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J. Biol. Chem., Vol. 277, Issue 6, 4317-4323, February 8, 2002
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From the We have previously shown that inhibiting
protein-tyrosine kinase increased whereas inhibiting
protein-tyrosine phosphatase (PTP) decreased renal outer medullary
potassium channel 1 (ROMK1) channel activity (1). We have now used
confocal microscopy, the patch clamp technique, and biotin labeling to
further examine the role of tyrosine phosphorylation in regulating
ROMK1 trafficking. Human embryonic kidney 293 cells were cotransfected
with c-Src and green fluorescent protein-ROMK1, which has the same
biophysical properties as those of ROMK1. Patch clamp studies have
shown that phenylarsine oxide (PAO), an inhibitor of PTP, decreased the
activity of ROMK1. Moreover, addition of PAO reduced the cell surface
localization of green fluorescent protein-ROMK1 detected by confocal
microscopy and diminished the surface ROMK1 density by 65% measured by
biotin labeling. Also, PAO treatment significantly increased the
phosphorylation of ROMK1. The notion that the effect of PAO is mediated
by stimulating tyrosine phosphorylation-induced endocytosis of ROMK1
has also been supported by findings that mutating the tyrosine residue 337 of ROMK1 to alanine abolished the effect of PAO. Finally, the
inhibitory effect of PAO on ROMK1 was completely blocked in the cells
co-transfected with dominant negative dynamin (dynaminK44A). This
indicates that the tyrosine phosphorylation-induced endocytosis of
ROMK1 is dynamin-dependent. We conclude that inhibiting PTP increases ROMK1 phosphorylation and results in a
dynamin-dependent internalization of the channel.
Inhibition of Protein-tyrosine Phosphatase Stimulates
the Dynamin-dependent Endocytosis of ROMK1*
,,,
Department of Pharmacology, New York
Medical College, Valhalla, New York 10595 and the
§ Department of Cellular and Molecular Physiology, Yale
University School of Medicine, New Haven, Connecticut 06510
*
The work was supported in part by National Institutes of
Health Grants DK 47402 and DK 54983.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, BSB Rm. 537, Valhalla, NY
10595. Tel.: 914-594-4120; Fax: 914-347-4956; E-mail:
wenhui_wang@nymc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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