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Structure paper

TitleStructural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 2453, Year 2025
Publish dateMar 12, 2025
AuthorsQi Gao / Florian W Hofer / Sebastian Filbeck / Bram J A Vermeulen / Martin Würtz / Annett Neuner / Charlotte Kaplan / Maja Zezlina / Cornelia Sala / Hyesu Shin / Oliver J Gruss / Elmar Schiebel / Stefan Pfeffer /
PubMed AbstractThe γ-tubulin ring complex (γ-TuRC) acts as a structural template for microtubule formation at centrosomes, associating with two main compartments: the pericentriolar material and the centriole ...The γ-tubulin ring complex (γ-TuRC) acts as a structural template for microtubule formation at centrosomes, associating with two main compartments: the pericentriolar material and the centriole lumen. In the pericentriolar material, the γ-TuRC is involved in microtubule organization, while the function of the centriole lumenal pool remains unclear. The conformational landscape of the γ-TuRC, which is crucial for its activity, and its centrosomal anchoring mechanisms, which determine γ-TuRC activity and turnover, are not understood. Using cryo-electron tomography, we analyze γ-TuRCs in human cells and purified centrosomes. Pericentriolar γ-TuRCs simultaneously associate with the essential adapter NEDD1 and the microcephaly protein CDK5RAP2. NEDD1 forms a tetrameric structure at the γ-TuRC base through interactions with four GCP3/MZT1 modules and GCP5/6-specific extensions, while multiple copies of CDK5RAP2 engage the γ-TuRC in two distinct binding patterns to promote γ-TuRC closure and activation. In the centriole lumen, the microtubule branching factor Augmin tethers a condensed cluster of γ-TuRCs to the centriole wall with defined directional orientation. Centriole-lumenal γ-TuRC-Augmin is protected from degradation during interphase and released in mitosis to aid chromosome alignment. This study provides a unique view on γ-TuRC structure and molecular organization at centrosomes and identifies an important cellular function of centriole-lumenal γ-TuRCs.
External linksNat Commun / PubMed:40074789 / PubMed Central
MethodsEM (subtomogram averaging) / EM (single particle)
Resolution4.3 - 31.0 Å
Structure data

EMDB-52717: 'Consensus refinement' of the human gamma-tubulin ring complex in purified centrosomes
Method: EM (subtomogram averaging) / Resolution: 16.4 Å

52718

9i8g

EMDB-52718: 'Inwards conformation' of the human gamma-TuRC from purified centrosomes
PDB-9i8g: Inwards conformation' of the human gamma-TuRC from purified centrosomes obtained by rigid body docking
Method: EM (subtomogram averaging) / Resolution: 22.4 Å

52719

9i8h

EMDB-52719: 'Outwards conformation' of the human gamma-TuRC from purified centrosomes
PDB-9i8h: Outwards conformation' of the human gamma-TuRC from purified centrosomes obtained by rigid body docking
Method: EM (subtomogram averaging) / Resolution: 23.2 Å

EMDB-52720: Human gamma-tubulin ring complex from purified centrosomes of CDK5RAP2-knockout cells
Method: EM (subtomogram averaging) / Resolution: 31.0 Å

EMDB-52721: Human gamma-tubulin ring complex from purified centrosomes of RPE1 cells
Method: EM (subtomogram averaging) / Resolution: 25.0 Å

EMDB-52722: Human gamma-tubulin ring complex in centrosomes of HCT116 and HeLa cells
Method: EM (subtomogram averaging) / Resolution: 30.6 Å

EMDB-52723: Human microtubule triplet in centrosomes of HeLa cells
Method: EM (subtomogram averaging) / Resolution: 30.5 Å

EMDB-52728: Spoke 12-14 of the NEDD1-bound native vertebrate gamma-tubulin ring complex from Xenopus laevis
Method: EM (single particle) / Resolution: 7.5 Å

52729

9i8m

EMDB-52729, PDB-9i8m:
NEDD1-bound native vertebrate gamma-tubulin ring complex from Xenopus laevis, focused reconstruction
Method: EM (single particle) / Resolution: 4.3 Å

52730

9i8n

EMDB-52730, PDB-9i8n:
NEDD1-bound native vertebrate gamma-tubulin ring complex from Xenopus laevis
Method: EM (single particle) / Resolution: 4.6 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
  • xenopus laevis (African clawed frog)
KeywordsCELL CYCLE / centrosome / cytoskeleton / microtubule / microtubule nucleation / complex / template / cap / gamma-tubulin / gamma-tubulin ring complex / nedd1 / neural precursor cell-expressed developmentally down-regulated 1 / CDK5RAP2 / cyclin-dependent kinase 5 regulatory subunit associated protein 2

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