| First Author | Ninkovic M | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 19 | Pages | 3077-84 |
| PubMed ID | 22841712 | Mgi Jnum | J:188709 |
| Mgi Id | MGI:5441649 | Doi | 10.1016/j.febslet.2012.07.055 |
| Citation | Ninkovic M, et al. (2012) Physical and functional interaction of K(V)10.1 with Rabaptin-5 impacts ion channel trafficking. FEBS Lett 586(19):3077-84 |
| abstractText | 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). |
