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J Biol Chem, Vol. 274, Issue 8, 4939-4946, February 19, 1999
From the Divisions of The ETS domain transcription factor PU.1 is
necessary for the development of monocytes and regulates, in
particular, the expression of the monocyte-specific macrophage
colony-stimulating factor (M-CSF) receptor, which is critical for
monocytic cell survival, proliferation, and differentiation. The bZIP
transcription factor c-Jun, which is part of the AP-1 transcription
factor complex, is also important for monocytic differentiation, but
the monocyte-specific M-CSF receptor promoter has no AP-1 consensus
binding sites. We asked the question of whether c-Jun could promote the
induction of the M-CSF receptor by collaborating with PU.1. We
demonstrate that c-Jun enhances the ability of PU.1 to transactivate
the M-CSF receptor promoter as well as a minimal thymidine kinase
promoter containing only PU.1 DNA binding sites. c-Jun does not
directly bind to the M-CSF receptor promoter but associates via its
basic domain with the ETS domain of PU.1. Consistent with our
observation that AP-1 binding does not contribute to c-Jun coactivation
is the observation that the activation of PU.1 by c-Jun is blocked by
overexpression of c-Fos. Phosphorylation of c-Jun by c-Jun NH2-terminal kinase on Ser-63 and -73 does not alter
the ability of c-Jun to enhance PU.1 transactivation. Activated Ras
enhances the transcriptional activity of PU.1 by up-regulating c-Jun
expression without changing the phosphorylation pattern of PU.1. The
activation of PU.1 by Ras is blocked by a mutant c-Jun protein lacking
the basic domain. The expression of this mutant form of c-Jun also completely blocks
12-O-tetradecanoylphorbol-13-acetate-induced M-CSF receptor
promoter activity during monocytic differentiation. We propose
therefore that c-Jun acts as a c-Jun NH2-terminal
kinase-independent coactivator of PU.1, resulting in M-CSF receptor
expression and development of the monocytic lineage.
c-Jun Is a JNK-independent Coactivator of the PU.1 Transcription
Factor
,
,,,
Hematology/Oncology and
Signal Transduction, Beth Israel Deaconess Medical Center and
Harvard Medical School, Boston, Massachusetts 02115, the
¶ Department of Biochemistry and Molecular Biology, University of
Massachusetts Medical School, Worcester, Massachusetts 01605, and the
** Clinical Research Institute of Montreal, Montreal, Quebec
H2W1R7, Canada
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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