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-Structure paper
Title | Molecular architecture of the augmin complex. |
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Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 5449, Year 2022 |
Publish date | Sep 16, 2022 |
Authors | Clinton A Gabel / Zhuang Li / Andrew G DeMarco / Ziguo Zhang / Jing Yang / Mark C Hall / David Barford / Leifu Chang / |
PubMed 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 ...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. |
External links | Nat Commun / PubMed:36114186 / PubMed Central |
Methods | EM (single particle) |
Resolution | 8.0 Å |
Structure data | EMDB-25387, PDB-7sqk: |
Source |
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Keywords | CELL CYCLE / Cell Division / Mitosis / Microtubules |