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TitleStructure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 119, Issue 22, Page e2202723119, Year 2022
Publish dateMay 31, 2022
AuthorsBojian Ding / Heidy Y Narvaez-Ortiz / Yuvraj Singh / Glen M Hocky / Saikat Chowdhury / Brad J Nolen /
PubMed AbstractArp2/3 complex nucleates branched actin filaments that provide pushing forces to drive cellular processes such as lamellipodial protrusion and endocytosis. Arp2/3 complex is intrinsically inactive, ...Arp2/3 complex nucleates branched actin filaments that provide pushing forces to drive cellular processes such as lamellipodial protrusion and endocytosis. Arp2/3 complex is intrinsically inactive, and multiple classes of nucleation promoting factors (NPFs) stimulate its nucleation activity. When activated by WASP family NPFs, the complex must bind to the side of a preexisting (mother) filament of actin to complete the nucleation process, ensuring that WASP-mediated activation creates branched rather than linear actin filaments. How actin filaments contribute to activation is currently not understood, largely due to the lack of high-resolution structures of activated Arp2/3 complex bound to the side of a filament. Here, we present the 3.9-Å cryo-electron microscopy structure of the Arp2/3 complex at a branch junction. The structure reveals contacts between Arp2/3 complex and the side of the mother actin filament that likely stimulate subunit flattening, a conformational change that allows the actin-related protein subunits in the complex (Arp2 and Arp3) to mimic filamentous actin subunits. In contrast, limited contact between the bottom half of the complex and the mother filament suggests that clamp twisting, a second major conformational change observed in the active state, is not stimulated by actin filaments, potentially explaining why actin filaments are required but insufficient to trigger nucleation during WASP-mediated activation. Along with biochemical and live-cell imaging data and molecular dynamics simulations, the structure reveals features critical for the interaction of Arp2/3 complex with actin filaments and regulated assembly of branched actin filament networks in cells.
External linksProc Natl Acad Sci U S A / PubMed:35622886 / PubMed Central
MethodsEM (single particle)
Resolution3.9 Å
Structure data

26063

7tpt

EMDB-26063, PDB-7tpt:
Single-particle Cryo-EM structure of Arp2/3 complex at branched-actin junction.
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • bos taurus (cattle)
  • cattle (cattle)
  • rabbit (rabbit)
  • amanita phalloides (death cap)
  • oryctolagus cuniculus (rabbit)
KeywordsSTRUCTURAL PROTEIN / Arp2/3 / actin / cytoskeletal protein / actin regulator

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