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

Louis Philippe Bergeron-Sandoval, Sandeep Kumar, Hossein Khadivi Heris, Catherine L.A. Chang, Caitlin E. Cornell, Sarah L. Keller, Paul François, Adam G. Hendricks, Allen J. Ehrlicher, Rohit V. Pappu, Stephen W. Michnick

Research output: Contribution to journalArticlepeer-review

64 Scopus citations


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.

Original languageEnglish
Article numbere2113789118
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number50
StatePublished - Dec 14 2021


  • Biomolecular condensates
  • Endocytosis
  • Protein–protein interactions
  • Viscoelasticity


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