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Vol. 15, Issue 9, 4073-4088, September 2004
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The University of Vermont College of Medicine, Burlington, VT 05405
Submitted November 5, 2003;
Revised June 7, 2004;
Accepted June 11, 2004
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 because 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.
* Corresponding author. E-mail address: anthony.morielli{at}uvm.edu.
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