Publication Date:
1996-12-20
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, T C -- Fadool, D A -- Ren, R -- Levitan, I B -- F32 NS009952/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2089-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Volen Center for Complex Systems, Brandeis University, Waltham, MA 02254, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953041" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Cell Line
;
Cloning, Molecular
;
Humans
;
Kv1.5 Potassium Channel
;
Molecular Sequence Data
;
Myocardium/chemistry
;
Oncogene Protein pp60(v-src)/metabolism
;
Patch-Clamp Techniques
;
Phosphorylation
;
Phosphotyrosine/metabolism
;
Potassium Channels/chemistry/*metabolism
;
*Potassium Channels, Voltage-Gated
;
Recombinant Fusion Proteins/metabolism
;
Signal Transduction
;
Transfection
;
src Homology Domains/*physiology
;
src-Family Kinases/chemistry/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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