TRPV1 splice variants: structure and function

Front Biosci (Landmark Ed). 2010 Jun 1;15:872-82. doi: 10.2741/3651.

Abstract

The capsaicin receptor (TRPV1) is a non-selective cation channel predominantly expressed in specialized sensory neurons that detect painful stimuli. Although its many functional roles continue to be revealed, it has been confirmed to play a critical role in the perception of peripheral inflammatory hyperalgesia and pain. TRPV1 not only is sensitized and/or activated under a wide range of conditions including inflammation and nerve injury but also undergoes changes in expressed levels in response to these same pathologic conditions. Just as our understanding of the structural requirements of TRPV1 activation has grown, there is evidence that TRPV1 forms heteromeric channel complexes. This review is focused on the structural and functional consequence of TRPV1 splice variants: VR.5'sv, TRPV1b/beta and TRPV1var. Through their co-expression and formation of heteromeric complexes with TRPV1, they have been shown to modulate TRPV1 activation. Moreover, TRPV1 splice variant subunits may also contribute unique properties of activation such as the detection of hypertonic conditions.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alternative Splicing*
  • Animals
  • Diabetes Mellitus / genetics
  • Diabetes Mellitus / physiopathology
  • Gene Expression
  • Humans
  • Pain / genetics
  • Pain / physiopathology
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / physiology
  • Protein Multimerization
  • Sensory Receptor Cells / metabolism
  • TRPV Cation Channels / chemistry
  • TRPV Cation Channels / genetics*
  • TRPV Cation Channels / physiology*

Substances

  • Protein Isoforms
  • TRPV Cation Channels
  • TRPV1 protein, human