title: Some, but not all, retromer components promote morphogenesis of C. elegans sensory compartments.
abstract: The endings of sensory receptor cells often lie within specialized compartments formed by glial cells. The main sensory organ of Caenorhabditis elegans, the amphid, provides a powerful setting for studying glial compartment morphogenesis. Our previous studies showed that amphid compartment size is controlled by opposing activities of the Nemo-like kinase LIT-1, which promotes compartment expansion, and the Patched-related protein DAF-6, which restricts compartment growth. From a genetic screen for mutations able to suppress the bloated sensory compartments of daf-6 mutants, we identified an allele of the sorting nexin gene snx-1. SNX-1 protein is a component of the retromer, a protein complex that facilitates recycling of transmembrane proteins from the endosome to the Golgi network. We find that snx-1 functions cell autonomously within glia to promote sensory compartment growth, and that SNX-1 protein is enriched near the surface of the sensory compartment. snx-1 interacts genetically with lit-1 and another regulator of compartment size, the Dispatched-related gene che-14. Mutations in snx-3 and vps-29, also retromer genes, can suppress daf-6 defects. Surprisingly, however, remaining retromer components seem not to be involved. Our results suggest that a novel assembly of retromer components is important for determining sensory compartment dimensions.
authors.affiliation: Laboratory of Developmental Genetics, The Rockefeller University, New York, NY 10065, USA.
authors.forename: Grigorios
authors.initials: G
authors.lastname: Oikonomou
authors.forename: Elliot A
authors.initials: EA
authors.lastname: Perens
authors.forename: Yun
authors.initials: Y
authors.lastname: Lu
authors.forename: Shai
authors.initials: S
authors.lastname: Shaham
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000196:embryology*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D046529:Microscopy, Electron, Transmission; D008856:Microscopy, Fluorescence; D009024:Morphogenesis / Q000502:physiology*; D046912:Multiprotein Complexes / Q000235:genetics* / Q000502:physiology; D009154:Mutation / Q000235:genetics; D009457:Neuroglia / Q000502:physiology*; D010957:Plasmids / Q000235:genetics; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011984:Sensory Receptor Cells / Q000502:physiology*; D058305:Sorting Nexins / Q000235:genetics* / Q000378:metabolism / Q000502:physiology
chemical_list: D029742:Caenorhabditis elegans Proteins; C502788:DAF-6 protein, C elegans; D008565:Membrane Proteins; D046912:Multiprotein Complexes; C545103:SNX-1 protein, C elegans; D058305:Sorting Nexins; D017346:Protein Serine-Threonine Kinases; C120085:lit-1 protein, C elegans