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ProteomicsCross-linking/mass spectrometry analysis of AUGMIN complex
We applied cross-linking/mass spectrometry to characterize in vivo Augmin from Drosophila in absence of any other structural information. The identified cross-links revealed topology of the Augmin complex and allowed us to predict potential interfaces between Augmin and γ-TuRC.
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2017-04-04 | PXD006246 | Pride
Augmin complex Cross-linking/mass spectromentry 
ProteomicsThe augmin complex architecture reveals structural insights into microtubule branching
In mitosis, the augmin complex binds to spindle microtubules to recruit the γ-tubulin ring complex (γ-TuRC), the principal microtubule nucleator, for the formation of branched microtubules. Our understanding of augmin-mediated microtubule branching is strongly hampered by the lack of structural info...
ORGANISM(S): Xenopus laevis (African clawed frog) 
2022-10-13 | PXD034895 | Pride
Microtubule Augmin Nucleation Cell cycle Branching 
ProteomicsCryo-EM structures of the Plant Augmin reveal its intertwined coiled-coil assembly, antiparallel dimerization and NEDD1 binding mechanisms
Microtubule (MT) branch nucleation is fundamental for building parallel MT networks in eukaryotic cells. In plants and metazoans, MT branch nucleation requires Augmin and NEDD1 proteins which bind along MTs and then recruit and activate the gamma-tubulin ring complex (g-TuRC). Augmin is a fork-shap...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-10-31 | PXD065516 | Pride
Microtubule Augmin G-turc Xl-ms Nedd1 
ProteomicsSub-centrosomal mapping identifies augmin-TuRC as part of a centriole-stabilizing scaffold
Centriole biogenesis and maintenance are crucial for cells to generate cilia and assemble centrosomes that function as microtubule organizing centers (MTOCs). Centriole biogenesis and MTOC function both require the microtubule nucleator -tubulin ring complex (TuRC). It is widely accepted that TuRC n...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD027352 | Pride
Augmin Ciliogenesis Microtubules Centriole turc 
UnknownMolecular architecture of the augmin complex.
Not available
S-EPMC9481612 | biostudies-literature
ProteomicsThe HAUS6 CH domain binds microtubules to orient augmin for microtubule branching
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 de...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) Homo sapiens (Human) Escherichia coli Drosophila melanogaster (Fruit fly) Xenopus laevis (African clawed frog) 
2025-07-30 | PXD060099 | Pride
Microtubule nucleation Microtubules Cell division 
UnknownIntegrated model of the vertebrate augmin complex.
Not available
S-EPMC10102177 | biostudies-literature
UnknownThe augmin complex architecture reveals structural insights into microtubule branching.
Not available
S-EPMC9512787 | biostudies-literature
UnknownIdentification of the augmin complex in the filamentous fungus Aspergillus nidulans.
Not available
S-EPMC4086812 | biostudies-literature
UnknownAugmin is a Ran-regulated spindle assembly factor.
Not available
S-EPMC10318467 | biostudies-literature
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