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Clathrin adaptors drive phase separation in endocytosis and trafficking.
Communications Biology · · Journal Article · Open access
Draper-Barr, Schiller + more
Abstract ↗AI summary
The abstract is read at the publisher; the summary is JClub's.
Yeast adaptors Ent5 and Sla2 undergo LLPS, with Ent5's disordered helix and Sla2's coiled-coil region mediating condensate formation.
- Why it matters: Understanding how adaptor proteins contribute to membrane trafficking through phase separation can clarify mechanisms underlying endocytosis and cellular organization.
- What they did: The study examined Ent5 and Sla2 in vitro and in vivo, showing that Ent5's LLPS depends on a specific helix, while Sla2's condensation involves its coiled-coil region, linking structural features to phase separation.
- The result: Disruption of Ent5's helix delays transport events and alters membrane coating dynamics, indicating that phase separation driven by adaptors couples clathrin binding with membrane association in endocytosis.
The findingWhy it mattersWhat they didThe result
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