title: Does sumoylation control K2P1/TWIK1 background K+ channels?
abstract: A novel model for the regulation of cell excitability has recently been proposed. It originates from the observation that the background K(+) channel K2P1 (TWIK1) may be silenced by sumoylation in Xenopus oocytes and that inactivation of the putative sumoylation site (mutation K274E) gives rise to robust current expression in transfected COS-7 cells. Here, we show that only the mutation K274E, and not K274R, is associated with an increase of K2P1 current density, suggesting a charge effect of K274E. Furthermore, we failed to observe any band shift by western blot analysis that would confirm an eventual sumoylation of K2P1 in COS-7 cells and oocytes.
authors: Institut de Pharmacologie Moléculaire et Cellulaire, CNRS UMR6097, Institut Paul Hamel, 660, route des lucioles, 06560 Valbonne, France.
authors: Sylvain
authors: S
authors: Feliciangeli
authors: Saïd
authors: S
authors: Bendahhou
authors: Guillaume
authors: G
authors: Sandoz
authors: Pierre
authors: P
authors: Gounon
authors: Markus
authors: M
authors: Reichold
authors: Richard
authors: R
authors: Warth
authors: Michel
authors: M
authors: Lazdunski
authors: Jacques
authors: J
authors: Barhanin
authors: Florian
authors: F
authors: Lesage
mesh_terms: D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D006801:Humans; D024683:Potassium Channels, Tandem Pore Domain / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*; D014982:Xenopus laevis
chemical_list: C109137:KCNK1 protein, human; D024683:Potassium Channels, Tandem Pore Domain; D025841:Small Ubiquitin-Related Modifier Proteins