<i>Tetrahymena</i> Poc5 is a transient basal body component that is important for basal body maturation

Heydeck, Westley; Bayless, Brian A.; Stemm-Wolf, Alexander J.; O’Toole, Eileen; Fabritius, Amy S.; Ozzello, Courtney; Nguyen, Marina; Winey, Mark

doi:10.1242/jcs.240838

Cited by 9 publications

(6 citation statements)

References 102 publications

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“…Loss-of-function experiments revealed CCDC15 functions during regulation of centriole size and integrity. Since inner scaffold proteins WDR90 and POC5 were also described to have similar functions, our results corroborate the role of the inner scaffold in these processes (Azimzadeh et al, 2009;Heydeck et al, 2020;Mercey et al, 2022;Steib et al, 2020). While WDR90 and POC5 depletion resulted in longer centrioles in interphase and shorter centrioles in prometaphase in U2OS cells, CCDC15 depletion resulted in shorter centrioles in RPE1 cells (Steib et al, 2020).…”

Section: Discussionsupporting

confidence: 85%

“…As shown in Fig. S1, Centrin-2 and POC5 proximity interactomes were enriched for GO categories that are relevant for their published functions during centrosomal and/or nuclear biological processes and related cellular compartments (Azimzadeh et al, 2009; Dantas et al, 2013; Heydeck et al, 2020; Khouj et al, 2019; Resendes et al, 2008; Salisbury et al, 2002; Steib et al, 2020; Yang et al, 2010; Ying et al, 2019). For example, the highly enriched GO categories for biological processes include cell division, protein folding, mRNA splicing, and chromatin remodeling for Centrin-2 and centriole replication, protein localization to centrosome and cilium assembly for POC5 (Fig.…”

Section: Resultsmentioning

confidence: 92%

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CCDC15 localizes to the centriole inner scaffold and regulates centriole integrity and ciliogenesis

Arslanhan

Steib

Hamel

et al. 2023

Preprint

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Centrioles are evolutionarily conserved microtubule-based organelles critical to form centrosomes and cilia, which act as microtubule-organizing, signaling and motility centers. Biogenesis and maintenance of centrioles with proper number, size and architecture are crucial for their functions during development and physiology. Consequently, their deregulation causes developmental disorders and cancer. Although centriole number control has been extensively studied, less is known about how centrioles are maintained as stable structures with conserved size and architecture over successive cell divisions and upon ciliary and flagellar motility. Here, we addressed this question by identifying and characterizing new components of the centriole inner scaffold, a recently discovered centriolar sub-compartment critical for centriole size control and integrity. To this end, we generated proximity interactomes of Centrin-2 and POC5 and used them to define CCDC15 as a new centriolar protein that co-localizes and interacts with known inner scaffold proteins. Ultrastructure expansion microscopy analysis of CCDC15-depleted cells revealed its functions in centriole length control and integrity, resulting in defective ciliogenesis and Hedgehog signaling. Loss-of-function experiments also defined CCDC15 as a dual regulator for the recruitment of the inner scaffold protein POC1B and the distal SFI1/Centrin complex to the centrioles. Together, our findings uncovered new players and mechanisms of centriole architectural integrity and thereby, provide insights into diseases linked to centriolar defects.

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Section: Discussionsupporting

confidence: 85%

Section: Resultsmentioning

confidence: 92%

CCDC15 localizes to the centriole inner scaffold and regulates centriole integrity and ciliogenesis

Arslanhan

Steib

Hamel

et al. 2023

Preprint

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“…This may reflect a dynamic molecular and structural remodeling of the inner scaffold to improve force resistance, akin to force-responsive maturation and remodeling of focal adhesions (Grandy et al, 2023; Legerstee and Houtsmuller, 2021). Precedence for such remodeling is evident with Poc5, a proposed inner scaffold protein in humans, but which is only present in immature BBs in Tetrahymena (Heydeck et al, 2020). Further experimentation is needed to understand these putative remodeling events.…”

Section: Discussionmentioning

confidence: 99%

Poc1 is a basal body inner junction protein that promotes triplet microtubule integrity and interconnections

Ruehle,

Li,

Agard

et al. 2023

Preprint

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Basal bodies (BBs) are conserved eukaryotic structures that organize motile and primary cilia. The BB is comprised of nine, cylindrically arranged, triplet microtubules (TMTs) that are connected to each other by inter-TMT linkages which maintain BB structure. During ciliary beating, forces transmitted to the BB must be resisted to prevent BB disassembly. Poc1 is a conserved BB protein important for BBs to resist ciliary forces. To understand how Poc1 confers BB stability, we identified the precise position of Poc1 binding in theTetrahymenaBB and the effect of Poc1 loss on BB structure. Poc1 binds at the TMT inner junctions, stabilizing TMTs directly. From this location, Poc1 also stabilizes inter-TMT linkages throughout the BB, including the cartwheel pinhead and the inner scaffold. Moreover, we identify a molecular response to ciliary forces via a molecular remodeling of the inner scaffold, as determined by differences in Fam161A localization. Thus, while not essential for BB assembly, Poc1 promotes BB interconnections that establish an architecture competent to resist ciliary forces.

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“…Defective TZ formation has been observed in Tetrahymena after co-depletion of POC5 and the POC5-like Sfr1 protein ( Heydeck et al, 2020 ) despite what appears to be correctly anchored BBs. In these co-depleted cells, cilia formation is impaired, suggesting that there is a requirement for Poc5 in building the distal end of BBs.…”

Section: Introductionmentioning

confidence: 99%

“…In these co-depleted cells, cilia formation is impaired, suggesting that there is a requirement for Poc5 in building the distal end of BBs. In addition to this defective TZ phenotype, depletion of POC5, Sfr1 or their co-depletion leads to too many rows of BBs ( Heydeck et al, 2020 ). How POC5 may affect these two processes is not yet clear and further studies are required to shed light on those phenotypes.…”

Section: Introductionmentioning

confidence: 99%

Paramecium, a Model to Study Ciliary Beating and Ciliogenesis: Insights From Cutting-Edge Approaches

Bouhouche

Valentine

Borgne

et al. 2022

Front. Cell Dev. Biol.

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Cilia are ubiquitous and highly conserved extensions that endow the cell with motility and sensory functions. They were present in the first eukaryotes and conserved throughout evolution (Carvalho-Santos et al., 2011). Paramecium has around 4,000 motile cilia on its surface arranged in longitudinal rows, beating in waves to ensure movement and feeding. As with cilia in other model organisms, direction and speed of Paramecium ciliary beating is under bioelectric control of ciliary ion channels. In multiciliated cells of metazoans as well as paramecia, the cilia become physically entrained to beat in metachronal waves. This ciliated organism, Paramecium, is an attractive model for multidisciplinary approaches to dissect the location, structure and function of ciliary ion channels and other proteins involved in ciliary beating. Swimming behavior also can be a read-out of the role of cilia in sensory signal transduction. A cilium emanates from a BB, structurally equivalent to the centriole anchored at the cell surface, and elongates an axoneme composed of microtubule doublets enclosed in a ciliary membrane contiguous with the plasma membrane. The connection between the BB and the axoneme constitutes the transition zone, which serves as a diffusion barrier between the intracellular space and the cilium, defining the ciliary compartment. Human pathologies affecting cilia structure or function, are called ciliopathies, which are caused by gene mutations. For that reason, the molecular mechanisms and structural aspects of cilia assembly and function are actively studied using a variety of model systems, ranging from unicellular organisms to metazoa. In this review, we will highlight the use of Paramecium as a model to decipher ciliary beating mechanisms as well as high resolution insights into BB structure and anchoring. We will show that study of cilia in Paramecium promotes our understanding of cilia formation and function. In addition, we demonstrate that Paramecium could be a useful tool to validate candidate genes for ciliopathies.

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Tetrahymena Poc5 is a transient basal body component that is important for basal body maturation

Cited by 9 publications

References 102 publications

CCDC15 localizes to the centriole inner scaffold and regulates centriole integrity and ciliogenesis

CCDC15 localizes to the centriole inner scaffold and regulates centriole integrity and ciliogenesis

Poc1 is a basal body inner junction protein that promotes triplet microtubule integrity and interconnections

Paramecium, a Model to Study Ciliary Beating and Ciliogenesis: Insights From Cutting-Edge Approaches

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