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- Title
Arp2/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation.
- Authors
Martin, Adam C.; Welch, Matthew D.; Drubin, David G.
- Abstract
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.
- Subjects
HYDROLYSIS; ENDOCYTOSIS; ACTIN; SACCHAROMYCES cerevisiae; NUCLEATION; CELLS
- Publication
Nature Cell Biology, 2006, Vol 8, Issue 8, p826
- ISSN
1465-7392
- Publication type
Article
- DOI
10.1038/ncb1443