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J Biol Chem, Vol. 275, Issue 2, 1015-1022, January 14, 2000

Contributions of the Different Extramembranous Domains of the Mechanosensitive Ion Channel MscL to Its Response to Membrane Tension*

Bassam AjouzDagger , Catherine BerrierDagger , Madeleine BesnardDagger §, Boris Martinac, and Alexandre GhaziDagger par

From the Dagger  Laboratoire des Biomembranes, Unité Mixte de Recherche CNRS 8619, Bâtiment 430, Université Paris-Sud 91405 Orsay Cedex France and the  Department of Pharmacology, University of Western Australia, Nedlands, Western Australia 6907, Australia

MscL is a mechanosensitive channel that is gated by tension in the membrane bilayer alone. It is a homo-oligomer of a protein comprising two transmembrane segments connected by an external loop, with the NH2 and COOH termini located in the cytoplasm. The contributions of the extramembranous domains of the channel to its activity were investigated by specific proteolysis during patch-clamp experiments. Limited proteolysis of the COOH terminus or the NH2 terminus increased the mechanosensitivity of the channel without changing its conductance. Strikingly, after cleavage of the external loop of each monomer, the channel was still functional, and its mechanosensitivity was increased dramatically, indicating that the loop acts as a spring that resists the opening of the channel and promotes its closure when it is open. These results indicate that the integrity of most of the extramembranous domains is not essential for mechanosensitivity. They suggest that these domains counteract the movement of the transmembrane helices to which they are connected, thus setting the level of sensitivity of the channel to tension.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: URA CNRS 1218, Faculté de Pharmacie, Université Paris-Sud, 5 rue Jean-Baptiste Clément, 92296 Châtenay-Malabry Cedex, France.

par To whom correspondence should be addressed. Tel.: 33-1-6915-7194; Fax: 33-1-6985-3715; E-mail: alexandre.ghazi@biomemb.u-psud.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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