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Related Experiment Video

Updated: May 8, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction

In vivo and in vitro Studies of Adaptor-clathrin Interaction

Published on: January 26, 2011

Endocytic accessory proteins assemble clathrin while simultaneously destabilizing protein condensates.

Brandon Malady¹, Susovan Sarkar¹, Liping Wang²

¹Department of Biomedical Engineering, The University of Texas at Austin, United States.

Biorxiv : the Preprint Server for Biology

|May 7, 2026

Summary

This summary is machine-generated.

Clathrin accessory proteins regulate biomolecular condensates to drive vesicle formation during endocytosis. This study reveals how condensate stability controls clathrin assembly and vesicle release.

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Area of Science:

Cell Biology
Biophysics

Background:

Endocytosis involves clathrin coat assembly driven by a protein network.
Eps15 protein forms biomolecular condensates via liquid-liquid phase separation, facilitating clathrin assembly.
Clathrin accessory proteins are crucial but their interaction with condensates is unexplored.

Purpose of the Study:

To investigate how clathrin accessory proteins interact with Eps15 condensates.
To determine the role of condensate stability in clathrin lattice assembly and vesicle exclusion.
To elucidate the physical mechanisms linking phase separation to membrane trafficking.

Main Methods:

Formation of Eps15 biomolecular condensates in vitro.
Addition of various clathrin accessory proteins to Eps15 condensates.
Observation of effects on condensate stability, clathrin lattice assembly, and clathrin exclusion.

Main Results:

Accessory proteins that cross-link Eps15 stabilize condensates; those competing with Eps15 interactions destabilize them.
Destabilization of condensates by accessory proteins promotes clathrin assembly and exclusion.
Stabilization of condensates opposes clathrin exclusion.
Decreased condensate stability enhances clathrin assembly and exclusion.

Conclusions:

Clathrin accessory proteins actively regulate biomolecular condensate stability.
Condensate destabilization by accessory proteins drives clathrin lattice assembly and vesicle exclusion.
This provides a physical mechanism for coordinating phase separation with membrane trafficking in endocytosis.