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MscL: channeling membrane tension

Walton, Troy A. and Idigo, Chinenye A. and Herrera, Nadia and Rees, Douglas C. (2015) MscL: channeling membrane tension. Pflügers Archiv European Journal of Physiology, 467 (1). pp. 15-25. ISSN 0031-6768. PMCID PMC4246047. https://resolver.caltech.edu/CaltechAUTHORS:20140604-130904300

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Abstract

Mechanosensitive channels are integral components for the response of bacteria to osmotic shock. The mechanosensitive channel of large conductance (MscL) responds to extreme turgor pressure increase that would otherwise lyse the cellular membrane. MscL has been studied as a model mechanosensitive channel using both structural and functional approaches. We will summarize the structural data and discuss outstanding questions surrounding the gating mechanism of this homo-oligomeric channel that has ~3 nS conductance. Specifically, we will explore the following: (1) the variability in oligomeric state that has been observed, (2) the open pore size measurements, and (3) the role of the C-terminal coiled coil domain for channel function. The oligomeric state of MscL has been characterized using various techniques, with a pentamer being the predominant form; however, the presence of mixtures of oligomers in the membrane is still uncertain. In the absence of structural data for the open state of MscL, the diameter of the open state pore has been estimated by several different approaches, leading to a current estimate between 25 and 30 Å. While the C-terminal domain is highly conserved among MscL homologues, it is not required for activity in vivo or in vitro. This domain is likely to remain intact during the gating transition and perform a filtering function that retains valuable osmolytes in the cytosol. Overall, studies of MscL have provided significant insight to the field, and serve as a paradigm for the analysis of non-homologous, eukaryotic mechanosensitive channel proteins.


Item Type:Article
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URLURL TypeDescription
http://dx.doi.org/10.1007/s00424-014-1535-xDOIArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4246047/PubMed CentralArticle
http://rdcu.be/tteGPublisherFree ReadCube access
ORCID:
AuthorORCID
Herrera, Nadia0000-0003-4157-9429
Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 2014 Springer-Verlag Berlin Heidelberg. Received: 7 April 2014. Revised: 6 May 2014. Accepted: 9 May 2014. We thank Chris Gandhi, Rob Phillips, Elizabeth Haswell, and Ian Booth for stimulating discussions. N. Herrera is the recipient of a Gilliam graduate fellowship of the Howard Hughes Medical Institute, and C. Idigo received support from the US National Institutes of Health/National Research Service Award T32 GM07616. Research in the authors' lab was supported by US National Institutes of Health grant GM84211.
Funders:
Funding AgencyGrant Number
NIH Predoctoral FellowshipT32 GM076165
NIHGM84211
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Subject Keywords:Mechanosensitive channels. Stretch activated channels. Bacterial channels. Hypo-osmotic stress response. Turgor pressure
Issue or Number:1
PubMed Central ID:PMC4246047
Record Number:CaltechAUTHORS:20140604-130904300
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20140604-130904300
Official Citation:Walton, T.A., Idigo, C.A., Herrera, N. et al. Pflugers Arch - Eur J Physiol (2015) 467: 15. doi:10.1007/s00424-014-1535-x
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:46075
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:04 Jun 2014 21:55
Last Modified:10 Jun 2020 23:41

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