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J. Biol. Chem., Vol. 276, Issue 10, 7156-7163, March 9, 2001
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From the We have used the two-electrode voltage clamp
technique and the patch clamp technique to investigate the
regulation of ROMK1 channels by protein-tyrosine phosphatase (PTP) and
protein-tyrosine kinase (PTK) in oocytes coexpressing ROMK1 and cSrc.
Western blot analysis detected the presence of the endogenous PTP-1D
isoform in the oocytes. Addition of phenylarsine oxide (PAO), an
inhibitor of PTP, reversibly reduced K+ current by
55% in oocytes coinjected with ROMK1 and cSrc. In contrast, PAO had no
significant effect on K+ current in oocytes injected with
ROMK1 alone. Moreover, application of herbimycin A, an inhibitor of
PTK, increased K+ current by 120% and completely abolished
the effect of PAO in oocytes coexpressing ROMK1 and cSrc. The effects
of herbimycin A and PAO were absent in oocytes expressing the ROMK1
mutant R1Y337A in which the tyrosine residue at position 337 was
mutated to alanine. However, addition of exogenous cSrc had no
significant effect on the activity of ROMK1 channels in inside-out
patches. Moreover, the effect of PAO was completely abolished by
treatment of oocytes with 20% sucrose and 250 µg/ml concanavalin A,
agents that inhibit the endocytosis of ROMK1 channels. Furthermore, the
effect of herbimycin A is absent in the oocytes pretreated with either
colchicine, an inhibitor of microtubules, or taxol, an agent
that freezes microtubules. We conclude that PTP and PTK play an
important role in regulating ROMK1 channels. Inhibiting PTP increases
the internalization of ROMK1 channels, whereas blocking PTK stimulates
the insertion of ROMK1 channels.
Regulation of ROMK1 Channels by Protein-tyrosine
Kinase and -tyrosine Phosphatase*
,,,,,,
Department of Pharmacology, New
York Medical College, Valhalla, New York 10595, the
§ Department of Cellular and Molecular Physiology, Yale
University School of Medicine, New Haven, Connecticut 06510, and the
¶ Department of Physiology, Cornell University Medical College,
New York, New York 10021
*
This work was supported by National Institutes of Health
Grants DK 47402 and DK 54983 (to W.-H. W.), DK 17433 (to G. G.), and
DK 37605 (to S. C. H.).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.
To whom correspondence should be addressed: Dept. of
Pharmacology, New York Medical College, Valhalla, NY 10595. Tel.:
914-594-4120; Fax: 914-347-4956; E-mail: wenhui_wang@nymc.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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