NDLI: Homo- and heteromeric assembly of TRP channel subunits

Content Provider	Springer Nature Link
Author	Schaefer, Michael
Copyright Year	2005
Abstract	Mammalian homologues of the Drosophila melanogaster transient receptor potential (TRP) channels are the second largest cation channel family within the superfamily of hexahelical cation channels. Most mammalian TRP channels function as homooligomers and mediate mono- or divalent cation entry upon activation by a variety of stimuli. Because native TRP channels may be multimeric proteins of possibly complex composition, it is difficult to compare cation conductances in native tissues to those of clearly defined homomeric TRP channel complexes in living cells. Therefore, the possibility of heteromeric TRP channel assembly has been investigated in recent years by several groups. As a major conclusion of these studies, most heteromeric TRP channel complexes appear to consist of subunit combinations only within relatively narrow confines of phylogenetic subfamilies. Although the general capability of heteromer formation between closely related TRP channel subunits is now clearly established, we are only beginning to understand whether these heteromeric complexes are of physiological significance. This review summarizes the current knowledge on the promiscuity and specificity of the assembly of channel complexes composed of TRPC-, TRPV- and TRPM-subunits of mammalian TRP channels.
Starting Page	35
Ending Page	42
Page Count	8
File Format	PDF
ISSN	00316768
Journal	Pflügers Archiv
Volume Number	451
Issue Number	1
e-ISSN	14322013
Language	English
Publisher	Springer-Verlag
Publisher Date	2005-06-22
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Calcium channels Transient receptor potential protein, Drosophila Vanilloid receptors Protein structure, Quaternary Fluorescence resonance energy transfer
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Clinical Biochemistry

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