Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly.
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.
Mesh Terms:
Amino Acid Sequence, Centrosome, Cytoskeletal Proteins, Microtubule-Associated Proteins, Microtubule-Organizing Center, Microtubules, Nuclear Proteins, Protein Binding, Protein Structure, Quaternary, Protein Subunits, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Spindle Apparatus, Tubulin
Amino Acid Sequence, Centrosome, Cytoskeletal Proteins, Microtubule-Associated Proteins, Microtubule-Organizing Center, Microtubules, Nuclear Proteins, Protein Binding, Protein Structure, Quaternary, Protein Subunits, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Spindle Apparatus, Tubulin
Mol. Biol. Cell
Date: Jul. 15, 2016
PubMed ID: 27226487
View in: Pubmed Google Scholar
Download Curated Data For This Publication
205231
Switch View:
- Interactions 2