How lipids affect the activities of integral membrane proteins.

By Anthony G. Lee. Biochimica et Biophysica Acta, 2004

1,231 citations recorded by the source corpus.

The activities of integral membrane proteins are often affected by the structures of the lipid molecules that surround them in the membrane. One important parameter is the hydrophobic thickness of the lipid bilayer, defined by the lengths of the lipid fatty acyl chains. Membrane proteins are not rigid entities, and deform to ensure good hydrophobic matching to the surrounding lipid bilayer. The structure of the lipid headgroup region is likely to be important in defining the structures of those parts of a membrane protein that are located in the lipid headgroup region. A number of examples are given where the conformation of the headgroup-embedded region of a membrane protein changes during the reaction cycle of the protein; activities of such proteins might be expected to be particularly sensitive to lipid headgroup structure. Differences in hydrogen bonding potential and hydration between the headgroups of phosphatidycholines and phosphatidylethanolamines could be important factors in determining the effects of these lipids on protein activities, as well as any effects related to the tendency of the phosphatidylethanolamines to form a curved, hexagonal H(II) phase. Effects of lipid structure on protein aggregation and helix-helix interactions are also discussed, as well as the effects of charged lipids on ion concentrations close to the surface of the bilayer. Interpretations of lipid effects in terms of changes in protein volume, lipid free volume, and curvature frustration are also described. Finally, the role of non-annular, or 'co-factor' lipids, tightly bound to membrane proteins, is described.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d571a38d40283e9c31444e40586c515b66d90f5a

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Citations in the corpus

Bilayer thickness and membrane protein function: an energetic perspective. (2007, background): “Not surprisingly, the membrane lipid regulation of membrane protein function has been formulated with different descriptors: bilayer fluidity (103); bilayer compression, or bilayerprotein hydrophobic mismatch (79); intrinsic lipid curvature (38) or curvature frustration (60); bilayer deformation ene”
Role of cholesterol and lipid organization in disease (2005, background): “In the past few years, several lines of evidence have shown that the biophysical properties of membrane bilayers have significant effects on the properties of membrane protein”
Fluid phase lipid areas and bilayer thicknesses of commonly used phosphatidylcholines as a function of temperature. (2011, background): “It is now generally accepted that the function, insertion, orientation, and subcellular localization of integral membrane proteins are all affected by themembrane's physical properties [1].”
Positioning of proteins in membranes: A computational approach (2006, background): “This is not surprising, since the octanol solution contains a significant amount of water (;2.3M; Leo et al. 1971) and has high dielectric constant (;10–20), unlike the hydrocarbon core of lipid bilayers (Benz et al. 1975; Radzicka and Wolfenden 1988).”
Cellular cholesterol trafficking and compartmentalization (2008, background): “For instance, sterol-induced alterations in membrane biophysical properties could indirectly affect protein function”
Lipid-Dependent Alternating Access Mechanism of a Bacterial Multidrug ABC Exporter (2019, positive): “64 Here we provide evidence that the lipid − protein and lipid − lipid interaction networks present in the PE lipid environment facilitate the closing of the Sav1866 transporter, while the absence of these interactions along with the sheer presence of the PC lipids in the periplasmic gate of…”
CHARMM-GUI Membrane Builder for mixed bilayers and its application to yeast membranes. (2009, background): “Moreover, it was reported that for some proteins, the heterogeneity of a membrane is particularly important for protein function (2,20,22).”