Assembly domains in TRP channels

Biochem Soc Trans. 2007 Feb;35(Pt 1):84-5. doi: 10.1042/BST0350084.

Abstract

The large family of mammalian TRP (transient receptor potential) ion channels encompasses diverse sensory functions. TRP proteins consist of six transmembrane domains, with a pore-loop motif between the fifth and sixth domains and cytosolic N- and C-termini. The intracellular strands not only interact with various proteins and lipids, but also include essential multimerization regions. This review summarizes the current knowledge of the intrinsic assembly domains that assure tetrameric TRP channel formation.

Publication types

  • Review

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Ankyrins / chemistry
  • Calcium Channels / chemistry
  • Cytosol / metabolism
  • Drosophila
  • Humans
  • Models, Biological
  • Protein Binding
  • Protein Structure, Tertiary
  • TRPC Cation Channels / chemistry*
  • TRPC Cation Channels / physiology*
  • TRPV Cation Channels / chemistry

Substances

  • Ankyrins
  • Calcium Channels
  • TRPC Cation Channels
  • TRPC3 cation channel
  • TRPV Cation Channels
  • TRPV1 protein, human
  • TRPV5 protein, human
  • TRPV6 protein, human