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Mol Biol Cell. 2016 Jul 15;27(14):2245-58. doi: 10.1091/mbc.E16-02-0072. Epub 2016 May 25.

Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly.

Author information

1
Department of Biochemistry and Biophysics and Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158.
2
Department of Biochemistry, University of Washington, Seattle, WA 98195.
3
Department of Biochemistry and Biophysics and Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94158 agard@msg.ucsf.edu.

Abstract

The microtubule (MT) cytoskeleton plays important roles in many cellular processes. In vivo, MT nucleation is controlled by the γ-tubulin ring complex (γTuRC), a 2.1-MDa complex composed of γ-tubulin small complex (γTuSC) subunits. The mechanisms underlying the assembly of γTuRC are largely unknown. In yeast, the conserved protein Spc110p both stimulates the assembly of the γTuRC and anchors the γTuRC to the spindle pole body. Using a quantitative in vitro FRET assay, we show that γTuRC assembly is critically dependent on the oligomerization state of Spc110p, with higher-order oligomers dramatically enhancing the stability of assembled γTuRCs. Our in vitro findings were confirmed with a novel in vivo γTuSC recruitment assay. We conclude that precise spatial control over MT nucleation is achieved by coupling localization and higher-order oligomerization of the receptor for γTuRC.

PMID:
27226487
PMCID:
PMC4945142
DOI:
10.1091/mbc.E16-02-0072
[Indexed for MEDLINE]
Free PMC Article

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