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and
*Department of Physiology and
Androgen receptor (AR) belongs to the nuclear receptor superfamily
and mediates the biological actions of male sex steroids. In this work,
we have characterized a novel 130-kDa Ser/Thr protein kinase ANPK that
interacts with the zinc finger region of AR in vivo and in vitro. The
catalytic kinase domain of ANPK shares considerable sequence similarity
with the minibrain gene product, a protein kinase
suggested to contribute to learning defects associated with Down
syndrome. However, the rest of ANPK sequence, including the
AR-interacting interface, exhibits no apparent homology with other
proteins. ANPK is a nuclear protein that is widely expressed in
mammalian tissues. Its overexpression enhances AR-dependent transcription in various cell lines. In addition to the zinc finger region, ligand-binding domain and activation function AF1 of AR are
needed, as the activity of AR mutants devoid of these domains was not
influenced by ANPK. The receptor protein does not appear to be a
substrate for ANPK in vitro, and overexpression of ANPK does not
increase the extent of AR phosphorylation in vivo. In view of this, it
is likely that ANPK-mediated activation of AR function is exerted
through modification of AR-associated proteins, such as coregulatory
factors, and/or through stabilization of the receptor protein against
degradation.
Department of Clinical
Chemistry, Institute of Biomedicine, University of Helsinki, FIN-00014
Helsinki, Finland
Corresponding author. E-mail address:
jorma.palvimo{at}helsinki.fi.
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