High temperature sensitivity is intrinsic to voltage-gated potassium channels

Fan Yang, Jie Zheng

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

Temperature-sensitive transient receptor potential (TRP) ion channels are members of the large tetrameric cation channels superfamily but are considered to be uniquely sensitive to heat, which has been presumed to be due to the existence of an unidentified temperature-sensing domain. Here we report that the homologous voltage-gated potassium (Kv) channels also exhibit high temperature sensitivity comparable to that of TRPV1, which is detectable under specific conditions when the voltage sensor is functionally decoupled from the activation gate through either intrinsic mechanisms or mutations. Interestingly, mutations could tune Shaker channel to be either heat-activated or heat-deactivated. Therefore, high temperature sensitivity is intrinsic to both TRP and Kv channels. Our findings suggest important physiological roles of heat-induced variation in Kv channel activities. Mechanistically our findings indicate that temperature-sensing TRP channels may not contain a specialized heat-sensor domain; instead, non-obligatory allosteric gating permits the intrinsic heat sensitivity to drive channel activation, allowing temperature-sensitive TRP channels to function as polymodal nociceptors.

Original languageEnglish (US)
Pages (from-to)e03255
JournaleLife
Volume3
DOIs
StatePublished - 2014

Keywords

  • allosteric coupling
  • conformational changes
  • gating
  • potassium channel
  • temperature sensing
  • TRP channel

ASJC Scopus subject areas

  • Medicine(all)

Fingerprint Dive into the research topics of 'High temperature sensitivity is intrinsic to voltage-gated potassium channels'. Together they form a unique fingerprint.

Cite this