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PMID: 22000509 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

Mechanosensitive channels: what can they do and how do they do it?

Structure (London, England : 1993) ·Vol. 19 ·No. 10 ·2011-10-12 ·Pages 1356-69

Haswell ES, Phillips R, Rees DC

Abstract

While mechanobiological processes employ diverse mechanisms, at their heart are force-induced perturbations in the structure and dynamics of molecules capable of triggering subsequent events. Among the best characterized force-sensing systems are bacterial mechanosensitive channels. These channels reflect an intimate coupling of protein conformation with the mechanics of the surrounding membrane; the membrane serves as an adaptable sensor that responds to an input of applied force and converts it into an output signal, interpreted for the cell by mechanosensitive channels. The cell can exploit this information in a number of ways: ensuring cellular viability in the presence of osmotic stress and perhaps also serving as a signal transducer for membrane tension or other functions. This review focuses on the bacterial mechanosensitive channels of large (MscL) and small (MscS) conductance and their eukaryotic homologs, with an emphasis on the outstanding issues surrounding the function and mechanism of this fascinating class of molecules.

MeSH Terms
Arabidopsis/metabolism,physiology Cell Membrane/metabolism,physiology Computational Biology Escherichia coli/metabolism,physiology Escherichia coli Proteins/metabolism Eukaryota/metabolism,physiology Hydrophobic and Hydrophilic Interactions Ion Channel Gating/physiology Ion Channels/metabolism Mechanotransduction, Cellular Membrane Proteins/metabolism Mutagenesis, Site-Directed Osmotic Pressure Protein Conformation Protein Stability
Chemicals
Escherichia coli Proteins Ion Channels MSL2 protein, Arabidopsis Membrane Proteins MscL protein, E coli MscS protein, E coli
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Haswell Elizabeth S
Department of Biology, Washington University, St. Louis, MO 63130, USA. ehaswell@wustl.edu
Phillips Rob
Rees Douglas C
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Article Info
Journal
Structure (London, England : 1993)
Abbr.
Structure
ISSN
1878-4186
DOI
10.1016/j.str.2011.09.005
Email
ehaswell@wustl.edu
Published
2011-10-12
Pages
1356-69
Language
English
Region
United States
NLM ID
101087697
PMCID
PMC3203646
Subset
IM
Grants
NIGMS NIH HHS · R01 GM084211 · United States
NIGMS NIH HHS · R01 GM084211-04 · United States
NIGMS NIH HHS · GM-084211 · United States
External Links
PubMed source DOI: 10.1016/j.str.2011.09.005 PMC Full Text View journal details
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