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TitleMolecular architecture of the augmin complex.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 5449, Year 2022
Publish dateSep 16, 2022
AuthorsClinton A Gabel / Zhuang Li / Andrew G DeMarco / Ziguo Zhang / Jing Yang / Mark C Hall / David Barford / Leifu Chang /
PubMed AbstractAccurate 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 linksNat Commun / PubMed:36114186 / PubMed Central
MethodsEM (single particle)
Resolution8.0 Å
Structure data

25387

7sqk

EMDB-25387: Structure of a Protein Complex in Cell Division
PDB-7sqk: Cryo-EM structure of the human augmin complex
Method: EM (single particle) / Resolution: 8.0 Å

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / Cell Division / Mitosis / Microtubules

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