Cep164 mediates vesicular docking to the mother centriole during early steps of ciliogenesis

Schmidt, Kerstin; Kuhns, Stefanie; Neuner, Annett; Hub, Birgit; Zentgraf, Hanswalter; Pereira, Gislene

doi:10.1083/jcb.201202126

Cited by 262 publications

(427 citation statements)

References 68 publications

(135 reference statements)

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“…Docking of Golgi-derived ciliary vesicles to the mother centriole is a critical step in cilium biogenesis (8). Recent studies have suggested that centriolar distal appendages are required for docking ciliary vesicles (9,12,13). The distal appendage assembly defects in C2cd3 GT mutant cells prompted us to examine whether ciliary vesicle docking to the mother centriole was affected.…”

Section: Resultsmentioning

confidence: 99%

“…jax.org/marker/MGI:2141942), an inhibitor of ciliogenesis, from the distal end of the mother centriole (10). Recent studies have also suggested that components of the distal appendages are essential for docking ciliary vesicles to the mother centriole (9,(11)(12)(13)(14).…”

mentioning

confidence: 99%

“…Mutations disrupting the functions of the IFT motors (kinesin II and cytoplasmic dynein) or the IFT cargo adaptor complexes (IFT-A and IFT-B) lead to defects in cilia biogenesis. Recent studies have revealed an essential role for distal appendage proteins in recruiting IFT proteins to the mother centriole, suggesting another mechanism by which centriolar distal appendages promote ciliogenesis (9,12,13).…”

mentioning

confidence: 99%

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C2cd3 is critical for centriolar distal appendage assembly and ciliary vesicle docking in mammals

Zeng

Ning

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

133

158

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The primary cilium plays critical roles in vertebrate development and physiology, but the mechanisms underlying its biogenesis remain poorly understood. We investigated the molecular function of C2 calcium-dependent domain containing 3 (C2cd3), an essential regulator of primary cilium biogenesis. We show that C2cd3 is localized to the centriolar satellites in a microtubule-and Pcm1-dependent manner; however, C2cd3 is dispensable for centriolar satellite integrity. C2cd3 is also localized to the distal ends of both mother and daughter centrioles and is required for the recruitment of five centriolar distal appendage proteins: Sclt1, Ccdc41, Cep89, Fbf1, and Cep164. Furthermore, loss of C2cd3 results in failure in the recruitment of Ttbk2 to the ciliary basal body as well as the removal of Cp110 from the ciliary basal body, two critical steps in initiating ciliogenesis. C2cd3 is also required for recruiting the intraflagellar transport proteins Ift88 and Ift52 to the mother centriole. Consistent with a role in distal appendage assembly, C2cd3 is essential for ciliary vesicle docking to the mother centriole. Our results suggest that C2cd3 regulates cilium biogenesis by promoting the assembly of centriolar distal appendages critical for docking ciliary vesicles and recruiting other essential ciliogenic proteins.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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C2cd3 is critical for centriolar distal appendage assembly and ciliary vesicle docking in mammals

Zeng

Ning

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

133

158

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“…However, we cannot rule out that ubiquitination/deubiquitination processes might affect centriole appendages and centriolar satellite functions 59,60 .…”

Section: Discussionmentioning

confidence: 99%

The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells

et al. 2014

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CYLD is a tumour suppressor gene mutated in familial cylindromatosis, a genetic disorder leading to the development of skin appendage tumours. It encodes a deubiquitinating enzyme that removes Lys63-or linear-linked ubiquitin chains. CYLD was shown to regulate cell proliferation, cell survival and inflammatory responses, through various signalling pathways. Here we show that CYLD localizes at centrosomes and basal bodies via interaction with the centrosomal protein CAP350 and demonstrate that CYLD must be both at the centrosome and catalytically active to promote ciliogenesis independently of NF-kB. In transgenic mice engineered to mimic the smallest truncation found in cylindromatosis patients, CYLD interaction with CAP350 is lost disrupting CYLD centrosome localization, which results in cilia formation defects due to impairment of basal body migration and docking. These results point to an undiscovered regulation of ciliogenesis by Lys63 ubiquitination and provide new perspectives regarding CYLD function that should be considered in the context of cylindromatosis.

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“…Sa localisation proche du centrosome au cours des étapes très précoces de la ciliogenèse indique sa présence sur la vésicule ciliaire. Son recrutement et son activation seraient sous le contrôle de CEP164 via son interaction avec Rabin8 [21], un facteur d'échange de Rab8 qui est associé à des vésicules contenant Rab11 (endosomes de recyclage), elle-même requise pour la ciliogenèse [22]. Rab11 et CEP164 participeraient ainsi à l'activation coordonnée de Rabin8 qui, à son tour, activerait Rab8 à la membrane de la vésicule ciliaire au contact des appendices distaux.…”

Section: Les Appendices Distauxunclassified

La poche ciliaire : fruit des liaisons du centrosome avec le trafic vésiculaire

Benmerah¹

2014

Med Sci (Paris)

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Cep164 mediates vesicular docking to the mother centriole during early steps of ciliogenesis

Abstract: Cep164 provides a molecular link between the mother centriole and the ciliary membrane biogenesis machinery by interacting with the GEF Rabin8 and the GTPase Rab8.

Cited by 262 publications

References 68 publications

C2cd3 is critical for centriolar distal appendage assembly and ciliary vesicle docking in mammals

C2cd3 is critical for centriolar distal appendage assembly and ciliary vesicle docking in mammals

The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells

La poche ciliaire : fruit des liaisons du centrosome avec le trafic vésiculaire

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