Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion channel trafficking.
Article Details
- CitationCopy to clipboard
Ninkovic M, Mitkovski M, Kohl T, Stuhmer W, Pardo LA
Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion channel trafficking.
FEBS Lett. 2012 Sep 21;586(19):3077-84. doi: 10.1016/j.febslet.2012.07.055. Epub 2012 Jul 25.
- PubMed ID
- 22841712 [ View in PubMed]
- Abstract
K(V)10.1 is a potassium channel expressed in brain and implicated in tumor progression. We have searched for proteins interacting with K(V)10.1 and identified Rabaptin-5, an effector of the Rab5 GTPase. Both proteins co-localize on large early endosomes induced by Rab5 hyperactivity. Silencing of Rabaptin-5 induces down-regulation of recycling of K(V)10.1 channel in transfected cells and reduction of K(V)10.1 current density in cells natively expressing K(V)10.1, indicating a role of Rabaptin-5 in channel trafficking. K(V)10.1 co-localizes, but does not physically interact, with Rab7 and Rab11. Our data highlights the complex control of the amount of K(V)10.1 channels on the cell surface.