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- Publisher Website: 10.1016/j.cell.2019.12.007
- Scopus: eid_2-s2.0-85077325865
- PMID: 31862189
- WOS: WOS:000506574100020
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Article: Asymmetric Molecular Architecture of the Human γ-Tubulin Ring Complex
Title | Asymmetric Molecular Architecture of the Human γ-Tubulin Ring Complex |
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Authors | |
Keywords | γ-tubulin ring complex microtubules microtubule nucleation single particle cryo-EM actin |
Issue Date | 2019 |
Publisher | Cell Press. The Journal's web site is located at http://www.elsevier.com/locate/cell |
Citation | Cell, 2019, v. 180 n. 1, p. 165-175.E16 How to Cite? |
Abstract | The γ-tubulin ring complex (γ-TuRC) is an essential regulator of centrosomal and acentrosomal microtubule formation, yet its structure is not known. Here, we present a cryo-EM reconstruction of the native human γ-TuRC at ∼3.8 Å resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the γ-TuRC “seam.” We also identify an unanticipated structural bridge that includes an actin-like protein and spans the γ-TuRC lumen. Despite its asymmetric architecture, the γ-TuRC arranges γ-tubulins into a helical geometry poised to nucleate microtubules. Diversity in the γ-TuRC subunits introduces large (>100,000 Å 2) surfaces in the complex that allow for interactions with different regulatory factors. The observed compositional complexity of the γ-TuRC could self-regulate its assembly into a cone-shaped structure to control microtubule formation across diverse contexts, e.g., within biological condensates or alongside existing filaments. |
Persistent Identifier | http://hdl.handle.net/10722/281995 |
ISSN | 2023 Impact Factor: 45.5 2023 SCImago Journal Rankings: 24.342 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Wieczorek, M | - |
dc.contributor.author | Urnavicius, L | - |
dc.contributor.author | Ti, S-C | - |
dc.contributor.author | Molloy, KR | - |
dc.contributor.author | Chait, BT | - |
dc.contributor.author | Kapoor, TM | - |
dc.date.accessioned | 2020-04-19T03:33:53Z | - |
dc.date.available | 2020-04-19T03:33:53Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | Cell, 2019, v. 180 n. 1, p. 165-175.E16 | - |
dc.identifier.issn | 0092-8674 | - |
dc.identifier.uri | http://hdl.handle.net/10722/281995 | - |
dc.description.abstract | The γ-tubulin ring complex (γ-TuRC) is an essential regulator of centrosomal and acentrosomal microtubule formation, yet its structure is not known. Here, we present a cryo-EM reconstruction of the native human γ-TuRC at ∼3.8 Å resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the γ-TuRC “seam.” We also identify an unanticipated structural bridge that includes an actin-like protein and spans the γ-TuRC lumen. Despite its asymmetric architecture, the γ-TuRC arranges γ-tubulins into a helical geometry poised to nucleate microtubules. Diversity in the γ-TuRC subunits introduces large (>100,000 Å 2) surfaces in the complex that allow for interactions with different regulatory factors. The observed compositional complexity of the γ-TuRC could self-regulate its assembly into a cone-shaped structure to control microtubule formation across diverse contexts, e.g., within biological condensates or alongside existing filaments. | - |
dc.language | eng | - |
dc.publisher | Cell Press. The Journal's web site is located at http://www.elsevier.com/locate/cell | - |
dc.relation.ispartof | Cell | - |
dc.subject | γ-tubulin ring complex | - |
dc.subject | microtubules | - |
dc.subject | microtubule nucleation | - |
dc.subject | single particle cryo-EM | - |
dc.subject | actin | - |
dc.title | Asymmetric Molecular Architecture of the Human γ-Tubulin Ring Complex | - |
dc.type | Article | - |
dc.identifier.email | Ti, S-C: jeffti@hku.hk | - |
dc.identifier.authority | Ti, S-C=rp02617 | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1016/j.cell.2019.12.007 | - |
dc.identifier.pmid | 31862189 | - |
dc.identifier.pmcid | PMC7027161 | - |
dc.identifier.scopus | eid_2-s2.0-85077325865 | - |
dc.identifier.hkuros | 309709 | - |
dc.identifier.volume | 180 | - |
dc.identifier.issue | 1 | - |
dc.identifier.spage | 165 | - |
dc.identifier.epage | 175.E16 | - |
dc.identifier.isi | WOS:000506574100020 | - |
dc.publisher.place | United States | - |
dc.identifier.f1000 | 737100284 | - |
dc.identifier.issnl | 0092-8674 | - |