Does sumoylation control K2P1/TWIK1 background K+ channels?

Article Details

Citation

Feliciangeli S, Bendahhou S, Sandoz G, Gounon P, Reichold M, Warth R, Lazdunski M, Barhanin J, Lesage F

Does sumoylation control K2P1/TWIK1 background K+ channels?

Cell. 2007 Aug 10;130(3):563-9.

PubMed ID
17693262 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Potassium channel subfamily K member 1O00180Details