Item Type: | Article |
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Title: | The AP-1 clathrin adaptor facilitates cilium formation and functions with RAB-8 in C. elegans ciliary membrane transport |
Creators Name: | Kaplan, O.I., Molla-Herman, A., Cevik, S., Ghossoub, R., Kida, K., Kimura, Y., Jenkins, P., Martens, J.R., Setou, M., Benmerah, A. and Blacque, O.E. |
Abstract: | Clathrin 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. |
Keywords: | C. elegans, RAB-8, Cilia, Clathrin Adaptor 1, Membrane Transport, Animals |
Source: | Journal of Cell Science |
ISSN: | 0021-9533 |
Publisher: | Company of Biologists |
Volume: | 123 |
Number: | Pt 22 |
Page Range: | 3966-3977 |
Date: | 15 November 2010 |
Official Publication: | https://doi.org/10.1242/jcs.073908 |
PubMed: | View item in PubMed |
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