Endophilin-A1 BAR domain interaction with arachidonyl CoA [PDF]
Frontiers in Molecular Biosciences, 2014 Endophilin-A1 belongs to the family of BAR domain containing proteins that catalyze membrane remodeling processes via sensing, inducing and stabilizing membrane curvature.
Maxim V. Petoukhov +3 more
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Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and Autoregulation [PDF]
Cell Reports, 2015 F-BAR domain proteins regulate and sense membrane curvature by interacting with negatively charged phospholipids and assembling into higher-order scaffolds. However, regulatory mechanisms controlling these interactions are poorly understood.
Charlotte F. Kelley +12 more
doaj +4 more sources
Purification of Recombinant Human Amphiphysin 1 and its N-BAR Domain [PDF]
Bio-Protocol, 2023 Bin/Amphiphysin/Rvs (BAR) proteins are known as classical membrane curvature generators during endocytosis. Amphiphysin, a member of the N-BAR sub-family of proteins that contain a characteristic amphipathic sequence at the N-terminus of the BAR domain ...
Samsuzzoha Mondal +4 more
doaj +2 more sources
Ca2+ Regulates Dimerization of the BAR Domain Protein PICK1 and Consequent Membrane Curvature [PDF]
Frontiers in Molecular Neuroscience, 2022 Bin-Amphiphysin-Rvs (BAR) domain proteins are critical regulators of membrane geometry. They induce and stabilize membrane curvature for processes, such as clathrin-coated pit formation and endosomal membrane tubulation.
Georgiana F. Stan +3 more
doaj +2 more sources
An atypical BAR domain protein in autophagy. [PDF]
Autophagy, 2018 The sorting nexin Atg20 interacts with the selective macroautophagy/autophagy scaffolding protein Atg11, suggesting an important role for Atg20 in the initiation of selective autophagy. To explore this possibility, we recently investigated the structure and function of Atg20 using a variety of biophysical and yeast genetic approaches.
Popelka H, Klionsky DJ, Ragusa MJ.
europepmc +4 more sources
The ArfGAP ASAP1 Controls Actin Stress Fiber Organization via Its N-BAR Domain [PDF]
iScience, 2019 Summary: ASAP1 is a multi-domain ArfGAP that controls cell migration, spreading, and focal adhesion dynamics. Although its GAP activity contributes to remodeling of the actin cytoskeleton, it does not fully explain all cellular functions of ASAP1.
Anjelika Gasilina +4 more
doaj +2 more sources
Coding variants identified in patients with diabetes alter PICK1 BAR domain function in insulin granule biogenesis [PDF]
The Journal of Clinical Investigation, 2022 Bin/amphiphysin/Rvs (BAR) domains are positively charged crescent-shaped modules that mediate curvature of negatively charged lipid membranes during remodeling processes.
Rita C. Andersen +21 more
doaj +2 more sources
A bacterial membrane sculpting protein with BAR domain-like activity [PDF]
eLife, 2021 Bin/Amphiphysin/RVS (BAR) domain proteins belong to a superfamily of coiled-coil proteins influencing membrane curvature in eukaryotes and are associated with vesicle biogenesis, vesicle-mediated protein trafficking, and intracellular signaling. Here, we
Daniel A Phillips +13 more
doaj +2 more sources
Dendritic Spine Initiation in Brain Development, Learning and Diseases and Impact of BAR-Domain Proteins [PDF]
Cells, 2021 Dendritic spines are small, bulbous protrusions along neuronal dendrites where most of the excitatory synapses are located. Dendritic spine density in normal human brain increases rapidly before and after birth achieving the highest density around 2–8 ...
Pushpa Khanal, Pirta Hotulainen
doaj +2 more sources
BAR domain proteins regulate Rho GTPase signaling [PDF]
Small GTPases, 2014 The Bin-Amphiphysin-Rvs (BAR) domain is a membrane lipid binding domain present in a wide variety of proteins, often proteins with a role in Rho-regulated signaling pathways. BAR domains do not only confer binding to lipid bilayers, they also possess a membrane sculpturing ability and thereby directly control the topology of biomembranes.
Pontus Aspenström
exaly +4 more sources