Temperature Sensitivity of Two-Pore (K2P) Potassium Channels

Eve R. Schneider; Evan O. Anderson; Elena O. Gracheva; Sviatoslav N. Bagriantsev

doi:10.1016/B978-0-12-800181-3.00005-1

Temperature Sensitivity of Two-Pore (K_2P) Potassium Channels

Eve R. Schneider, Evan O. Anderson, Elena O. Gracheva, Sviatoslav N. Bagriantsev

Biology

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

51 Scopus citations

Abstract

At normal body temperature, the two-pore potassium channels TREK-1 (K_2P2.1/KCNK2), TREK-2 (K_2P10.1/KCNK10), and TRAAK (K_2P4.1/KCNK2) regulate cellular excitability by providing voltage-independent leak of potassium. Heat dramatically potentiates K_2P channel activity and further affects excitation. This review focuses on the current understanding of the physiological role of heat-activated K_2P current, and discusses the molecular mechanism of temperature gating in TREK-1, TREK-2, and TRAAK.

Original language	English
Title of host publication	Current Topics in Membranes
Pages	113-133
Number of pages	21
Edition	1
DOIs	https://doi.org/10.1016/B978-0-12-800181-3.00005-1
State	Published - 2014

Publication series

Name	Current Topics in Membranes
Number	1
Volume	74
ISSN (Print)	1063-5823

Bibliographical note

Publisher Copyright:
© 2014 Elsevier Inc.

Keywords

Ion channel
K
Potassium channel
TRAAK
TREK-1
TREK-2
Thermosensitivity
Thermotransduction
Two-pore

ASJC Scopus subject areas

Molecular Biology
Cell Biology

Access to Document

10.1016/B978-0-12-800181-3.00005-1

Cite this

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title = "Temperature Sensitivity of Two-Pore (K2P) Potassium Channels",

abstract = "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.",

keywords = "Ion channel, K, Potassium channel, TRAAK, TREK-1, TREK-2, Thermosensitivity, Thermotransduction, Two-pore",

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AU - Anderson, Evan O.

AU - Gracheva, Elena O.

AU - Bagriantsev, Sviatoslav N.

PY - 2014

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AB - 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.

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KW - K

KW - Potassium channel

KW - TRAAK

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KW - TREK-2

KW - Thermosensitivity

KW - Thermotransduction

KW - Two-pore

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