• Corpus ID: 251467835

Dependence of protein-induced lipid bilayer deformations on protein shape

  title={Dependence of protein-induced lipid bilayer deformations on protein shape},
  author={Carlos Alas and Christoph A. Haselwandter},
Membrane proteins typically deform the surrounding lipid bilayer membrane, which can play an important role in the function, regulation, and organization of membrane proteins. Membrane elasticity theory provides a beautiful description of protein-induced lipid bilayer deformations, in which all physical parameters can be directly determined from experiments. Analytic treatments of the membrane elasticity theory of protein-induced lipid bilayer deformations have largely focused on idealized… 



Bilayer-thickness-mediated interactions between integral membrane proteins.

The work presented here puts into place an analytic and numerical framework which allows calculation of bilayer-mediated elastic interactions between integral membrane proteins for the complicated protein shapes suggested by structural biology and at the small protein separations most relevant for the crowded membrane environments provided by living cells.

Mechanochemical coupling of lipid organization and protein function through membrane thickness deformations.

The resulting lipid-protein organization can endow membrane proteins with diverse and controlled mechanical environments that, via protein-induced lipid bilayer thickness deformations, can strongly influence protein function.

Regulation of membrane proteins through local heterogeneity in lipid bilayer thickness.

It is suggested that protein-induced lipid bilayer thickness deformations endow proteins in cell membranes with diverse and controlled mechanical environments that, in turn, allow targeted regulation of membrane proteins.

Energetics of inclusion-induced bilayer deformations.

Inclusion-induced bilayer deformations: effects of monolayer equilibrium curvature.

Cooperative Gating and Spatial Organization of Membrane Proteins through Elastic Interactions

This work uses the mechanosensitive channel of large conductance (MscL) as a case study to examine the implications of bilayer-mediated elastic interactions on protein conformational statistics and clustering, and finds that conformational changes can severely alter the average separation between two proteins.

Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes.

It is found that SERCA adapts to membranes of different hydrophobic thicknesses by inducing local deformations in the lipid bilayers and by undergoing small rearrangements of the amino-acid side chains and helix tilts that allow smooth transitions through large conformational changes associated with the transport cycle of SERCA.

Lipid self-assembly and lectin-induced reorganization of the plasma membrane

  • T. SychY. MélyW. Römer
  • Biology, Chemistry
    Philosophical Transactions of the Royal Society B: Biological Sciences
  • 2018
The driving forces of lipid self-assembly into a bilayer membrane and the formation of small, transient domains within the plasma membrane are highlighted.