Gramicidin A channels switch between stretch activation and stretch inactivation depending on bilayer thickness

Boris Martinac, Owen Hamill

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

The patch clamp-liposome technique was used to examine the stretch sensitivity of a model membrane ion channel, gramicidin A, in membrane patches of different bilayer thickness. We found that small changes in phospholipid acyl chain length (i.e., PC-20 to PC-18) can switch gramicidin A from a stretch-activated to a stretch-inactivated channel. The demonstration that subnanometer changes in bilayer thickness can reverse the response polarity of a model channel has implications for other signaling proteins that may experience local changes in bilayer thickness as a consequence of dynamic targeting to lipid microdomains, electrocompression, or chemical modification of the bilayer.

Original languageEnglish (US)
Pages (from-to)4308-4312
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number7
DOIs
StatePublished - Apr 2 2002

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Gramicidin
Ion Channels
Patch-Clamp Techniques
Liposomes
Phospholipids
Lipids
Membranes
Proteins

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

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AB - The patch clamp-liposome technique was used to examine the stretch sensitivity of a model membrane ion channel, gramicidin A, in membrane patches of different bilayer thickness. We found that small changes in phospholipid acyl chain length (i.e., PC-20 to PC-18) can switch gramicidin A from a stretch-activated to a stretch-inactivated channel. The demonstration that subnanometer changes in bilayer thickness can reverse the response polarity of a model channel has implications for other signaling proteins that may experience local changes in bilayer thickness as a consequence of dynamic targeting to lipid microdomains, electrocompression, or chemical modification of the bilayer.

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