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(Received for publication, February 23, 1996, and in revised form, June 18, 1996)
From the SPRK (also called PTK-1 and MLK-3), a member of
the mixed lineage kinase subfamily of (Ser/Thr) protein kinases,
encodes an amino-terminal SH3 domain followed by a kinase
catalytic domain, two leucine zippers interrupted by a short spacer, a
Rac/Cdc42 binding domain, and a long carboxyl-terminal proline-rich
region. We report herein that SPRK activates the stress-activated
protein kinases (SAPKs) but not ERK-1 during transient expression in
COS cells; the p38 kinase is activated modestly (1.3-2 fold) but
consistently. SPRK also activates cotransfected SEK-1/MKK-4, a dual
specificity kinase which phosphorylates and activates SAPK.
Reciprocally, expression of mutant, inactive SEK-1 inhibits completely
the basal and SPRK-activated SAPK activity. Immunoprecipitated
recombinant SPRK is able to phosphorylate and activate recombinant
SEK-1 in vitro to an extent comparable to that achieved by
MEK kinase-1. These results identify SPRK as a candidate upstream
activator of the stress-activated protein kinases, acting through the
phosphorylation and activation of SEK-1.
Volume 271, Number 32,
Issue of August 9, 1996
pp. 19025-19028
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
,
,
,
and
Diabetes Unit and Medical Service,
Massachusetts General Hospital, Boston, Massachusetts 02129 and the
Department of Medicine, Harvard Medical School, Boston, Massachusetts
02115, the ¶ Department of Physiology, Michigan State University,
East Lansing, Michigan 48824, the 
Department of Molecular
Biology, Genentech, Inc., South San Francisco, California 94080, the
'' Department of Molecular Biology, Yokohama City University School of
Medicine, 3-9 Fuku-ura Kanazawa-ku, Yokohama 236, Japan, and the
Howard Hughes Medical Institute and
Division of Hematology/Oncology, Children's Hospital and Dana Farber
Cancer Institute, Boston, Massachusetts 02115
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