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Prokaryotic Mechanosensitive Channels

Strop, Pavel and Bass, Randal and Rees, Douglas C. (2003) Prokaryotic Mechanosensitive Channels. In: Membrane Proteins. Advances in Protein Chemistry. No.63. Elsevier , New York, NY, pp. 177-209. ISBN 978-0-12-034263-1. https://resolver.caltech.edu/CaltechAUTHORS:20141212-145528968

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Abstract

Mechanosensitive ion channels are integral membrane proteins that open and close in response to mechanical stress applied either directly to the cell membrane (in the case of intrinsically mechanosensitive channels) or indirectly, through forces applied to other cytoskeletal components. Cellular phenomena mediated by mechanosensitive channels include touch, hearing, cardiovascular tone, detection of gravity, pressure sensation, pain perception, and osmoregulation. Mechanosensirive channels are quite diverse both physiologically and structurally and have been discovered in all fundamental branches of the phylogenetic tree, Eubacteria, Eukarya, and Archaea. Eukaryotic mechanosensitive channels include the TRPV subclass of the Transient Receptor Potential channel family: the TREK-1 and TRAAK members of the two-pore domain potassium channel family K2p; and the DEG/ENaC superfamily composed of degenerins, eptithelial sodium channels, and acid-sensing channels that have been implicated in the touch response of nematodes. Although many of these channels, including the degenerins and the yet-to-be identified channel receptors involved in hearing, appear to have an obligatory requirement for cytoskeletal coupling, others, such as the TREK-1 and TRAAK channels, exhibit intrisinic mechanosensitive activity.


Item Type:Book Section
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/S0065-3233(03)63008-1DOIArticle
http://www.sciencedirect.com/science/article/pii/S0065323303630081PublisherArticle
ORCID:
AuthorORCID
Rees, Douglas C.0000-0003-4073-1185
Contact Email Address:phoebe@caltech.edu
Additional Information:Copyright © 2003 Elsevier. Discussions with Sidney Wang, Meg Barclay, Rober Spencer, Kaspar Locher, Geoffrey Chang, Dennis Dougherty, Henry Lester, Rob Phillips, and Eduardo Perozo are greatly appreciated. This work was supported in part by NIH grants GM62532 to D.C.R. and GM20705 to R.B.B.
Funders:
Funding AgencyGrant Number
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
NIHGM62532
NIHGM20705
Series Name:Advances in Protein Chemistry
Issue or Number:63
Record Number:CaltechAUTHORS:20141212-145528968
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20141212-145528968
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52789
Collection:CaltechAUTHORS
Deposited By: SWORD User
Deposited On:22 Dec 2014 19:54
Last Modified:03 Oct 2019 07:44

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