ArticleMolecular biology of the cell2010
Dissecting BAR domain function in the yeast Amphiphysins Rvs161 and Rvs167 during endocytosis.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Role of the dynamin-related protein 2 family and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana.Journal of cell science · 2024Article
- New Insights on the Uptake and Trafficking of Coenzyme Q.Antioxidants (Basel, Switzerland) · 2023Review
- Self-organizing actin networks drive sequential endocytic protein recruitment and vesicle release on synthetic lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Self-organizing actin networks drive sequential endocytic protein recruitment and vesicle release on synthetic lipid bilayers.bioRxiv : the preprint server for biology · 2023Article
- GTP-stimulated membrane fission by the N-BAR protein AMPH-1.Traffic (Copenhagen, Denmark) · 2023Article
- Regulation of membrane scission in yeast endocytosis.Molecular biology of the cell · 2022Article
- Amphiphysin AoRvs167-Mediated Membrane Curvature Facilitates Trap Formation, Endocytosis, and Stress Resistance inPathogens (Basel, Switzerland) · 2022Article
- Microfluidic screening and genomic mutation identification for enhancing cellulase production in Pichia pastoris.Biotechnology for biofuels and bioproducts · 2022Article
- ER-phagy requires the assembly of actin at sites of contact between the cortical ER and endocytic pits.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling.Molecular biology of the cell · 2021Article
- Thermodynamics and Free Energy Landscape of BAR-Domain Dimerization from Molecular Simulations.The journal of physical chemistry. B · 2021Article
- Chemical-Genetic Interactions with the Proline Analog L-Azetidine-2-Carboxylic Acid inG3 (Bethesda, Md.) · 2020Article
- Review
- TORC2 controls endocytosis through plasma membrane tension.The Journal of cell biology · 2019Article
- Communicate and Fuse: How Filamentous Fungi Establish and Maintain an Interconnected Mycelial Network.Frontiers in microbiology · 2019Review
- BAR domain proteins-a linkage between cellular membranes, signaling pathways, and the actin cytoskeleton.Biophysical reviews · 2018Review
- Correlative Microscopy of Vitreous Sections Provides Insights into BAR-Domain Organization In Situ.Structure (London, England : 1993) · 2018Article
- Cytosolic proteins can exploit membrane localization to trigger functional assembly.PLoS computational biology · 2018Article
- The SAGA complex, together with transcription factors and the endocytic protein Rvs167p, coordinates the reprofiling of gene expression in response to changes in sterol composition inMolecular biology of the cell · 2017Article
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Authors and funding
11 authors.
Funding
Abstract
BAR domains are protein modules that bind to membranes and promote membrane curvature. One type of BAR domain, the N-BAR domain, contains an additional N-terminal amphipathic helix, which contributes to membrane-binding and bending activities. The only known N-BAR-domain proteins in the budding yeast Saccharomyces cerevisiae, Rvs161 and Rvs167, are required for endocytosis. We have explored the mechanism of N-BAR-domain function in the endocytosis process using a combined biochemical and genetic approach. We show that the purified Rvs161-Rvs167 complex binds to liposomes in a curvature-independent manner and promotes tubule formation in vitro. Consistent with the known role of BAR domain polymerization in membrane bending, we found that Rvs167 BAR domains interact with each other at cortical actin patches in vivo. To characterize N-BAR-domain function in endocytosis, we constructed yeast strains harboring changes in conserved residues in the Rvs161 and Rvs167 N-BAR domains. In vivo analysis of the rvs endocytosis mutants suggests that Rvs proteins are initially recruited to sites of endocytosis through their membrane-binding ability. We show that inappropriate regulation of complex sphingolipid and phosphoinositide levels in the membrane can impinge on Rvs function, highlighting the relationship between membrane components and N-BAR-domain proteins in vivo.
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