title: Dynamic regulation of lipid-protein interactions.
abstract: We review the importance of helix motions for the function of several important categories of membrane proteins and for the properties of several model molecular systems. For voltage-gated potassium or sodium channels, sliding, tilting and/or rotational movements of the S4 helix accompanied by a swapping of cognate side-chain ion-pair interactions regulate the channel gating. In the seven-helix G protein-coupled receptors, exemplified by the rhodopsins, collective helix motions serve to activate the functional signaling. Peptides which initially associate with lipid-bilayer membrane surfaces may undergo dynamic transitions from surface-bound to tilted-transmembrane orientations, sometimes accompanied by changes in the molecularity, formation of a pore or, more generally, the activation of biological function. For single-span membrane proteins, such as the tyrosine kinases, an interplay between juxtamembrane and transmembrane domains is likely to be crucial for the regulation of dimer assembly that in turn is associated with the functional responses to external signals. Additionally, we note that experiments with designed single-span transmembrane helices offer fundamental insights into the molecular features that govern protein-lipid interactions. This article is part of a Special Issue entitled: Lipid-protein interactions.
authors: Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA.
authors: Ashley N
authors: AN
authors: Martfeld
authors: Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA.
authors: Venkatesan
authors: V
authors: Rajagopalan
authors: Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA.
authors: Denise V
authors: DV
authors: Greathouse
authors: Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA. Electronic address: rk2@uark.edu.
authors: Roger E
authors: RE
authors: Koeppe
mesh_terms: D000818:Animals; D006801:Humans; D007700:Kinetics; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D008563:Membrane Lipids / Q000737:chemistry* / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins
keywords: Lipid–protein interaction; Membrane dynamics; Membrane protein; Solid-state nuclear magnetic resonance