ArticleMolecular biology of the cell2022
Regulation of membrane scission in yeast endocytosis.
Article in Molecular biology of the cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Friction-driven scission: How nonlocal mechanisms contribute to membrane fission across domains of life.Science advances · 2026Review
- Chlamydia trachomatis invasion: a duet of effectors.Biochemical Society transactions · 2025Review
- Cytotoxicity of Quantum Dots in Receptor-Mediated Endocytic and Pinocytic Pathways in Yeast.International journal of molecular sciences · 2024Article
- Quantifying Protein Dynamics by Kymograph Analysis.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Spatio-temporal regulation of endocytic protein assembly by SH3 domains in yeast.Molecular biology of the cell · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During clathrin-mediated endocytosis, a flat plasma membrane is shaped into an invagination that undergoes scission to form a vesicle. In mammalian cells, the force that drives the transition from invagination to vesicle is primarily provided by the GTPase dynamin that acts in concert with crescent-shaped BAR domain proteins. In yeast cells, the mechanism of endocytic scission is unclear. The yeast BAR domain protein complex Rvs161/167 (Rvs) nevertheless plays an important role in this process: deletion of Rvs dramatically reduces scission efficiency. A mechanistic understanding of the influence of Rvs on scission, however, remains incomplete. We used quantitative live-cell imaging and genetic manipulation to understand the recruitment and function of Rvs and other late-stage proteins at yeast endocytic sites. We found that arrival of Rvs at endocytic sites is timed by interaction of its BAR domain with specific membrane curvature. A second domain of Rvs167-the SH3 domain-affects localization efficiency of Rvs. We show that Myo3, one of the two type-I myosins in
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.