Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Conserved function of the HAUS6 calponin homology domain in anchoring augmin for microtubule branching.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 7845, Year 2025
Publish date	Aug 22, 2025
Authors	Martin Würtz / Giulia Tonon / Bram J A Vermeulen / Maja Zezlina / Qi Gao / Annett Neuner / Angelika Seidl / Melanie König / Maximilian Harkenthal / Sebastian Eustermann / Sylvia Erhardt / Fabio Lolicato / Elmar Schiebel / Stefan Pfeffer /
PubMed Abstract	Branching microtubule nucleation is a key mechanism for mitotic and meiotic spindle assembly and requires the hetero-octameric augmin complex. Augmin recruits the major microtubule nucleator, the γ- ...Branching microtubule nucleation is a key mechanism for mitotic and meiotic spindle assembly and requires the hetero-octameric augmin complex. Augmin recruits the major microtubule nucleator, the γ-tubulin ring complex, to pre-existing microtubules to direct the formation of new microtubules in a defined orientation. Although recent structural work has provided key insights into the structural organization of augmin, molecular details of its interaction with microtubules remain elusive. Here, we identify the minimal conserved microtubule-binding unit of augmin across species and demonstrate that stable microtubule anchoring is predominantly mediated via the calponin homology (CH) domain in Dgt6/HAUS6. Comparative sequence and functional analyses in vitro and in vivo reveal a highly conserved functional role of the HAUS6 CH domain in microtubule binding. Using cryo-electron microscopy and molecular dynamics simulations in combination with AlphaFold structure predictions, we show that the D. melanogaster Dgt6/HAUS6 CH domain binds microtubules at the inter-protofilament groove between two adjacent β-tubulin subunits and thereby orients augmin on microtubules. Altogether, our findings reveal how augmin binds microtubules to pre-determine the branching angle during microtubule nucleation and facilitate the rapid assembly of complex microtubule networks.
External links	Nat Commun / PubMed:40846850 / PubMed Central
Methods	EM (helical sym.) / EM (single particle)
Resolution	3.9 - 4.9 Å
Structure data	EMDB-52832: Helical reconstruction of a D. melanogaster N-clamp-decorated microtubule Method: EM (helical sym.) / Resolution: 4.0 Å 54160 9rpd EMDB-54160: D. melanogaster augmin TII N-clamp (GST-fusion) bound to a microtubule PDB-9rpd: D. melanogaster Augmin TII N-clamp (GST-fusion) bound to a microtubule, well-defined subset of particles Method: EM (single particle) / Resolution: 3.9 Å 54161 9rpd EMDB-54161, PDB-9rpd: D. melanogaster Augmin TII N-clamp (GST-fusion) bound to a microtubule, well-defined subset of particles Method: EM (single particle) / Resolution: 4.9 Å EMDB-54174: D. melanogaster Augmin TII N-clamp bound to a microtubule Method: EM (single particle) / Resolution: 4.7 Å
Source	drosophila melanogaster (fruit fly) sus scrofa (pig) schistosoma japonicum (invertebrata) aequorea victoria (jellyfish)
Keywords	CELL CYCLE / augmin / N-clamp / TII / microtubule / branching / nucleation / HAUS / HAUS augmin-like complex subunit / HAUS6 / HAUS7 / HAUS2 / HAUS8 / Dgt6 / Msd5 / Dgt4 / Msd1 / Drosophila melanogaster / complex / CH domain / calponin homology domain / MAP / cell division