AI Article Synopsis
- The Arp2/3 complex is crucial for forming branched actin networks that facilitate endocytosis at the cell cortex.
- Dip1 activates Arp2/3 without needing existing actin filaments, while Wsp1 was previously thought to only help with branching from preexisting filaments.
- New findings reveal that Wsp1 also plays a key role in initiating actin networks by working together with Dip1, even in the absence of existing filaments.
Article Abstract
The actin filament nucleator Arp2/3 complex is activated at cortical sites in to assemble branched actin networks that drive endocytosis. Arp2/3 complex activators Wsp1 and Dip1 are required for proper actin assembly at endocytic sites, but how they coordinately control Arp2/3-mediated actin assembly is unknown. Alone, Dip1 activates Arp2/3 complex without preexisting actin filaments to nucleate 'seed' filaments that activate Wsp1-bound Arp2/3 complex, thereby initiating branched actin network assembly. In contrast, because Wsp1 requires preexisting filaments to activate, it has been assumed to function exclusively in propagating actin networks by stimulating branching from preexisting filaments. Here we show that Wsp1 is important not only for propagation but also for initiation of endocytic actin networks. Using single molecule total internal reflection fluorescence microscopy we show that Wsp1 synergizes with Dip1 to co-activate Arp2/3 complex. Synergistic co-activation does not require preexisting actin filaments, explaining how Wsp1 contributes to actin network initiation in cells.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7707826 | PMC |
| http://dx.doi.org/10.7554/eLife.60419 | DOI Listing |
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