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Updated: May 20, 2026

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
Published on: July 13, 2013
Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion channel trafficking
Milena Ninkovic1, Mišo Mitkovski, Tobias Kohl
1Department of Molecular Biology of Neuronal Signals, Max-Planck-Institute of Experimental Medicine, Göttingen, Germany.
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.
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