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Article: Autoinhibitory mechanism controls binding of centrosomin motif 1 to γ-tubulin ring complex

TitleAutoinhibitory mechanism controls binding of centrosomin motif 1 to γ-tubulin ring complex
Authors
Issue Date22-May-2023
PublisherRockefeller 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 Identifierhttp://hdl.handle.net/10722/331698
ISSN
2023 Impact Factor: 7.4
2023 SCImago Journal Rankings: 3.717
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYang, Shaozhong-
dc.contributor.authorAu, Franco KC-
dc.contributor.authorLi, Gefei-
dc.contributor.authorLin, Jianwei-
dc.contributor.authorLi, Xiang David-
dc.contributor.authorQi, Robert Z-
dc.date.accessioned2023-09-21T06:58:07Z-
dc.date.available2023-09-21T06:58:07Z-
dc.date.issued2023-05-22-
dc.identifier.citationJournal of Cell Biology, 2023, v. 222, n. 7-
dc.identifier.issn0021-9525-
dc.identifier.urihttp://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.languageeng-
dc.publisherRockefeller University Press-
dc.relation.ispartofJournal of Cell Biology-
dc.titleAutoinhibitory mechanism controls binding of centrosomin motif 1 to γ-tubulin ring complex-
dc.typeArticle-
dc.identifier.doi10.1083/jcb.202007101-
dc.identifier.scopuseid_2-s2.0-85159770592-
dc.identifier.volume222-
dc.identifier.issue7-
dc.identifier.eissn1540-8140-
dc.identifier.isiWOS:001006685600001-
dc.identifier.issnl0021-9525-

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