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TitleActivation of Arp2/3 complex by a SPIN90 dimer in linear actin-filament nucleation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 11, Page 2272-2284, Year 2025
Publish dateSep 15, 2025
AuthorsJustus Francis / Achyutha Krishna Pathri / Kankipati Teja Shyam / Sridhar Sripada / Rishav Mitra / Heidy Y Narvaez-Ortiz / Kiran Vyshnav Eliyan / Brad J Nolen / Saikat Chowdhury /
PubMed AbstractArp2/3 complex is a key nucleator of actin filaments. It requires activation by nucleation-promoting factors (NPFs). WISH/DIP1/SPIN90 (WDS) proteins represent a unique class of NPFs that activate the ...Arp2/3 complex is a key nucleator of actin filaments. It requires activation by nucleation-promoting factors (NPFs). WISH/DIP1/SPIN90 (WDS) proteins represent a unique class of NPFs that activate the Arp2/3 complex independently of preexisting filaments, promoting linear actin-filament nucleation. In fission yeast, Dip1 binds to the clamp subunits in Arp2/3 complex to induce the short-pitch conformation, where Arp2 moves closer to Arp3 to mimic a filamentous actin dimer. However, how WDS proteins stimulate subunit flattening in Arp subunits, a 'scissor-like' conformational change akin to what is observed in an actin monomer during filament formation, remained unclear. Here we present cryo-electron microscopy structures of human SPIN90 bound to activated bovine Arp2/3 complex on an actin filament pointed end. The structures show that SPIN90 dimerizes through a metazoan-specific domain in the middle segment, engaging both the clamp and the Arp3/ARPC3 interface, to drive the activating conformational changes in Arp2/3 complex. Remarkably, a single SPIN90 dimer can also bridge two Arp2/3 complexes, enabling bidirectional actin nucleation and suggesting a mechanism for rapidly assembling complex actin network architectures.
External linksNat Struct Mol Biol / PubMed:40954370
MethodsEM (single particle)
Resolution3.13 - 3.6 Å
Structure data

63642

9m5e

EMDB-63642, PDB-9m5e:
Structure of SPIN90 dimer-Arp2/3 complex-nucleated actin filament (singlet complex)
Method: EM (single particle) / Resolution: 3.55 Å

63658

9m64

EMDB-63658, PDB-9m64:
Structure of SPIN90 dimer-Arp2/3 complexes-nucleated actin filaments (Doublet Complex)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-63880: Focused Arp2/3 complex map of SPIN90 dimer-Arp2/3 complex-filament singlet complex structure
Method: EM (single particle) / Resolution: 3.44 Å

EMDB-63883: Focused SPIN90-dimer map of SPIN90 dimer-Arp2/3 complex-filament singlet complex structure
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-63886: Focused actin filament map of SPIN90 dimer-Arp2/3 complex-filament singlet complex structure
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-63887: Arp2/3 complex from bottom half of SPIN90 dimer-Arp2/3 complex-actin filament Doublet complex
Method: EM (single particle) / Resolution: 3.13 Å

EMDB-63888: Arp2/3 complex from the top half of SPIN90 dimer-Arp2/3 complex-actin filament Doublet complex
Method: EM (single particle) / Resolution: 3.13 Å

EMDB-63889: Focused SPIN90-dimer of SPIN90 dimer-Arp2/3 complex-actin filament Doublet complex
Method: EM (single particle) / Resolution: 3.36 Å

EMDB-63890: Focused filament from second half of SPIN90 dimer-Arp2/3 complex-actin filament Doublet complex
Method: EM (single particle) / Resolution: 3.17 Å

EMDB-63891: Focused filament from one half of SPIN90 dimer-Arp2/3 complex-actin filament Doublet complex
Method: EM (single particle) / Resolution: 3.13 Å

Chemicals

ChemComp-MG:
Unknown entry

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

Source
  • bos taurus (domestic cattle)
  • homo sapiens (human)
  • gallus gallus (chicken)
KeywordsCYTOSOLIC PROTEIN / SPIN90 / actin / cytoskeleton / Arp2-3 complex / Nucleation Promoting Factor

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