Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 15, Issue 9, Pages 4073-4088Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E03-11-0788
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Funding
- NCI NIH HHS [P30CA22435, P30 CA022435] Funding Source: Medline
- NCRR NIH HHS [P20 RR016435, 1P20RR16435] Funding Source: Medline
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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.
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