At normal body temperature, the two-pore potassium channels TREK-1 (K2P2.1/KCNK2), TREK-2 (K2P10.1/KCNK10), and TRAAK (K2P4.1/KCNK2) regulate cellular excitability by providing voltage-independent leak of potassium. Heat dramatically potentiates K2P channel activity and further affects excitation. This review focuses on the current understanding of the physiological role of heat-activated K2P current, and discusses the molecular mechanism of temperature gating in TREK-1, TREK-2, and TRAAK.
|Title of host publication||Current Topics in Membranes|
|Number of pages||21|
|State||Published - 2014|
|Name||Current Topics in Membranes|
Bibliographical noteFunding Information:
We thank Willem Laursen for comments on the manuscript. This work was supported by a grant from the American Heart Association (14SDG17880015) to S.N.B., and by fellowships from the Beckman Foundation and Alfred P. Sloan Foundation to E.O.G. Correspondence should be addressed to S.N.B. ( email@example.com ).
© 2014 Elsevier Inc.
- Ion channel
- Potassium channel
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology