Insights into the roles of conserved and divergent residues in the ankyrin repeats of TRPV ion channels.

Christopher B. Phelps, Erik Procko, Polina V. Lishko, Ruiqi R. Wang, Rachelle Gaudet

Research output: Contribution to journalArticlepeer-review

Abstract

Ion channels are often modulated by intracellular calcium levels. TRPV1, a channel responsible for the burning pain sensation in response to heat, acid or capsaicin, is desensitized at high intracellular calcium concentrations. We recently identified a multiligand-binding site in the N-terminal ankyrin repeat domain (ARD) of TRPV1 that binds ATP and sensitizes the channel. Calcium-calmodulin binds the same site and is necessary for calcium-mediated TRPV1 desensitization. Here, we examine in more detail the conservation of this TRPV1 multiligand-binding site in other species. Furthermore, using sequence analysis, we determine that the unusually twisted shape of the TRPV1-ARD is likely conserved in other TRPV channels, but not in the ARDs of other TRP subfamilies.

Original languageEnglish (US)
Pages (from-to)148-151
Number of pages4
JournalChannels (Austin, Tex.)
Volume1
Issue number3
DOIs
StatePublished - 2007
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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