Cep97 Is Required for Centriole Structural Integrity and Cilia Formation in Drosophila
Abstract
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 acetyl marks 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.
Related
- In Step, the sole Drosophila TENT5 poly(A) polymerase, is required for spermatid elongation and individualization
- Centrosome maintains the integrity of and repairs mature olfactory cilia in adult Drosophila
- SAF-A/HNRNPU regulates euchromatin dynamics and is required for nuclear envelope integrity
- PEELING WALLS1 encodes a GT106 protein required for seed surface integrity
- Spectraplakin is required for dendritic microtubule organization via a tip-based mechanism in Drosophila
BibTeX
@article{dobbelaere2026cep97,
title = {{Cep97 Is Required for Centriole Structural Integrity and Cilia Formation in Drosophila}},
author = {Jeroen Dobbelaere and Marketa Schmidt Cernohorska and Martina Huranova and Dea Slade and Alexander Dammermann},
journal = {Current Biology},
year = {2026},
month = oct,
doi = {10.1016/j.cub.2020.05.078},
url = {https://hal.science/hal-05787702v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - Cep97 Is Required for Centriole Structural Integrity and Cilia Formation in Drosophila
AU - Jeroen Dobbelaere
AU - Marketa Schmidt Cernohorska
AU - Martina Huranova
AU - Dea Slade
AU - Alexander Dammermann
PY - 2026
DA - 2026/10/08
JO - Current Biology
DO - 10.1016/j.cub.2020.05.078
UR - https://hal.science/hal-05787702v1
AB - 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 acetyl marks 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.
SN - 0960-9822
SN - 1879-0445
ER -