气候变化领域集成服务门户(CCPortal): Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling

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DOI	10.1073/pnas.2113789118
	Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling
	Bergeron-Sandoval L.-P.; Kumar S.; Heris H.K.; Chang C.L.A.; Cornell C.E.; Keller S.L.; François P.; Hendricks A.G.; Ehrlicher A.J.; Pappu R.V.; Michnick S.W.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:50
英文摘要	Membrane invagination and vesicle formation are key steps in endocytosis and cellular trafficking. Here, we show that endocytic coat proteins with prion-like domains (PLDs) form hemispherical puncta in the budding yeast, Saccharomyces cerevisiae. These puncta have the hallmarks of biomolecular condensates and organize proteins at the membrane for actin-dependent endocytosis. They also enable membrane remodeling to drive actin-independent endocytosis. The puncta, which we refer to as endocytic condensates, form and dissolve reversibly in response to changes in temperature and solution conditions. We find that endocytic condensates are organized around dynamic protein–protein interaction networks, which involve interactions among PLDs with high glutamine contents. The endocytic coat protein Sla1 is at the hub of the protein–protein interaction network. Using active rheology, we inferred the material properties of endocytic condensates. These experiments show that endocytic condensates are akin to viscoelastic materials. We use these characterizations to estimate the interfacial tension between endocytic condensates and their surroundings. We then adapt the physics of contact mechanics, specifically modifications of Hertz theory, to develop a quantitative framework for describing how interfacial tensions among condensates, the membrane, and the cytosol can deform the plasma membrane to enable actin-independent endocytosis. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Biomolecular condensates; Endocytosis; Protein–protein interactions; Viscoelasticity
语种	英语
scopus关键词	membrane protein; sla1 protein; unclassified drug; cytoskeleton protein; glutamine; Saccharomyces cerevisiae protein; SLA1 protein, S cerevisiae; viscoelastic substance; Article; budding yeast; controlled study; endocytosis; endosome; nonhuman; prion; protein protein interaction; Saccharomyces cerevisiae; viscoelasticity; cell membrane; chemistry; cytosol; gene expression regulation; genetics; mechanotransduction; metabolism; physiology; prion; protein conformation; Cell Membrane; Cytoskeletal Proteins; Cytosol; Endocytosis; Gene Expression Regulation, Fungal; Glutamine; Mechanotransduction, Cellular; Prions; Protein Conformation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Viscoelastic Substances
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/250938
作者单位	Departement de Biochimie, Universite de Montreal, Montreal, QC H3C 3J7, Canada; Department of Bioengineering, McGill University, Montreal, QC H3A 0C3, Canada; Department of Chemistry, University of Washington,, Seattle, Seattle, WA 98195-1700, United States; Ernest Rutherford Physics Building, McGill University, Montreal, QC H3A 2T8, Canada; Department of Biomedical Engineering, Center for Science and Engineering of Living Systems, Washington University in St. Louis, St. Louis, MO 63130, United States; Centre Robert-Cedergren, Bio-Informatique et Genomique, Universite de Montreal, Montreal, QC H3C 3J7, Canada
推荐引用方式 GB/T 7714	Bergeron-Sandoval L.-P.,Kumar S.,Heris H.K.,et al. Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling[J],2021,118(50).
APA	Bergeron-Sandoval L.-P..,Kumar S..,Heris H.K..,Chang C.L.A..,Cornell C.E..,...&Michnick S.W..(2021).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,118(50).
MLA	Bergeron-Sandoval L.-P.,et al."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 118.50(2021).