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J. Biol. Chem., Vol. 278, Issue 20, 18085-18091, May 16, 2003
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From the Sterile 20 (STE20) protein kinases, which include
germinal center kinases and p21-activated protein kinases, are
known to activate mitogen-activated protein kinase pathways (c-Jun
NH2-terminal kinase, p38, or extracellular
signal-regulated kinase), leading to changes in gene
transcription. Some STE20s can also regulate the cytoskeleton,
and we have shown that the germinal center kinase-like kinase
prostate-derived STE20-like kinase (PSK) affects actin cytoskeletal
organization. Here, we demonstrate that PSK colocalizes with
microtubules; and that this localization is disrupted by the
microtubule depolymerizing agent nocodazole. The association of PSK
with microtubules results in the production of stabilized perinuclear
microtubule cables that are nocodazole-resistant and contain increased
levels of acetylated
The Prostate-derived Sterile 20-like Kinase (PSK) Regulates
Microtubule Organization and Stability*
,,¶
Department of Academic Surgery, GKT School
of Medicine and Dentistry, Rayne Institute, 123 Coldharbour Lane,
London SE5 9NU, United Kingdom, § The Ludwig Institute
for Cancer Research (University College London Branch),
London W1W 7BS, United Kingdom, and the Department of Biochemistry
and Molecular Biology, University College London, Gower Street,
London WC1E 6BT, United Kingdom
-tubulin. Kinase-defective PSK (K57A) or the C
terminus of PSK (amino acids 745-1235) lacking the kinase domain are
sufficient for microtubule binding and stabilization, demonstrating
that the catalytic activity of the protein is not required. The
localization of PSK to microtubules occurs via its C terminus, and PSK
binds and phosphorylates - and 
-tubulin in vitro. The
N terminus of PSK (1-940) is unable to bind or stabilize microtubules,
demonstrating that PSK must associate with microtubules for their
reorganization to occur. These results demonstrate that PSK interacts
with microtubules and affects their organization and stability
independently of PSK kinase activity.
*
This research was supported by the Biotechnology and
Biological Sciences Research Council, UK (Grant 29/C14086), the
Association for International Cancer Research, St. Andrews, Scotland,
the Ludwig Institute for Cancer Research, and by a donation from Laura Price.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.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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