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A more recent version of this article appeared on September 1, 2004
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Submitted on November 5, 2003
Revised on June 7, 2004
Accepted on June 11, 2004
The University of Vermont College of Medicine, Burlington, VT 05405
Monitoring Editor: Tony Hunter
The voltage gated potassium channel Kv1.2 undergoes tyrosine phosphorylation dependent suppression of its ionic current. However, little is known about the physical mechanism behind that process. We have found that the Kv1.2 alpha-subunit protein undergoes endocytosis in response to the same stimuli that evoke suppression of Kv1.2 ionic current. The process is tyrosine phosphorylation dependent since the same tyrosine to phenylalanine mutation in the N-terminus of Kv1.2 that confers resistance to channel suppression (Y132F) also confers resistance to channel endocytosis. Overexpression of a dominant negative form of dynamin blocked stimulus induced Kv1.2 endocytosis and also blocked suppression of Kv1.2 ionic current. These data indicate that endocytosis of Kv1.2 from the cell surface is a key mechanism for channel suppression by tyrosine kinases.
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