HomeAbout

SIGN IN   Advanced Search










 
Browse Illustration
Receptor-Operated Cation Entry--More Than Esoteric Terminology?

Many hormones and neurotransmitters elicit an increase in the intracellular calcium concentration by binding to phospholipase C–linked G protein–coupled receptors. Activated receptors signal to calcium-permeable cation channels in the plasma membrane, which are distinct from those engaged by emptying of intracellular stores of calcium. The TRPC family of the mammalian homologs of the Drosophila transient receptor potential (TRP) cation channel represents likely molecular correlates underlying receptor-operated cation entry. While all TRPC family members are gated in a phospholipase C–dependent manner, the exact activation mechanism still remains elusive, although lipids such as diacylglycerol and polyunsaturated fatty acids are potential diffusible messengers. Functional TRPC channel complexes in the plasma membrane are thought to be composed of four distinct subunits whose stoichiometry and composition under physiological conditions are still largely unknown. However, recent progress in defining the combinatorial rules of TRPC channel assembly may lead to the identification of TRPC-dependent ion fluxes in living cells. Because of the large number of TRP proteins and their frequently overlapping functional characteristics, the central question is whether TRP proteins are functionally interchangeable or whether unique physiological roles can be ascribed to them. Receptor-operated cation entry is critically involved in the control of airway and vascular smooth muscle tone; hence, TRPC proteins are promising new drug targets.

Rate this Resource:
1 = not useful, 5 = very useful

Please be the first to rate this resource.


Subscribe and
View Resource

Classifications


Resource Type: Diagram, Illustration, Journal article/Issue, Review
Audience Level: Undergraduate upper division 15-16, Graduate, Professional (degree program)

Author and Copyright


Authors and Editors: Thomas Gudermann of Institut fur Pharmakologie und Toxikologie, Philipps-Universitat Marburg, Michael Mederos y Schnitzler of Institut fur Pharmakologie und Toxikologie, Philipps-Universitat Marburg, Alexander Dietrich of Institut fur Pharmakologie und Toxikologie, Philipps-Universitat Marburg
Publisher: American Association for the Advancement of Science
Format: application/pdf, image/gif, image/jpeg, text/html
Copyright and other restrictions: Yes
Cost: Yes

Comments


» Sign In or register to post comments.


Collection:
STKE/Science Signaling


     
   

SITE MAP | CONTACT | POLICIES

Triple A S National Science Foundation Naitonal Science Digital Library Pathway
Funded by the individual BEN Collaborators and grants from the
National Science Foundation [DUE 0085840 / DUE 0226185 / DUE 0532797 / DUE 0734995]

This website is a National Science Digital Library (NSDL) Pathway.
Copyright © 2019. American Association for the Advancement of Science. All Rights Reserved.