title: Sensing membrane thickness: Lessons learned from cold stress.
abstract: The lipid bilayer component of biological membranes is important for the distribution, organization, and function of bilayer spanning proteins. These physical barriers are subjected to bilayer perturbations. As a consequence, nature has evolved proteins that are able to sense changes in the bilayer properties and transform these lipid-mediated stimuli into intracellular signals. A structural feature that most signal-transducing membrane-embedded proteins have in common is one or more α-helices that traverse the lipid bilayer. Because of the interaction with the surrounding lipids, the organization of these transmembrane helices will be sensitive to membrane properties, like hydrophobic thickness. The helices may adapt to the lipids in different ways, which in turn can influence the structure and function of the intact membrane proteins. We review recent insights into the molecular basis of thermosensing via changes in membrane thickness and consider examples in which the hydrophobic matching can be demonstrated using reconstituted membrane systems. This article is part of a Special Issue entitled: The cellular lipid landscape edited by Tim P. Levine and Anant K. Menon.
authors.affiliation: Laboratorio de Fisiología Microbiana, Instituto de Biología Molecular y Celular de Rosario (IBR), CONICET, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Ocampo y Esmeralda, Predio CONICET Rosario, 2000 Rosario, Argentina.
authors.forename: Emilio
authors.initials: E
authors.lastname: Saita
authors.affiliation: Laboratorio de Fisiología Microbiana, Instituto de Biología Molecular y Celular de Rosario (IBR), CONICET, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Ocampo y Esmeralda, Predio CONICET Rosario, 2000 Rosario, Argentina.
authors.forename: Daniela
authors.initials: D
authors.lastname: Albanesi
authors.affiliation: Laboratorio de Fisiología Microbiana, Instituto de Biología Molecular y Celular de Rosario (IBR), CONICET, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Ocampo y Esmeralda, Predio CONICET Rosario, 2000 Rosario, Argentina. Electronic address: demendoza@ibr-conicet.gov.ar.
authors.forename: Diego
authors.initials: D
authors.lastname: de Mendoza
mesh_terms: D000818:Animals; D058639:Cold-Shock Response / Q000502:physiology*; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism*; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism*; D008566:Membranes / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology; D013697:Thermosensing / Q000502:physiology
chemical_list: D008051:Lipid Bilayers; D008563:Membrane Lipids
keywords: Membrane thickness; Thermosensing; Transmembrane signaling