Endocytic proteins with prion-like domains form viscoelastic condensates that enable membrane remodeling.

Autor:	Bergeron-Sandoval LP; Département de Biochimie, Université de Montréal, Montréal, QC H3C 3J7, Canada., Kumar S; Département de Biochimie, Université de Montréal, Montréal, QC H3C 3J7, Canada., Heris HK; Department of Bioengineering, McGill University, Montreal, QC H3A 0C3, Canada., Chang CLA; Department of Chemistry, University of Washington, Seattle, Seattle, WA 98195-1700., Cornell CE; Department of Chemistry, University of Washington, Seattle, Seattle, WA 98195-1700., Keller SL; Department of Chemistry, University of Washington, Seattle, Seattle, WA 98195-1700., François P; Ernest Rutherford Physics Building, McGill University, Montreal, QC H3A 2T8, Canada., Hendricks AG; Department of Bioengineering, McGill University, Montreal, QC H3A 0C3, Canada., Ehrlicher AJ; Department of Bioengineering, McGill University, Montreal, QC H3A 0C3, Canada., Pappu RV; Department of Biomedical Engineering and Center for Science and Engineering of Living Systems, Washington University in St. Louis, St. Louis, MO 63130; pappu@wustl.edu stephen.michnick@umontreal.ca., Michnick SW; Département de Biochimie, Université de Montréal, Montréal, QC H3C 3J7, Canada; pappu@wustl.edu stephen.michnick@umontreal.ca.; Centre Robert-Cedergren, Bio-Informatique et Génomique, Université de Montréal, Montréal, QC H3C 3J7, Canada.
Jazyk:	angličtina
Zdroj:	Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2021 Dec 14; Vol. 118 (50).
DOI:	10.1073/pnas.2113789118
Abstrakt:	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. Competing Interests: Competing interest statement: R.V.P. is a member of the Scientific Advisory Board of Dewpoint Therapeutics. (Copyright © 2021 the Author(s). Published by PNAS.)
Databáze:	MEDLINE
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