Cells respond to applied external forces through different mechanosensitive processes, with many of them based on the interaction between membrane-embedded proteins and their lipid environments. This interaction can depend on membrane curvature at the location of such proteins. Here we elucidate the general characteristics of a macroscopically defined protein-lipid bilayer interaction based on a mismatch between the shape of the protein surface and the surrounding membrane curvature. It is shown how the parameters of this interaction are related to the experimentally determined distribution of membrane-embedded proteins between highly curved tubular and flat membrane regions of a giant phospholipid vesicle. The results obtained for such distribution of potassium channel KvAP are presented as an example. Possible participation of the curvature-dependent protein-lipid bilayer interaction in mechanosensitive processes is indicated.
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http://dx.doi.org/10.1007/s00249-015-1046-5 | DOI Listing |
Front Mol Biosci
January 2025
Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky, Lexington, KY, United States.
This study investigates the dynamics of oleate hydratase (OhyA), a bacterial flavoenzyme from , and its interactions with lipid membranes, focusing on the factors influencing membrane binding and oligomerization. OhyA catalyzes the hydration of unsaturated fatty acids, playing a key role in bacterial pathogenesis by neutralizing host antimicrobial fatty acids. OhyA binds the membrane bilayer to access membrane-embedded substrates for catalysis, and structural studies have revealed that OhyA forms oligomers on membrane surfaces, stabilized by both protein-protein and protein-lipid interactions.
View Article and Find Full Text PDFNeuron
January 2025
Department of Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461, USA. Electronic address:
Neurexin cell-adhesion molecules regulate synapse development and function by recruiting synaptic components. Here, we uncover a mechanism for presynaptic assembly that precedes neurexin recruitment, mediated by interactions between cytosolic proteins and membrane phospholipids. Developmental imaging in C.
View Article and Find Full Text PDFMethods Mol Biol
January 2025
Estrella Mountain Community College, Phoenix, AZ, USA.
Vacuole fusion is driven by SNARE proteins that require activation-or priming-by the AAA+ protein Sec18 (NSF) before they can bring membranes together and trigger the merger of two bilayers into a continuous membrane. Sec18 resides on vacuoles prior to engaging inactive cis-SNARE complexes through its interaction with the regulatory lipid phosphatidic acid (PA). Binding PA causes Sec18 to undergo large conformational changes that keeps it bound to the membrane, thus precluding its interactions with SNAREs.
View Article and Find Full Text PDFMethods Mol Biol
January 2025
Departments of Neurology, and Anatomy and Cell Biology, Wayne State University School of Medicine, University Health Center, Detroit, MI, USA.
Molecular dynamics (MD) simulations enable in silico investigation of the dynamic behavior of proteins and protein complexes. Here, we describe MD simulations of the SNARE bundle forming the complex with the neuronal proteins Synaptotagmin-1 (Syt1) and Complexin (Cpx). Syt1 is the synaptic vesicle (SV) protein that serves as the neuronal calcium sensor and triggers synaptic fusion upon calcium binding, and this process is promoted and accelerated by Cpx.
View Article and Find Full Text PDFJ Chem Phys
December 2024
Physical and Life Sciences Directorate, Lawrence Livermore National Laboratory, Livermore, California 94550, USA.
In this work, a model for anisotropic interactions between proteins and cellular membranes is proposed for large-scale continuum simulations. The framework of the model is based on dynamic density functional theory, which provides a formalism to describe the lipid densities within the membrane as continuum fields while still maintaining the fidelity of the underlying molecular interactions. Within this framework, we extend recent results to include the anisotropic effects of protein-lipid interactions.
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