Lipid-protein interactions: Lessons learned from stress

, Ridone, Pietro, Bavi, Navid, Nakayama, Yoshitaka, Nikolaev, Yury, & Martinac, Boris (2015) Lipid-protein interactions: Lessons learned from stress. Biochimica et Biophysica Acta - Biomembranes, 1848(9), pp. 1744-1756.

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Description

Full-text article is free to read on the publisher's website Biological membranes are essential for normal function and regulation of cells, forming a physical barrier between extracellular and intracellular space and cellular compartments. These physical barriers are subject to mechanical stresses. As a consequence, nature has developed proteins that are able to transpose mechanical stimuli into meaningful intracellular signals. These proteins, termed Mechanosensitive (MS) proteins provide a variety of roles in response to these stimuli. In prokaryotes these proteins form transmembrane spanning channels that function as osmotically activated nanovalves to prevent cell lysis by hypoosmotic shock. In eukaryotes, the function of MS proteins is more diverse and includes physiological processes such as touch, pain and hearing. The transmembrane portion of these channels is influenced by the physical properties such as charge, shape, thickness and stiffness of the lipid bilayer surrounding it, as well as the bilayer pressure profile. In this review we provide an overview of the progress to date on advances in our understanding of the intimate biophysical and chemical interactions between the lipid bilayer and mechanosensitive membrane channels, focusing on current progress in both eukaryotic and prokaryotic systems. These advances are of importance due to the increasing evidence of the role the MS channels play in disease, such as xerocytosis, muscular dystrophy and cardiac hypertrophy. Moreover, insights gained from lipid-protein interactions of MS channels are likely relevant not only to this class of membrane proteins, but other bilayer embedded proteins as well. This article is part of a Special Issue entitled: Lipid-protein interactions.

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ID Code: 114063
Item Type: Contribution to Journal (Journal Article)
Refereed: Yes
Measurements or Duration: 13 pages
DOI: 10.1016/j.bbamem.2015.04.012
ISSN: 0005-2736
Pure ID: 32957897
Divisions: Past > QUT Faculties & Divisions > Faculty of Health
Past > Institutes > Institute of Health and Biomedical Innovation
Current > Schools > School of Biomedical Sciences
Copyright Owner: Consult author(s) regarding copyright matters
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Deposited On: 18 Nov 2017 03:24
Last Modified: 01 Mar 2024 16:29