Association of Src Tyrosine Kinase with a Human Potassium Channel Mediated by SH3 Domain-Reference-Cited by-同舟云学术

Association of Src Tyrosine Kinase with a Human Potassium Channel Mediated by SH3 Domain

Published:1996-12-20 Issue:5295 Volume:274 Page:2089-2091
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Holmes Todd C.¹,Fadool Debra A.¹,Ren Ruibao²,Levitan Irwin B.¹

Affiliation:

1. T. C. Holmes, D. A. Fadool, I. B. Levitan, Department of Biochemistry and Volen Center for Complex Systems, Brandeis University, Waltham, MA 02254, USA.

2. R. Ren, Department of Biology and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254, USA.

Abstract

The human Kv1.5 potassium channel (hKv1.5) contains proline-rich sequences identical to those that bind to Src homology 3 (SH3) domains. Direct association of the Src tyrosine kinase with cloned hKv1.5 and native hKv1.5 in human myocardium was observed. This interaction was mediated by the proline-rich motif of hKv1.5 and the SH3 domain of Src. Furthermore, hKv1.5 was tyrosine phosphorylated, and the channel current was suppressed, in cells coexpressing v-Src. These results provide direct biochemical evidence for a signaling complex composed of a potassium channel and a protein tyrosine kinase.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference31 articles.

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4. Holmes T. C., Fadool D. A., Levitan I. B., J. Neurosci. 16, 1581 (1996).

5. Protein Kinase Activity Closely Associated with a Reconstituted Calcium-Activated Potassium Channel

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