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- Publisher Website: 10.1083/jcb.202007101
- Scopus: eid_2-s2.0-85159770592
- WOS: WOS:001006685600001
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Article: Autoinhibitory mechanism controls binding of centrosomin motif 1 to γ-tubulin ring complex
Title | Autoinhibitory mechanism controls binding of centrosomin motif 1 to γ-tubulin ring complex |
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Authors | |
Issue Date | 22-May-2023 |
Publisher | Rockefeller University Press |
Citation | Journal of Cell Biology, 2023, v. 222, n. 7 How to Cite? |
Abstract | The γ-tubulin ring complex (γTuRC) is the principal nucleator of cellular microtubules, and the microtubule-nucleating activity of the complex is stimulated by binding to the γTuRC-mediated nucleation activator (γTuNA) motif. The γTuNA is part of the centrosomin motif 1 (CM1), which is widely found in γTuRC stimulators, including CDK5RAP2. Here, we show that a conserved segment within CM1 binds to the γTuNA and blocks its association with γTuRCs; therefore, we refer to this segment as the γTuNA inhibitor (γTuNA-In). Mutational disruption of the interaction between the γTuNA and the γTuNA-In results in a loss of autoinhibition, which consequently augments microtubule nucleation on centrosomes and the Golgi complex, the two major microtubule-organizing centers. This also causes centrosome repositioning, leads to defects in Golgi assembly and organization, and affects cell polarization. Remarkably, phosphorylation of the γTuNA-In, probably by Nek2, counteracts the autoinhibition by disrupting the γTuNA‒γTuNA-In interaction. Together, our data reveal an on-site mechanism for controlling γTuNA function. |
Persistent Identifier | http://hdl.handle.net/10722/331698 |
ISSN | 2023 Impact Factor: 7.4 2023 SCImago Journal Rankings: 3.717 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Yang, Shaozhong | - |
dc.contributor.author | Au, Franco KC | - |
dc.contributor.author | Li, Gefei | - |
dc.contributor.author | Lin, Jianwei | - |
dc.contributor.author | Li, Xiang David | - |
dc.contributor.author | Qi, Robert Z | - |
dc.date.accessioned | 2023-09-21T06:58:07Z | - |
dc.date.available | 2023-09-21T06:58:07Z | - |
dc.date.issued | 2023-05-22 | - |
dc.identifier.citation | Journal of Cell Biology, 2023, v. 222, n. 7 | - |
dc.identifier.issn | 0021-9525 | - |
dc.identifier.uri | http://hdl.handle.net/10722/331698 | - |
dc.description.abstract | <p>The γ-tubulin ring complex (γTuRC) is the principal nucleator of cellular microtubules, and the microtubule-nucleating activity of the complex is stimulated by binding to the γTuRC-mediated nucleation activator (γTuNA) motif. The γTuNA is part of the centrosomin motif 1 (CM1), which is widely found in γTuRC stimulators, including CDK5RAP2. Here, we show that a conserved segment within CM1 binds to the γTuNA and blocks its association with γTuRCs; therefore, we refer to this segment as the γTuNA inhibitor (γTuNA-In). Mutational disruption of the interaction between the γTuNA and the γTuNA-In results in a loss of autoinhibition, which consequently augments microtubule nucleation on centrosomes and the Golgi complex, the two major microtubule-organizing centers. This also causes centrosome repositioning, leads to defects in Golgi assembly and organization, and affects cell polarization. Remarkably, phosphorylation of the γTuNA-In, probably by Nek2, counteracts the autoinhibition by disrupting the γTuNA‒γTuNA-In interaction. Together, our data reveal an on-site mechanism for controlling γTuNA function.<br></p> | - |
dc.language | eng | - |
dc.publisher | Rockefeller University Press | - |
dc.relation.ispartof | Journal of Cell Biology | - |
dc.title | Autoinhibitory mechanism controls binding of centrosomin motif 1 to γ-tubulin ring complex | - |
dc.type | Article | - |
dc.identifier.doi | 10.1083/jcb.202007101 | - |
dc.identifier.scopus | eid_2-s2.0-85159770592 | - |
dc.identifier.volume | 222 | - |
dc.identifier.issue | 7 | - |
dc.identifier.eissn | 1540-8140 | - |
dc.identifier.isi | WOS:001006685600001 | - |
dc.identifier.issnl | 0021-9525 | - |