These findings establish plant minimal START proteins as bona fide lipid-binding proteins that utilize a bipartite ligand-binding mechanism coupled with membrane-responsive gating dynamics, collectively suggesting a membrane-guided gating mechanism for lipid exchange.
It is suggested that bacterial START domains participate in a remarkably broad range of biological processes-including small-molecule binding, metabolic regulation, enzymatic catalysis, and stress adaptation-rather than traditional lipid transport.
Ece Aslan, Ksenia I. Lubova, Alexander Speer et al.· FEMS Microbiology Reviews· 0 citations
The present work provides the sequence basis and a mechanistic understanding of how IDPs employ aromatic-centered motifs to drive membrane insertion, and enriches the tools for the study of IDP-membrane association.
It is uncovered that membrane binding triggers a major conformational transition in LC3, exposing functional pockets that are occluded in its cytosolic form and can be engineered to precisely tune LC3-LIR interactions, offering a new strategy to regulate selective autophagy.
Deepanshi Gahlot, Jesu Castin, S. Mathur et al.· Nature Communications· 0 citations
Using super-resolution microscopy and molecular dynamics simulations, it is demonstrated that phosphatidylethanolamine stabilizes both NDC1 and MIC60 in highly curved membrane nanodomains, indicating that major membrane organizing complexes are positioned by selective lipid-protein interactions.
Katelyn C. Cook, Karen Palacio-Rodríguez, Kristi Bohlig et al.· bioRxiv· 1 citation
Regarded as one of the most complex membrane protein folds, CLCs form a large family of membrane proteins that function as anion channels and secondary active anion/proton transporters. Despite low sequence similarity, available structures are remarkably similar, maintaining the same inverted topology and fold, with su...
Janice L. Robertson· Chemical Reviews· 0 citations
The model provides a computationally efficient framework for studying conformational ensembles and assembly of proteins at bilayer–water interfaces and is validated against Wimley–White free energies of transfer of hydrophobic peptides and against an experimentally refined conformational ensemble of a flexible membrane...
Riccardo Saltutti, G. Tesei· bioRxiv· 0 citations
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