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J. Biol. Chem., Vol. 275, Issue 50, 39718-39726, December 15, 2000
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From the Department of Applied Molecular Biosciences, Graduate
School of Bioagricultural Sciences, Nagoya University, Furo-cho,
Chikusa-ku, Nagoya 464-8601, Japan
Prolactin (PRL) plays a central and crucial role
in the regulation of milk protein gene expression in mammary epithelial
cells. PRL binding to its cognate receptor leads to receptor
dimerization and activation of the tyrosine kinase Janus kinase 2 (JAK2), associated with the membrane-proximal, intracellular domain of
the receptor. In turn, JAK2 phosphorylates and activates STAT5, a
member of the signal transducers and activators of transcription (STAT) family. We have recently reported that 16 different protein-tyrosine phosphatases (PTP) were expressed in lactating mouse mammary gland and
mammary epithelial cells (Aoki, N., Kawamura, M., Yamaguchi-Aoki, Y.,
Ohira, S., and Matsuda, T. (1999) J. Biochem.
(Tokyo) 125, 669-675). We investigated the involvement of
each PTP in PRL signaling. Among the 12 phosphatases including SHP-2
examined, a cytosolic phosphatase PTP1B was found to specifically
dephosphorylate STAT5a and STAT5b in transfected COS7 and in
vitro. Nuclear translocation of STAT5a and STAT5b was largely
inhibited upon overexpression of PTP1B. The PRL-dependent
transcriptional activation of the
A Cytosolic Protein-tyrosine Phosphatase PTP1B Specifically
Dephosphorylates and Deactivates Prolactin-activated STAT5a and
STAT5b*
and
-casein gene promoter was also
inhibited by PTP1B. Furthermore, retrovirus-mediated overexpression of
PTP1B resulted in dephosphorylation of endogenous STAT5 and
down-regulation of -casein gene expression in mammary epithelial
COMMA-1D cells when the cells were treated with lactogenic hormones.
Endogenous tyrosine-phosphorylated STAT5 proteins in mammary epithelial
COMMA-1D cells as well as tyrosine-phosphorylated STAT5a and STAT5b
expressed in COS7 cells were co-precipitated by substrate-trapping
mutants of recombinant PTP1B. These results strongly suggest that PTP1B
dephosphorylates PRL-activated STAT5a and STAT5b, thereby negatively
regulating PRL-mediated signaling pathway.
*
This work was supported in part by grants from Japan Society
for Bioscience, Biotechnology, and Agrochemistry.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Applied
Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan. Fax:
81-52-789-4128; E-mail: naoki@agr.nagoya-u.ac.jp.
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