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Cited by 16Microtubule and mitosis dynamicsGenomics and Chromatin DynamicsProtein Structure and Dynamics

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Integrated model of the vertebrate augmin complex

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Travis, Sophie M., Mahon, Brian P., Huang, Wei, Ma, Meisheng, Rale, Michael J., Kraus, Jodi, Taylor, Derek J., Zhang, Rui, Petry, Sabine·2023·Nature Communications
DOI 10.1038/s41467-023-37519-4PMC PMC10102177

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Abstract

Accurate segregation of chromosomes is required to maintain genome integrity during cell division. This feat is accomplished by the microtubule-based spindle. To build a spindle rapidly and with high fidelity, cells take advantage of branching microtubule nucleation, which rapidly amplifies microtubules during cell division. Branching microtubule nucleation relies on the hetero-octameric augmin complex, but lack of structure information about augmin has hindered understanding how it promotes branching. In this work, we combine cryo-electron microscopy, protein structural prediction, and visualization of fused bulky tags via negative stain electron microscopy to identify the location and orientation of each subunit within the augmin structure. Evolutionary analysis shows that augmin’s structure is highly conserved across eukaryotes, and that augmin contains a previously unidentified microtubule binding site. Thus, our findings provide insight into the mechanism of branching microtubule nucleation.

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Metadata

Authors
Travis, S. M., Mahon, B. P., Huang, W., Ma, M., Rale, M. J., Kraus, J., Taylor, D. J., Zhang, R., & Petry, S.
Affiliations
  • Princeton University (US)
  • Case Western Reserve University (US)
  • Washington University in St. Louis (US)
  • Harvard University (US)
Corresponding author
  • Zhang, Rui
  • Petry, Sabine
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2023-04-13
Volume
14
Issue
1
Pages
2072-2072
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-023-37519-4
PMC
PMC10102177
OpenAlex
W4365447709
Cited by
16
References
3
Citations by year
2026: 2 · 2025: 7 · 2024: 2 · 2023: 4
FWCI
2.17
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Digital Commons@Becker (Washington University School of Medicine) (submittedVersion, cc-by)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (F32GM142149, 1R01GM138854, 1R01GM141100-01A1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
microtubule-binding site, mitotic spindle assembly, chromosome segregation, protein structure, evolutionary conservation
MeSH terms
Animals, Binding Sites, Microtubule-Associated Proteins, Microtubules, Spindle Apparatus, Tubulin, Vertebrates, Cryoelectron Microscopy

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