PubMed 22841712

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Title: Physical and functional interaction of K(V)10.1 with Rabaptin-5 impacts ion channel trafficking.

Authors: Milena Ninkovic, Mišo Mitkovski, Tobias Kohl, Walter Stühmer, Luis A Pardo

Journal, date & volume: FEBS Lett., 2012 Jul 25 , ,

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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. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: Rabaptin-5physically interacts with Kv10.1 by anti bait coimmunoprecipitation (View interaction) Rabaptin-5physically interacts with Rabaptin-5 by two hybrid (View interaction) Kv10.1physically interacts with Kv10.1 by two hybrid (View interaction) Kv10.1physically interacts with Rabaptin-5 by anti bait coimmunoprecipitation (View Interaction: 1, 2) RAB11 and Kv10.1colocalize by fluorescence microscopy (View interaction) Kv10.1 and Rabaptin-5colocalize by fluorescence microscopy (View interaction) Kv10.1physically interacts with Rabaptin-5 by two hybrid (View Interaction: 1, 2) Kv10.1 and RAB7colocalize by fluorescence microscopy (View interaction).