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The purified mechanosensitive channel TREK-1 is directly sensitive to membrane tension.
Berrier, Catherine; Pozza, Alexandre; de Lacroix de Lavalette, Agnes; Chardonnet, Solenne; Mesneau, Agnes; Jaxel, Christine; le Maire, Marc; Ghazi, Alexandre.
Afiliação
  • Berrier C; Institut de Biochimie et Biophysique Moléculaire et Cellulaire (IBBMC), Unité Mixte de Recherche (UMR) 8619, CNRS, Université Paris-Sud, 91405 Orsay.
  • Pozza A; Institute of Biology and Technology Saclay (iBitec-S), UMR 8221 Commissariat à l'Energie Atomique (CEA), CNRS, Université Paris-Sud and CEA Saclay, 91191 Gif sur Yvette, France.
  • de Lacroix de Lavalette A; Institute of Biology and Technology Saclay (iBitec-S), UMR 8221 Commissariat à l'Energie Atomique (CEA), CNRS, Université Paris-Sud and CEA Saclay, 91191 Gif sur Yvette, France.
  • Chardonnet S; Institut de Biochimie et Biophysique Moléculaire et Cellulaire (IBBMC), Unité Mixte de Recherche (UMR) 8619, CNRS, Université Paris-Sud, 91405 Orsay.
  • Mesneau A; Institut de Biochimie et Biophysique Moléculaire et Cellulaire (IBBMC), Unité Mixte de Recherche (UMR) 8619, CNRS, Université Paris-Sud, 91405 Orsay.
  • Jaxel C; Institute of Biology and Technology Saclay (iBitec-S), UMR 8221 Commissariat à l'Energie Atomique (CEA), CNRS, Université Paris-Sud and CEA Saclay, 91191 Gif sur Yvette, France.
  • le Maire M; Institute of Biology and Technology Saclay (iBitec-S), UMR 8221 Commissariat à l'Energie Atomique (CEA), CNRS, Université Paris-Sud and CEA Saclay, 91191 Gif sur Yvette, France.
  • Ghazi A; Institut de Biochimie et Biophysique Moléculaire et Cellulaire (IBBMC), Unité Mixte de Recherche (UMR) 8619, CNRS, Université Paris-Sud, 91405 Orsay. Electronic address: alexandre.ghazi@u-psud.fr.
J Biol Chem ; 288(38): 27307-27314, 2013 Sep 20.
Article em En | MEDLINE | ID: mdl-23897808
ABSTRACT
Mechanosensitive channels are detected in all cells and are speculated to play a key role in many functions including osmoregulation, growth, hearing, balance, and touch. In prokaryotic cells, a direct gating of mechanosensitive channels by membrane tension was clearly demonstrated because the purified channels could be functionally reconstituted in a lipid bilayer. No such evidence has been presented yet in the case of mechanosensitive channels from animal cells. TREK-1, a two-pore domain K(+) channel, was the first animal mechanosensitive channel identified at the molecular level. It is the target of a large variety of agents such as volatile anesthetics, neuroprotective agents, and antidepressants. We have produced the mouse TREK-1 in yeast, purified it, and reconstituted the protein in giant liposomes amenable to patch clamp recording. The protein exhibited the expected electrophysiological properties in terms of kinetics, selectivity, and pharmacology. Negative pressure (suction) applied through the pipette had no effect on the channel, but positive pressure could completely and reversibly close the channel. Our interpretation of these data is that the intrinsic tension in the lipid bilayer is sufficient to maximally activate the channel, which can be closed upon modification of the tension. These results indicate that TREK-1 is directly sensitive to membrane tension.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Pressão / Membrana Celular / Canais de Potássio de Domínios Poros em Tandem / Lipossomos Idioma: En Ano de publicação: 2013 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Pressão / Membrana Celular / Canais de Potássio de Domínios Poros em Tandem / Lipossomos Idioma: En Ano de publicação: 2013 Tipo de documento: Article