ArticleMethods in molecular biology (Clifton, N.J.)2013
Purification of Arp2/3 complex from Saccharomyces cerevisiae.
Article in Methods in molecular biology (Clifton, N.J.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Two ligands of Arp2/3 complex, yeast coronin and GMF, interact and synergize in pruning branched actin networks.The Journal of biological chemistry · 2025Article
- In vitro Reconstitution of Phase-separated p62 Bodies on the Arp2/3-derived Actin Network.Bio-protocol · 2023Article
- Specialization of actin isoforms derived from the loss of key interactions with regulatory factors.The EMBO journal · 2022Article
- Sizes of actin networks sharing a common environment are determined by the relative rates of assembly.PLoS biology · 2019Article
- Abp1 promotes Arp2/3 complex-dependent actin nucleation and stabilizes branch junctions by antagonizing GMF.Nature communications · 2018Article
- G-actin guides p53 nuclear transport: potential contribution of monomeric actin in altered localization of mutant p53.Scientific reports · 2016Article
- Actin, actin-binding proteins, and actin-related proteins in the nucleus.Histochemistry and cell biology · 2016Review
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- Purification of native Arp2/3 complex from bovine thymus.Methods in molecular biology (Clifton, N.J.) · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Much of the cellular control over actin dynamics comes through regulation of actin filament initiation. At the molecular level, this is accomplished through a collection of cellular protein machines, called actin nucleation factors, which position actin monomers to initiate a new actin filament. The Arp2/3 complex is a principal actin nucleation factor used throughout the eukaryotic family tree. The budding yeast Saccharomyces cerevisiae has proven to be not only an excellent genetic platform for the study of the Arp2/3 complex, but also an excellent source for the purification of endogenous Arp2/3 complex. Here we describe a protocol for the preparation of endogenous Arp2/3 complex from wild type Saccharomyces cerevisiae. This protocol produces material suitable for biochemical study and yields milligram quantities of purified Arp2/3 complex.
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