Centriole distal-end proteins CP110 and Cep97 influence centriole cartwheel growth at the proximal end.


Journal

Journal of cell science
ISSN: 1477-9137
Titre abrégé: J Cell Sci
Pays: England
ID NLM: 0052457

Informations de publication

Date de publication:
15 07 2022
Historique:
received: 14 03 2022
accepted: 13 06 2022
pubmed: 17 6 2022
medline: 22 7 2022
entrez: 16 6 2022
Statut: ppublish

Résumé

Centrioles are composed of a central cartwheel tethered to nine-fold symmetric microtubule (MT) blades. The centriole cartwheel and MTs are thought to grow from opposite ends of these organelles, so it is unclear how they coordinate their assembly. We previously showed that in Drosophila embryos an oscillation of Polo-like kinase 4 (Plk4) helps to initiate and time the growth of the cartwheel at the proximal end. Here, in the same model, we show that CP110 and Cep97 form a complex close to the distal-end of the centriole MTs whose levels rise and fall as the new centriole MTs grow, in a manner that appears to be entrained by the core cyclin-dependent kinase (Cdk)-Cyclin oscillator that drives the nuclear divisions in these embryos. These CP110 and Cep97 dynamics, however, do not appear to time the period of centriole MT growth directly. Instead, we find that changing the levels of CP110 and Cep97 appears to alter the Plk4 oscillation and the growth of the cartwheel at the proximal end. These findings reveal an unexpected potential crosstalk between factors normally concentrated at opposite ends of the growing centrioles, which might help to coordinate centriole growth. This article has an associated First Person interview with the first authors of the paper.

Identifiants

pubmed: 35707992
pii: 275722
doi: 10.1242/jcs.260015
pmc: PMC9450887
pii:
doi:

Substances chimiques

Cell Cycle Proteins 0
Microtubule-Associated Proteins 0
Phosphoproteins 0
PLK4 protein, human EC 2.7.1.-
Protein Serine-Threonine Kinases EC 2.7.11.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : University of California, San Francisco
ID : 2017078
Organisme : Wellcome Trust
ID : 104575
Pays : United Kingdom
Organisme : Edward Penley Abraham Scholarship
Organisme : Sandler Foundation
ID : 7029760
Organisme : Ludwig Institute for Cancer Research
Organisme : University of Oxford

Informations de copyright

© 2022. Published by The Company of Biologists Ltd.

Déclaration de conflit d'intérêts

Competing interests Laura Hankins is currently an employee of The Company of Biologists and had no role in the review of the paper. The authors declare no other competing interests for this study.

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Auteurs

Mustafa G Aydogan (MG)

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158, USA.

Laura E Hankins (LE)

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.

Thomas L Steinacker (TL)

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.

Mohammad Mofatteh (M)

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.

Saroj Saurya (S)

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.

Alan Wainman (A)

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.

Siu-Shing Wong (SS)

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.

Xin Lu (X)

Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, UK.

Felix Y Zhou (FY)

Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, UK.

Jordan W Raff (JW)

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.

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