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Mechanism of Arp2/3 complex branch disassembly by human Coro7

Nooshin Shatery Nejad1, Malgorzata Boczkowska2, Rouba Hilal3

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.

Nature Communications
|November 6, 2025
PubMed

Insights

Coro7 protein disassembles Arp2/3-nucleated actin branches, impacting cell transport. Full-length Coro7, but not its domains, rescues ER-Golgi trafficking defects caused by its depletion.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Structural Biology

Background:

  • The Arp2/3 complex is crucial for forming branched actin networks, essential for cell motility and intracellular transport.
  • Coronins are known inhibitors of the Arp2/3 complex, influencing actin branch density.
  • Coro7, a less-studied coronin member, possesses distinct structural domains (β1β2 and CA) requiring further investigation.

Purpose of the Study:

  • To elucidate the molecular mechanism of Coro7's interaction with the Arp2/3 complex.
  • To determine Coro7's role in actin dynamics and its functional implications in cellular processes.
  • To investigate the specific contributions of Coro7's domains to its function.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine structural details.
  • Biochemical assays to assess binding affinities and polymerization inhibition/induction.
  • Cellular experiments involving protein depletion and rescue assays to evaluate functional impact.

Main Results:

  • The Coro7 Central-Acidic (CA) domain binds to the Arp3 subunit of the Arp2/3 complex, inhibiting polymerization.
  • Full-length Coro7, unlike its isolated domains, acts as an Arp2/3 complex branch disassembly factor.
  • Coro7 depletion disrupts endoplasmic reticulum-Golgi transport; this defect is rescued by full-length Coro7 in cellular models.

Conclusions:

  • Coro7 functions as a novel Arp2/3 complex branch disassembly factor.
  • Coro7 plays a significant role in actin-dependent ER-Golgi trafficking.
  • The distinct functions of full-length Coro7 versus its domains highlight the importance of its complete structure for cellular roles.

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