Journal
SCIENCE ADVANCES
Volume 7, Issue 3, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.abd5956
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Funding
- Agence Nationale de la Recherche [ANR ANR-15-CE13-0016-01, ANR-11-EQPX-0029 Morphoscope2]
- Fondation ARC pour la Recherche sur le Cancer [PGA120140200831]
- Institut National du Cancer [INCA_6521]
- Medical Research Council [MC_ UP_1201/13]
- Human Frontier Science Program [CDA00034/2017]
- MRC [MC_UP_1201/13] Funding Source: UKRI
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The WASH complex interacts with dynactin through its FAM21 subunit and uncaps it, inducing the branching reaction of the Arp2/3 complex. The WASH complex plays an important role in coordinating two complexes containing actin-related proteins.
Dendritic actin networks develop from a first actin filament through branching by the Arp2/3 complex. At the surface of endosomes, the WASH complex activates the Arp2/3 complex and interacts with the capping protein for unclear reasons. Here, we show that the WASH complex interacts with dynactin and uncaps it through its FAM21 subunit. In vitro, the uncapped Arp1/11 minifilament elongates an actin filament, which then primes the WASH-induced Arp2/3 branching reaction. In dynactin-depleted cells or in cells where the WASH complex is reconstituted with a FAM21 mutant that cannot uncap dynactin, formation of branched actin at the endosomal surface is impaired. Our results reveal the importance of the WASH complex in coordinating two complexes containing actin-related proteins.
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