ArticleNature communications2023
Integrated model of the vertebrate augmin complex.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Arabidopsis AUGMIN8 Contains Two Independent Microtubule Association Domains.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Noncentrosomal Microtubule Assembly and Its Regulation.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026Review
- Cryo-EM structures of plant Augmin reveal coiled-coil assembly, antiparallel dimerization, and NEDD1 binding.Nature communications · 2025Article
- How augmin establishes the angle of the microtubule branch site.Nature communications · 2025Article
- Conserved function of the HAUS6 calponin homology domain in anchoring augmin for microtubule branching.Nature communications · 2025Article
- Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation.Nature communications · 2025Article
- HURP facilitates spindle assembly by stabilizing microtubules and working synergistically with TPX2.Nature communications · 2024Article
- HURP facilitates spindle assembly by stabilizing microtubules and working synergistically with TPX2.bioRxiv : the preprint server for biology · 2023Article
- Microtubule binding of the human augmin complex is directly controlled by importins and Ran-GTP.Journal of cell science · 2023Article
- Augmin is a Ran-regulated spindle assembly factor.The Journal of biological chemistry · 2023Article
- Structural insights into how augmin augments the mitotic spindle.Nature communications · 2023Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.