Endocytosis as a Mechanism for Tyrosine Kinase-dependent Suppression of a Voltage-gated Potassium Channel

@article{citeulike:2789730, 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. 10.1091/mbc.E03-11-0788}, author = {Nesti, Edmund and Everill, Brian and Morielli, Anthony D. }, citeulike-article-id = {2789730}, doi = {10.1091/mbc.E03-11-0788}, journal = {Mol. Biol. Cell}, keywords = {endocytosis, kv, phosphorylation}, month = {September}, number = {9}, pages = {4073--4088}, posted-at = {2008-05-12 16:23:44}, priority = {0}, title = {Endocytosis as a Mechanism for Tyrosine Kinase-dependent Suppression of a Voltage-gated Potassium Channel}, url = {http://dx.doi.org/10.1091/mbc.E03-11-0788}, volume = {15}, year = {2004} }

TY - JOUR ID - citeulike:2789730 L3 - citeulike-article-id:2789730 TI - Endocytosis as a Mechanism for Tyrosine Kinase-dependent Suppression of a Voltage-gated Potassium Channel JF - Mol. Biol. Cell VL - 15 IS - 9 SP - 4073 EP - 4088 N2 - 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. 10.1091/mbc.E03-11-0788 KW - endocytosis KW - kv KW - phosphorylation AU - Nesti, Edmund AU - Everill, Brian AU - Morielli, Anthony PY - 2004/09/01/ UR - http://dx.doi.org/10.1091/mbc.E03-11-0788 ER -