Cep97 Is Required for Centriole Structural Integrity and Cilia Formation in Drosophila
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F20%3A00531953" target="_blank" >RIV/68378050:_____/20:00531953 - isvavai.cz</a>
Result on the web
<a href="https://www.cell.com/current-biology/fulltext/S0960-9822(20)30765-X?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS096098222030765X%3Fshowall%3Dtrue" target="_blank" >https://www.cell.com/current-biology/fulltext/S0960-9822(20)30765-X?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS096098222030765X%3Fshowall%3Dtrue</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.cub.2020.05.078" target="_blank" >10.1016/j.cub.2020.05.078</a>
Alternative languages
Result language
angličtina
Original language name
Cep97 Is Required for Centriole Structural Integrity and Cilia Formation in Drosophila
Original language description
Centrioles are highly elaborate microtubule-based structures responsible for the formation of centrosomes and cilia. Despite considerable variation across species and tissues within any given tissue, their size is essentially constant [1, 2]. While the diameter of the centriole cylinder is set by the dimensions of the inner scaffolding structure of the cartwheel [3], how centriole length is set so precisely and stably maintained over many cell divisions is not well understood. Cep97 and CP110 are conserved proteins that localize to the distal end of centrioles and have been reported to limit centriole elongation in vertebrates [4, 5]. Here, we examine Cep97 function in Drosophila melanogaster. We show that Cep97 is essential for formation of full-length centrioles in multiple tissues of the fly. We further identify the microtubule deacetylase Sirt2 as a Cep97 interactor. Deletion of Sirt2 likewise affects centriole size. Interestingly, so does deletion of the acetylase Atat1, indicating that loss of stabilizing acetylmarks impairs centriole integrity. Cep97 and CP110 were originally identified as inhibitors of cilia formation in vertebrate cultured cells [6], and loss of CP110 is a widely used marker of basal body maturation. In contrast, in Drosophila, Cep97 appears to be only transiently removed from basal bodies and loss of Cep97 strongly impairs ciliogenesis. Collectively, our results support a model whereby Cep97 functions as part of a protective cap that acts together with the microtubule acetylation machinery to maintain centriole stability, essential for proper function in cilium biogenesis.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10601 - Cell biology
Result continuities
Project
<a href="/en/project/GJ17-20613Y" target="_blank" >GJ17-20613Y: BBSome and actin interplay in ciliogenesis and formation of the immunological synapse</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Current Biology
ISSN
0960-9822
e-ISSN
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Volume of the periodical
30
Issue of the periodical within the volume
15
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
3045-3056
UT code for WoS article
000555598100019
EID of the result in the Scopus database
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