Journal
BIOLOGY OPEN
Volume 9, Issue 7, Pages -Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/bio.054304
Keywords
Arp2/3; Actin; Cytoskeleton; Cryo-EM; Isoforms; Nucleation
Categories
Funding
- Biotechnology and Biological Sciences Research Council [BB/L00190X/1]
- Cancer Research UK [FC001209]
- UK Medical Research Council [FC001209]
- Wellcome Trust [FC001209]
- European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme [810207]
- Agence Nationale de la Recherche [grant MuScActin]
- BBSRC [BB/L00190X/1] Funding Source: UKRI
- European Research Council (ERC) [810207] Funding Source: European Research Council (ERC)
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The Arp2/3 complex regulates many cellular processes by stimulating formation of branched actin filament networks. Because three of its seven subunits exist as two different isoforms, mammals produce a family of Arp2/3 complexes with different properties that may be suited to different physiological contexts. To shed light on how isoform diversification affects Arp2/3 function, we determined a 4.2 angstrom resolution cryo-EM structure of the most active human Arp2/3 complex containing ARPC1 B and ARPC5L, and compared it with the structure of the least active ARPC1A-ARPC5-containing complex. The architecture of each isoform-specific Arp2/3 complex is the same. Strikingly, however, the N-terminal half of ARPC5L is partially disordered compared to ARPC5, suggesting that this region of ARPC5/ARPC5L is an important determinant of complex activity. Confirming this idea, the nucleation activity of Arp2/3 complexes containing hybrid ARPC5/ARPC5L subunits is higher when the ARPC5L N-terminus is present, thereby providing insight into activity differences between the different Arp2/3 complexes.
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