Molecular architecture of the augmin complex

Clinton A. Gabel, Zhuang Li, Andrew G. DeMarco, Ziguo Zhang, Jing Yang, Mark C. Hall, David Barford and Leifu Chang ()
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Clinton A. Gabel: Purdue University
Zhuang Li: Purdue University
Andrew G. DeMarco: Purdue University
Ziguo Zhang: MRC Laboratory of Molecular Biology
Jing Yang: MRC Laboratory of Molecular Biology
Mark C. Hall: Purdue University
David Barford: MRC Laboratory of Molecular Biology
Leifu Chang: Purdue University

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-33227-7

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