Referenced in: none

Automatically associated channels: Kv1.2

Title: Endocytosis as a mechanism for tyrosine kinase-dependent suppression of a voltage-gated potassium channel.

Authors: Edmund Nesti, Brian Everill, Anthony D Morielli

Journal, date & volume: Mol. Biol. Cell, 2004 Sep , 15, 4073-88

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/15215309

Abstract
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.