ArticleNature communications2022
Molecular architecture of the augmin complex.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 26 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
- Thyme Oil Alleviates Cadmium-Induced Disturbances in Mitotic Activity, Cytoskeletal Organization and H3T3/H3S10 Phosphorylation inInternational journal of molecular sciences · 2026Article
- The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026Review
- Development and Validation of a HAUS-Related Prognostic Signature in Liver Hepatocellular Carcinoma: A Multi-Omics Integration from Pan-Cancer Analysis to Single-Cell Resolution.Journal of hepatocellular carcinoma · 2026Article
- 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
- Photo-crosslinkers boost structural information from crosslinking mass spectrometry.Current opinion in structural biology · 2025Review
- Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation.Nature communications · 2025Article
- Regulation of Axonal Microtubule Polarity Orientation in Different Kinds of Neurons.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Structural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC.Nature communications · 2025Article
- Structure of E6AP in complex with HPV16-E6 and p53 reveals a novel ordered domain important for E3 ligase activation.Structure (London, England : 1993) · 2025Article
- Genome ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- AlphaFold two years on: Validation and impact.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Augmin complex activity finetunes dendrite morphology through non-centrosomal microtubule nucleation in vivo.Journal of cell science · 2024Article
- γ-TuRCs and the augmin complex are required for the development of highly branched dendritic arbors in Drosophila.Journal of cell science · 2024Article
- The microtubule-nucleating factor MACERATOR tethers AUGMIN7 to microtubules and governs phragmoplast architecture.The Plant cell · 2024Article
- Microtubule binding of the human augmin complex is directly controlled by importins and Ran-GTP.Journal of cell science · 2023Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Accurate segregation of chromosomes during mitosis depends on the correct assembly of the mitotic spindle, a bipolar structure composed mainly of microtubules. The augmin complex, or homologous to augmin subunits (HAUS) complex, is an eight-subunit protein complex required for building robust mitotic spindles in metazoa. Augmin increases microtubule density within the spindle by recruiting the γ-tubulin ring complex (γ-TuRC) to pre-existing microtubules and nucleating branching microtubules. Here, we elucidate the molecular architecture of augmin by single particle cryo-electron microscopy (cryo-EM), computational methods, and crosslinking mass spectrometry (CLMS). Augmin's highly flexible structure contains a V-shaped head and a filamentous tail, with the head existing in either extended or contracted conformational states. Our work highlights how cryo-EM, complemented by computational advances and CLMS, can elucidate the structure of a challenging protein complex and provides insights into the function of augmin in mediating microtubule branching 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.