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Crosslinking mass spectrometry analysis of ?TuRC complex

ABSTRACT: The ?-tubulin ring complex (?TuRC) is the major microtubule nucleator in cells. The mechanism of its regulation is not understood. To understand the molecular basis of microtubule nucleation, we investigate the structure of ?TuRC using crosslinking mass spectrometry.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Zhuo Chen

LAB HEAD: Juri Rappsilber

PROVIDER: PXD018106 | Pride | 2021-01-27

REPOSITORIES: Pride

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			Action	DRS
	B200124_02_Lumos_ZC_CO_160_BS3xTuRC-1.raw	Raw
	B200124_03_Lumos_ZC_CO_160_BS3xTuRC-2.raw	Raw
	B200124_05_Lumos_ZC_CO_140_BS3xTuRC_SEC_f5-1.raw	Raw
	B200124_06_Lumos_ZC_CO_140_BS3xTuRC_SEC_f5-2.raw	Raw
	B200124_07_Lumos_ZC_CO_140_BS3xTuRC_SEC_f6-1.raw	Raw

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Publications

Microtubule Nucleation Properties of Single Human γTuRCs Explained by Their Cryo-EM Structure.

Consolati Tanja T Locke Julia J Roostalu Johanna J Chen Zhuo Angel ZA Gannon Julian J Asthana Jayant J Lim Wei Ming WM Martino Fabrizio F Cvetkovic Milos A MA Rappsilber Juri J Costa Alessandro A Surrey Thomas T

Developmental cell 20200519 5

The γ-tubulin ring complex (γTuRC) is the major microtubule nucleator in cells. The mechanism of its regulation is not understood. We purified human γTuRC and measured its nucleation properties in a total internal reflection fluorescence (TIRF) microscopy-based real-time nucleation assay. We find that γTuRC stably caps the minus ends of microtubules that it nucleates stochastically. Nucleation is inefficient compared with microtubule elongation. The 4 Å resolution cryoelectron microscopy (cryo-E ...[more]

PMID: 32433913

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The augmin complex architecture reveals structural insights into microtubule branching

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