title: Assembly domains in TRP channels.
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.
authors.affiliation: Institute for Biophysics, University of Linz, A-4040 Linz, Austria. rainer.schindl@jku.at
authors.forename: R
authors.initials: R
authors.lastname: Schindl
authors.forename: C
authors.initials: C
authors.lastname: Romanin
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D017487:Ankyrins / Q000737:chemistry; D015220:Calcium Channels / Q000737:chemistry; D003600:Cytosol / Q000378:metabolism; D004330:Drosophila; D006801:Humans; D008954:Models, Biological; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D050052:TRPC Cation Channels / Q000737:chemistry* / Q000502:physiology*; D050916:TRPV Cation Channels / Q000737:chemistry
chemical_list: D017487:Ankyrins; D015220:Calcium Channels; D050052:TRPC Cation Channels; C104603:TRPC3 cation channel; D050916:TRPV Cation Channels; C494482:TRPV1 protein, human; C492239:TRPV5 protein, human; C422827:TRPV6 protein, human