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J. Biol. Chem., Vol. 277, Issue 8, 6214-6222, February 22, 2002
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From the § Diabetes Research Laboratory, Winthrop
University Hospital, Mineola, New York 11501, the
Recent studies from our laboratory have shown
that insulin stimulates myosin-bound phosphatase (MBP) in vascular
smooth muscle cells (VSMCs) by decreasing site-specific phosphorylation
of the myosin-bound subunit (MBS) of MBP via nitric oxide/cGMP-mediated Rho/Rho kinase inactivation. Here we tested potential interactions between Rho kinase and insulin signaling pathways. In control VSMCs,
insulin inactivates ROK-
Active Rho Kinase (ROK-
) Associates with Insulin Receptor
Substrate-1 and Inhibits Insulin Signaling in Vascular Smooth Muscle
Cells*
§¶,
, School of Medicine, State University of New York,
Stony Brook, New York 11794, the First Department of
Internal Medicine, Mie University School of Medicine, Mie 514-8507, Japan, and the ** Institut fur Klinische Biochemie und
Pathobiochemie, Medizinische Universitatsklinik,
Wuerzburg D97080, Germany
, the major Rho kinase isoform in VSMCs, and
inhibits thrombin-induced increase in ROK- association with the
insulin receptor substrate-1 (IRS-1). Hypertension (in spontaneous
hypertensive rats) or expression of an active RhoAV14
up-regulates Rho kinase activity and increases ROK-/IRS-1
association resulting in IRS-1 serine phosphorylation that leads to
inhibition of both insulin-induced IRS-1 tyrosine phosphorylation and
phosphatidylinositol 3-kinase (PI3-kinase) activation. In contrast,
expression of dominant negative RhoA or cGMP-dependent
protein kinase type I inactivates Rho kinase, abolishes
ROK-/IRS-1 association, and potentiates insulin-induced tyrosine
phosphorylation and PI3-kinase activation leading to decreased
MBST695 phosphorylation and decreased MBP inhibition.
Collectively, these results suggest a novel function for ROK- in
insulin signal transduction at the level of IRS-1 and potential
cross-talk between cGMP-dependent protein kinase type I,
Rho/Rho kinase signaling, and insulin signaling at the level of
IRS-1/PI3-kinase.
*
This work was supported by a American Heart Association
Established Investigator grant, medical education funds from Winthrop University Hospital, and by Deutsche Forschungsgemeinschaft Grant SFB355.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 © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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