Piecing together a ciliome

Inglis, Peter N.; Boroevich, Keith A.; Leroux, Michel R.

doi:10.1016/j.tig.2006.07.006

Cited by 190 publications

(195 citation statements)

References 69 publications

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“…At first, ubiquitinated proteins have been reported to be present in cilia and flagella 52 , and the K63-specific E2 ubiquitinconjugating enzyme Ubc13 is present in the ciliome of various species [52][53][54][55] . Next, protein ubiquitination was involved in flagellar disassembly 52 .…”

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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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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“…Many eukaryotic cells have cilia, which play diverse roles in many physiological processes, such as cell and fluid movement, sensory perception and development (Inglis et al 2006;Marshall & Nonaka 2006). Recently, aberrant cilia functions have been revealed to underlie the large number of human disorders (Pazour & Rosenbaum 2002;Ibanez-Tallon et al 2003;Afzelius 2004;Beales 2005;Pan et al 2005).…”

Section: Introductionmentioning

confidence: 99%

“…The IFT machinery conveys cargo, such as receptors and channels, to the ciliary tip by kinesin-II motors and recycles components to the basal body by a dynein motor (Rosenbaum & Witman 2002;Cole 2003;Scholey 2003;Inglis et al 2006). The motors cooperate with a multiprotein complex, IFT particle, which consists of two subcomplexes, A and B (Piperno & Mead 1997;Cole et al 1998).…”

Section: Introductionmentioning

confidence: 99%

IFT‐81 and IFT‐74 are required for intraflagellar transport in C. elegans

Kobayashi¹,

Gengyo-Ando²,

Ishihara³

et al. 2007

Genes to Cells

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“…In addition to sensory and motile functions, the primary cilium plays a central role in the signal transduction of the Hh, PDGF, Wnt, Hippo, and calcium signaling pathways (2)(3)(4). Recent genomic and proteomic approaches have identified a ciliome consisting of hundreds of proteins (5,6). However, the molecular functions of most of these proteins remain elusive.…”

mentioning

confidence: 99%

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.

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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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Piecing together a ciliome

Cited by 190 publications

References 69 publications

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

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

IFT‐81 and IFT‐74 are required for intraflagellar transport in C. elegans

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

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