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TitleCryo-EM structures of plant Augmin reveal coiled-coil assembly, antiparallel dimerization, and NEDD1 binding.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 11440, Year 2025
Publish dateDec 12, 2025
AuthorsMd Ashaduzzaman / Aryan Taheri / Yuh-Ru Julie Lee / Yuqi Tang / Shubham Mittal / Fei Guo / Faruck Morcos / Stephen D Fried / Bo Liu / Jawdat Al-Bassam /
PubMed AbstractMicrotubule (MT) branch nucleation requires Augmin and NEDD1 proteins, which recruit and activate the gamma-tubulin ring complex (γ-TuRC). Augmin is a fork-shaped assembly of eight coiled-coil ...Microtubule (MT) branch nucleation requires Augmin and NEDD1 proteins, which recruit and activate the gamma-tubulin ring complex (γ-TuRC). Augmin is a fork-shaped assembly of eight coiled-coil subunits, while NEDD1 is a β-propeller protein bridging MTs, Augmin, and γ-TuRC. We reconstitute Arabidopsis thaliana Augmin assemblies and determine 3.7-7.3-Å cryo-EM structures of its V-junction and extended regions using crosslinking mass spectrometry. These structures reveal a complete plant Augmin model showing multi-coiled-coil interfaces stabilizing its 40-nm hetero-octameric fork architecture. The dual calponin homology (CH) domains at the V-junction terminus adopt open and closed conformations for MT binding. A 12-Å cryo-EM structure shows Augmin undergoes anti-parallel dimerization through conserved surfaces on its extended region. We determine the NEDD1 β-propeller structure with Augmin, revealing direct binding inside the V-junction that enhances dimerization. Direct coupling and evolutionary analyses identify co-varying residue pairs validating the eight-subunit model and NEDD1 interface. Cooperativity between dual CH domains and NEDD1 binding may regulate V-junction binding to MT lattices. This V-shaped dual binding anchors Augmin along MTs, creating platforms for γ-TuRC recruitment and branched MT nucleation.
External linksNat Commun / PubMed:41387433 / PubMed Central
MethodsEM (single particle)
Resolution8.0 Å
Structure data

72072

9pzm

EMDB-72072, PDB-9pzm:
Augmin V junction with NEDD1 (WD)
Method: EM (single particle) / Resolution: 8.0 Å

Source
  • arabidopsis thaliana (thale cress)
KeywordsPLANT PROTEIN / Microtubule nucleator

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