Primary cilium, cortactine, and Kv10.1 dynamics under confocal microscopy
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AuthorSánchez, José Manuel; Carretero, Irene; González, Jorge; Urrego, Diana; Stühmer, Walter; Pardo, Luis A.
Archivos de Medicina Universitaria
Kv10.1 channelPrimary ciliumCortactinAcetylated alpha-tubulinCanal Kv10.1Cilio primarioCortactinaAlfa-tubulina acetilada
José Manuel Sánchez, Irene Carretero, Jorge González, Diana Urrego, Walter Stühmer and Luis A. Pardo. Primary cilium, cortactine, and Kv10.1 dynamics under confocal microscopy. AMU. 2016; 4: 27-30
OBJECTIVES: It is believed that tumor cells expressing Kv10.1 channel acquire selective advantages that allow them to maintain chronic proliferation. The ciliary disassembly is a prerequisite to enter into the cell cycle, therefore our objective was to find correlations between primary cilium disassembly and the Kv10.1 channel through the Kv10.1 cortactin binding site. Methods: Wild type Kv10.1, as well as the mutant form lacking the binding site to the cytoskeleton protein cortactin, were overexpressed in RPE-TERT cell line. The effect on ciliary disassembly of such overexpression forms was imaging using confocal microscopy. Results: Kv10.1 wild type overexpression induced disassembly of the primary cilium and alteration of the cytoskeleton, which corresponded to overproduction of filament structures positive to α-tubulin acetylated in the cytoplasm. Overexpression of mutated Kv10.1 did not show this pattern, nor the untreated cells. ConclusionS: This data suggests that Kv10.1 channel could be interfering with the cilium formation, and thus influences the cell cycle in a way that cortactine binding site is not involved. That should be furtherly studied because due to its possible implications in cancer.