Tidow,
Wenbing Wang,
Gregory E. Idos,
Sven Diederichs,
Rong Yang,
Carol Readhead,
Wolfgang E. Berdel,
Hubert Serve,
Mark Saville,
Roger Watson, and
H. Phillip Koeffler
From the Department of Medicine, Hematology,
and Oncology, University of Münster, Germany; the Division
of Hematology/Oncology, Cedars-Sinai Research Institute/UCLA School of
Medicine, Los Angeles, CA; the Division of Biology, California
Institute of Technology, Pasadena, CA; and the Ludwig Institute for
Cancer Research, Imperial College School of Medicine, London, England.
Cyclin A1 is tissue-specifically expressed during
spermatogenesis, but it is also highly expressed in acute myeloid
leukemia (AML). Its pathogenetic role in AML and in the cell cycle of
leukemic blasts is unknown. B-myb is essential for G1/S transition and has been shown to be phosphorylated by the cyclin A2/cdk2 complex. Here it is demonstrated that cyclin A1 interacts with the
C-terminal portion of B-myb as shown by glutathione S-transferase
(GST) precipitation. This interaction is confined to cyclin A1
because binding could not be detected between cyclin A2 and B-myb.
Also, cdk2 was not pulled down by GST-B-myb from U937 lysates. In
addition, co-immunoprecipitation of cyclin A1 and B-myb in leukemic
cells evidenced protein interaction in vivo. Baculovirus-expressed
cyclin A1/cdk2 complexes were able to phosphorylate human as well as
murine B-myb in vitro. Tryptic phosphopeptide mapping revealed that
cyclin A1/cdk2 complexes phosphorylated the C-terminal part of B-myb at
several sites including threonine 447, 490, and 497 and serine 581. These phosphorylation sites have been demonstrated to be important for
the enhancement of B-myb transcriptional activity. Further studies
showed that cyclin A1 cooperated with B-myb to transactivate myb
binding site containing promoters including the promoter of the human
cyclin A1 gene. Taken together, the data suggest that cyclin A1 is a tissue-specific regulator of B-myb function and activates B-myb in
leukemic blasts.
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