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Originally published In Press as doi:10.1074/jbc.M208448200 on October 1, 2002

J. Biol. Chem., Vol. 277, Issue 50, 48130-48138, December 13, 2002
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Modulation of the ERG K+ Current by the Tyrosine Phosphatase, SHP-1*

Francisco S. CayabyabDagger §, Florence W. L. TsuiDagger ||, and Lyanne C. SchlichterDagger §**

From the Dagger  Cellular and Molecular Biology Division, Toronto Western Research Institute, the § Department of Physiology and the || Department of Immunology, University of Toronto, Toronto, Ontario M5T 2S8, Canada

We reported previously (Cayabyab, F. S., and Schlichter, L. C. (2002) J. Biol. Chem. 277, 13673-13681) a functional interaction between the ERG-1 K+ channel and Src tyrosine kinase, which increased the current. We now show that the tyrosine phosphatase, SHP-1, which is present in microglia, is increased after brain damage, and is activated by colony-stimulating factor-1, associates with ERG-1 and regulates the current. Patch clamp recordings from the MLS-9 microglia cells were made with pipette solutions containing a recombinant SHP-1 protein: wild type (SHP-1 wild type (wt)), catalytically active (SHP-1 S6), or the substrate-trapping mutant (SHP-1 Cys right-arrow Ser). SHP-1 wt and SHP-1 S6 proteins decreased the current, an effect that was reversed by the phosphatase inhibitor, pervanadate, whereas SHP-1 Cys right-arrow Ser increased the current. Moreover, transient transfection with cDNA for SHP-1 wt or SHP-1 S6 decreased the ERG current without decreasing the protein level. Tyrosine phosphorylation of ERG-1 was decreased by transfection with SHP-1 wt and increased by SHP-1 Cys right-arrow Ser. The decrease in current by active SHP-1 was partly attributed to changes in the voltage dependence of activation and steady-state conductance, whereas inactivation kinetics and voltage dependence were not affected. Our results show that ERG-1 is a SHP-1 substrate constituting the first report that an ion current is regulated by SHP-1.


* This work was supported in part by Heart and Stroke Foundation of Ontario Grant T-3726, the Canadian Institutes for Health Research Grant MT-13657 (to L. C. S.), and National Cancer Institute of Canada Grant 11044 (to F. W. L. T.).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.

Recipient of a Heart and Stroke Foundation of Canada Research traineeship. Present address: School of Kinesiology, Faculty of Applied Sciences, Simon Fraser University, Academic Quadrangle K9626, 8888 University Drive, Burnaby, British Columbia V5A 1S6, Canada.

** To whom correspondence should be addressed: MC 9-415, Toronto Western Hospital, 399 Bathurst Street, Toronto, Ontario M5T 2S8, Canada. Tel.: 416-603-5800 (ext. 2052); Fax: 416-603-5745; E-mail: schlicht@uhnres.utoronto.ca.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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