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Publication Abstract from PubMed

The gamma-tubulin ring complex (gamma-TuRC) is a structural template for controlled nucleation of microtubules from alpha/beta-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes gamma-TuRC assembly from seven gamma-tubulin small complexes (gamma-TuSCs) and recruits the microtubule polymerase Stu2, yet their molecular interplay remains unclear. Here, we determine the cryo-EM structure of the Candida albicans cytoplasmic nucleation unit at 3.6 A resolution, revealing how the gamma-TuRC is assembled and conformationally primed for microtubule nucleation by the dimerised Spc72 CM1 motif. Two coiled-coil regions of Spc72 interact with the conserved C-terminal alpha-helix of Stu2 and thereby position the alpha/beta-tubulin-binding TOG domains of Stu2 in the vicinity of the microtubule assembly site. Collectively, we reveal the function of CM1 motifs in gamma-TuSC oligomerisation and the recruitment of microtubule polymerases to the gamma-TuRC.

Structural insights into the interplay between microtubule polymerases, gamma-tubulin complexes and their receptors.,Zheng A, Vermeulen BJA, Wurtz M, Neuner A, Lubbehusen N, Mayer MP, Schiebel E, Pfeffer S Nat Commun. 2025 Jan 5;16(1):402. doi: 10.1038/s41467-024-55778-7. PMID:39757296^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.