The ciliary pocket: an endocytic membrane domain at the base of primary and motile cilia

Mollà-Herman, Anahi; Ghossoub, Rania; Blisnick, Thierry; Meunier, Anne; Serres, Catherine; Silbermann, Flora; Emmerson, Chris; Romeo, Kelly; Bourdoncle, Pierre; Schmitt, Alain; Saunier, Sophie; Spassky, Nathalie; Bastin, Philippe; Benmerah, Alexandre

doi:10.1242/jcs.059519

Cited by 254 publications

(331 citation statements)

References 49 publications

(58 reference statements)

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“…Both TTBK2 recruitment and CP110 removal appeared normal in CEP290 null cells (Supplemental Figure 5). Attachment of ciliary vesicles to the distal appendages of the nascent basal body precedes axoneme assembly in RPE1 cells (12,18). We observed an increase in the number of cells exhibiting either a Smo-EGFP + ciliary vesicle attached to the basal body or pericentriolar Smo-EGFP + vesicles in a CEP290 null background (Supplemental Figure 6, A and B).…”

Section: Resultsmentioning

confidence: 71%

Eupatilin rescues ciliary transition zone defects to ameliorate ciliopathy-related phenotypes

Kim¹,

Kim²,

Jung³

et al. 2018

Journal of Clinical Investigation

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Section: Resultsmentioning

confidence: 71%

Eupatilin rescues ciliary transition zone defects to ameliorate ciliopathy-related phenotypes

Kim¹,

Kim²,

Jung³

et al. 2018

Journal of Clinical Investigation

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“…3A), defects in cilium positioning and orientation were observed. In basic cell culture conditions, RPE1 cilia grew parallel to adherent surfaces, with a confined Z-axis distribution, resulting in cilia appearing within the same focal plane (Molla-Herman et al, 2010). However, in AP-1-depleted cells, cilia were observed over three to four focal planes, indicating a more random distribution.…”

Section: Ap-1-rab-8 and Cilia Membrane Transportmentioning

confidence: 99%

The AP-1 clathrin adaptor facilitates cilium formation and functions with RAB-8 in C. elegans ciliary membrane transport

Kaplan

Mollà-Herman

Cevik

et al. 2010

Journal of Cell Science

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SummaryClathrin adaptor (AP) complexes facilitate membrane trafficking between subcellular compartments. One such compartment is the cilium, whose dysfunction underlies disorders classified as ciliopathies. Although AP-1mu subunit (UNC-101) is linked to cilium formation and targeting of transmembrane proteins (ODR-10) to nematode sensory cilia at distal dendrite tips, these functions remain poorly understood. Here, using Caenorhabditis elegans sensory neurons and mammalian cell culture models, we find conservation of AP-1 function in facilitating cilium morphology, positioning and orientation, and microtubule stability and acetylation. These defects appear to be independent of IFT, because AP-1-depleted cells possess normal IFT protein localisation and motility. By contrast, disruption of chc-1 (clathrin) or rab-8 phenocopies unc-101 worms, preventing ODR-10 vesicle formation and causing misrouting of ODR-10 to all plasma membrane destinations. Finally, ODR-10 colocalises with RAB-8 in cell soma and they cotranslocate along dendrites, whereas ODR-10 and UNC-101 signals do not overlap. Together, these data implicate conserved roles for metazoan AP-1 in facilitating cilium structure and function, and suggest cooperation with RAB-8 to coordinate distinct early steps in neuronal ciliary membrane sorting and trafficking.

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“…It is characterized by the presence of clathrin-coated vesicles resulting from the vesicular trafficking that originates and ends in this region. [12][13][14] Although it is not isolated from the cytoplasm, the PC is a highly compartmentalized organelle (Figure 1), surrounded by a specialized region of the plasma membrane that holds a different concentration of channels and receptors. The ciliary axoneme indeed is separated from the rest of the intracellular compartments by the 'ciliary necklace', which is located at the base of the cilium and connects the transition zone fibers of the basal body to the 'ciliary pore complex'.…”

Section: Cilium: Structure and Signalingmentioning

confidence: 99%

Autophagy and regulation of cilia function and assembly

et al. 2014

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Motile and primary cilia (PC) are microtubule-based structures located at the cell surface of many cell types. Cilia govern cellular functions ranging from motility to integration of mechanical and chemical signaling from the environment. Recent studies highlight the interplay between cilia and autophagy, a conserved cellular process responsible for intracellular degradation. Signaling from the PC recruits the autophagic machinery to trigger autophagosome formation. Conversely, autophagy regulates ciliogenesis by controlling the levels of ciliary proteins. The cross talk between autophagy and ciliated structures is a novel aspect of cell biology with major implications in development, physiology and human pathologies related to defects in cilium function. Cell Death and Differentiation (2015) 22, 389-397; doi:10.1038/cdd.2014.171; published online 31 October 2014 FactsAutophagy is a degradative and recycling mechanism that allows cells to adapt to stress situations including nutrient deprivation. Primary cilia (PC) and motile cilia (MC) are sensory structures at the cell surface. PC sense nutrient, growth factor and calcium changes in the extracellular environment and also respond to mechanical stress. MC are beating structures that contribute to innate defense in the lung, for example. The PC is a site for the recruitment of autophagy-related (ATG) proteins that mediate autophagosome formation in response to cilium-dependent signaling. In turn, autophagy regulates the biogenesis of cilia by degrading certain proteins involved in cilia formation. Modulation of autophagy represents a new therapeutic opportunity in diseases related to defective cilia function. Open QuestionsHow are ATG proteins transported to the PC? How do ATG proteins recruited to the PC contribute to the biogenesis of phagophores and autophagosomes? Ciliary proteins are degraded by autophagy. How selective is this degradative pathway? Do some of these proteins contain motifs that result in selective engulfment by autophagosomes?What are the determinants that switch the degradation of ciliary proteins between basal and induced autophagy? Is there any specific function for cilium-dependent autophagy in ciliated cells? Do signals that trigger cilium-dependent autophagy depend on the stimuli (chemical, mechanical) or do all stimuli converge to a single signaling pathway upstream of the autophagy machinery? Can modulation of autophagy contribute to the restoration of cilium functions?Receptors, transporters and specialized plasma membrane structures such as cilia constitute the interfaces between the extracellular and intracellular milieu and allow the cells to trigger specific responses to adapt to changes imposed by the environment. Among these adaptive responses, macroautophagy (hereafter referred to as 'autophagy') is a catabolic process conserved in eukaryotic cells by which the cell recycles its own constituents. 1 Autophagy is involved in the adaptation to starvation, cell differentiation and development, the degradation of aberrant structure...

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The ciliary pocket: an endocytic membrane domain at the base of primary and motile cilia

Cited by 254 publications

References 49 publications

Eupatilin rescues ciliary transition zone defects to ameliorate ciliopathy-related phenotypes

Eupatilin rescues ciliary transition zone defects to ameliorate ciliopathy-related phenotypes

The AP-1 clathrin adaptor facilitates cilium formation and functions with RAB-8 in C. elegans ciliary membrane transport

Autophagy and regulation of cilia function and assembly

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