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PMID: 1700306 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Mechanosensitive ion channels of E. coli activated by amphipaths.

Nature ·Vol. 348 ·No. 6298 ·1990-11-15 ·Pages 261-3

Martinac B, Adler J, Kung C

Abstract

Mechanosensitive channels have been found in more than 30 cell types, including bacterial, yeast, plant and animal cells. Whether tension is transferred to the channel through the lipid bilayer and/or underlying cytoskeleton is not clear. Using the patch-clamp method, we found that amphipathic compounds, which are molecules having hydrophobic and hydrophilic character with positive, negative or no net electric charge at pH 7, could slowly activate the mechanosensitive channels of giant Escherichia coli spheroplasts, with effectiveness proportional to their lipid solubility. The cationic or anionic amphipaths were able to compensate for each other's effect. After a channel was activated by an amphipath of one charge, if that amphipath was gradually replaced by one with the opposite charge, the channel first inactivated before reactivating. These findings support the view that the mechanical gating force can come from the surrounding lipids.

MeSH Terms
Cell Membrane/physiology Chemical Phenomena Chemistry, Physical Chlorpromazine/pharmacology Electrochemistry Escherichia coli/physiology Hydrogen-Ion Concentration Ion Channel Gating/physiology Ion Channels/drug effects,physiology Membrane Lipids Picrates/pharmacology Solubility
Chemicals
Ion Channels Membrane Lipids Picrates picric acid Chlorpromazine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Martinac B
Laboratory of Molecular Biology, University of Wisconsin, Madison 53706.
Adler J
Kung C
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1990-11-15
Pages
261-3
Language
English
Region
England
NLM ID
0410462
Subset
IM
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