Versatile membrane deformation potential of activated pacsin. [PDF]
Endocytosis is a fundamental process in signaling and membrane trafficking. The formation of vesicles at the plasma membrane is mediated by the G protein dynamin that catalyzes the final fission step, the actin cytoskeleton, and proteins that sense or ...
Shih Lin Goh +3 more
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Membrane Binding by the Endophilin N-BAR Domain [PDF]
The structure of the endophilin N-terminal amphipathic helix Bin/Amphiphysin/Rvs-homology (N-BAR) domain is unique because of an additional insert helix under the arch of the N-BAR dimer. The structure of this additional helix has not been fully resolved in crystallographic studies, and thus presents a challenge to molecular-level analysis. Large-scale
Cui, Haosheng +2 more
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APPL proteins FRET at the BAR: direct observation of APPL1 and APPL2 BAR domain-mediated interactions on cell membranes using FRET microscopy. [PDF]
Human APPL1 and APPL2 are homologous RAB5 effectors whose binding partners include a diverse set of transmembrane receptors, signaling proteins, and phosphoinositides.
Heidi J Chial, Peter Lenart, Yong Q Chen
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A mutational analysis of the endophilin-A N-BAR domain performed in living flies. [PDF]
BACKGROUND: Endophilin is a cytoplasmic protein with an important function in clathrin-dependent endocytosis at synapses and elsewhere. Endophilin has a BAR (Bin/Amphiphysin/Rvs-homology) domain, which is implicated in the sensing and induction of ...
Anita G Jung +5 more
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BAR domain competition during directional cellular migration [PDF]
While directed cellular migration facilitates the coordinated movement of cells during development and tissue repair, the precise mechanisms regulating the interplay between the extracellular environment, the actin cytoskeleton, and the overlying plasma membrane remain inadequately understood.
Gabriel A, Quiñones, Anthony E, Oro
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Structural Basis of Membrane Invagination by F-BAR Domains [PDF]
BAR superfamily domains shape membranes through poorly understood mechanisms. We solved structures of F-BAR modules bound to flat and curved bilayers using electron (cryo)microscopy. We show that membrane tubules form when F-BARs polymerize into helical coats that are held together by lateral and tip-to-tip interactions. On gel-state membranes or after
Frost, Adam +7 more
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Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7
The Bin/Amphiphysin/Rvs167 (BAR) domain superfamily, which includes FCH-BAR (F-BAR) domain proteins are membrane-sculpting proteins. Here the authors combine a range of techniques and show that the F-BAR domain of growth-arrest specific protein 7 (GAS7 ...
Kyoko Hanawa-Suetsugu +19 more
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An Amphiphysin-Like Domain in Fus2p Is Required for Rvs161p Interaction and Cortical Localization
Cell–cell fusion fulfils essential roles in fertilization, development and tissue repair. In the budding yeast, Saccharomyces cerevisiae, fusion between two haploid cells of opposite mating type generates the diploid zygote.
Richard A. Stein +2 more
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Dielectric analysis of degraded stator bars of a hydro generator
This paper presents the investigation of dielectric analysis of degraded stator bars by Polarization and Depolarization Current (PDC) measurement. The stator bars obtained from the 30-year in-service synchronous machine were divided into two groups.
Norasage Pattanadech +4 more
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Four-Scale Description of Membrane Sculpting by BAR Domains [PDF]
BAR domains are proteins that sense and sculpt curved membranes in cells, furnishing a relatively well-studied example of mechanisms employed in cellular morphogenesis. We report a computational study of membrane bending by BAR domains at four levels of resolution, described by 1), all-atom molecular dynamics; 2), residue-based coarse-graining ...
Arkhipov, Anton +2 more
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