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J. Biol. Chem., Vol. 277, Issue 44, 41311-41317, November 1, 2002
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From the The androgen receptor (AR) has been shown to be
modified by SUMO-1, a ubiquitin-like protein. Recently we showed
that PIAS family proteins function as SUMO-E3 ligases. Here we provide
evidence that PIAS1 and PIASx
PIAS1 and PIASx
Function as SUMO-E3 Ligases toward Androgen
Receptor and Repress Androgen Receptor-dependent
Transcription*
and§¶
Division of Molecular Biology, School of
Life Science, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan and the
§ Department of Chemistry, School of Science, University
of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
act as specific SUMO-E3 ligases for
the AR. PIAS1 and PIASx but not PIAS3 or PIASx
enhanced
the sumoylation of AR in intact cells and in
vitro. PIAS1 and PIASx bound Ubc9, the E2 enzyme for SUMO-1,
in a RING finger-like domain-dependent manner. Consistent
with previous studies (Kahyo, T., Nishida, T., and Yasuda, H. (2001)
Mol. Cell 8, 713-718), the RING finger-like domain
of the SUMO-E3 was required for ligase activity. The binding of a
ligand, e.g. testosterone, to the AR was required for the sumoylation of AR in intact cells. Although AR-dependent
transcription was enhanced by PIAS proteins without sumoylation of the
receptor, PIAS1 and PIASx repressed AR-dependent
transcription in a manner dependent on the ectopic expression of SUMO-1
and their RING finger-like domain. Furthermore, the sumoylation sites
of the AR were necessary for the full repressive effect on
AR-dependent transactivation, indicating that the
sumoylation of AR was crucial for the repression of transactivation of
the AR. Thus, PIAS1 and PIASx modulate the AR-dependent
transactivation, which, at least in part, can be attributed to their
SUMO-E3 activity toward AR.
*
This work was supported in part by a grant-in-aid from the
Ministry of Education, Culture, Sports, Science, and Technology of
Japan and also by the Uehara Memorial Foundation (to H. Y.).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.
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