Letter abstract
Nature Cell Biology 8, 826 - 833 (2006)
Published online: 23 July 2006 | doi:10.1038/ncb1443
Arp2/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation
Adam C. Martin1, Matthew D. Welch1 & David G. Drubin1
The Arp2/3 complex, which is crucial for actin-based motility, nucleates actin filaments and organizes them into y-branched networks. The Arp2 subunit has been shown to hydrolyse ATP, but the functional importance of Arp2/3 ATP hydrolysis is not known. Here, we analysed an Arp2 mutant in Saccharomyces cerevisiae that is defective in ATP hydrolysis. Arp2 ATP hydrolysis and Arp2/3-dependent actin nucleation occur almost simultaneously. However, ATP hydrolysis is not required for nucleation. In addition, Arp2 ATP hydrolysis is not required for the release of a WASP-like activator from y-branches. ATP hydrolysis by Arp2, and possibly Arp3, is essential for efficient y-branch dissociation in vitro. In living cells, both Arp2 and Arp3 ATP-hydrolysis mutants exhibit defects in endocytic internalization and actin-network disassembly. Our results suggest a critical feature of dendritic nucleation in which debranching and subsequent actin-filament remodelling and/or depolymerization are important for endocytic vesicle morphogenesis.
- 16 Barker Hall, Dept. of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA.
Correspondence to: David G. Drubin1 e-mail: drubin@socrates.berkeley.edu
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