Mechanism of Arp2/3 complex branch disassembly by human Coro7

Nooshin Shatery Nejad, Malgorzata Boczkowska, Rouba Hilal, Fred E. Fregoso, Kyle R. Barrie, Grzegorz Rebowski, Andrew J. Saks, Alexis M. Gautreau, Enrique M. Cruz and Roberto Dominguez ()
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Nooshin Shatery Nejad: Yale University
Malgorzata Boczkowska: University of Pennsylvania
Rouba Hilal: Institut Polytechnique de Paris
Fred E. Fregoso: University of Pennsylvania
Kyle R. Barrie: University of Pennsylvania
Grzegorz Rebowski: University of Pennsylvania
Andrew J. Saks: University of Pennsylvania
Alexis M. Gautreau: Institut Polytechnique de Paris
Enrique M. Cruz: Yale University
Roberto Dominguez: University of Pennsylvania

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract Arp2/3 complex nucleates branched actin networks that drive cell motility and intracellular trafficking. Coronins, a family of seven proteins in humans, inhibit Arp2/3 complex in vitro and reduce branch density in cells. Coro7, a distant member of this family, features two β-propeller domains (β1β2) and C-terminal Central-Acidic (CA) domains and remains poorly studied. Here, cryo-EM and biochemical data show that CA binds subunit Arp3 of free Arp2/3 complex with ~1 µM affinity, inhibiting polymerization like Arpin, while displacing Arp3’s autoinhibitory C-terminal tail and promoting the active, short-pitch conformation, like WASP-family nucleation-promoting factors. Full-length Coro7, however, does not inhibit Arp2/3 complex polymerization but effectively induces debranching, whereas the isolated β1β2 or CA domains do not. In cells, Coro7 depletion disrupts ER-Golgi transport, which is rescued by full-length Coro7 but not by truncated variants. These results suggest that Coro7 functions as an Arp2/3 complex branch disassembly factor implicated in actin-dependent ER-Golgi trafficking.

Date: 2025
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DOI: 10.1038/s41467-025-64787-z

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