title: Caenorhabditis elegans paraoxonase-like proteins control the functional expression of DEG/ENaC mechanosensory proteins.
abstract: Caenorhabditis eleganssenses gentle touch via a mechanotransduction channel formed from the DEG/ENaC proteins MEC-4 and MEC-10. An additional protein, the paraoxonase-like protein MEC-6, is essential for transduction, and previous work suggested that MEC-6 was part of the transduction complex. We found that MEC-6 and a similar protein, POML-1, reside primarily in the endoplasmic reticulum and do not colocalize with MEC-4 on the plasma membrane in vivo. As with MEC-6, POML-1 is needed for touch sensitivity, the neurodegeneration caused by themec-4(d)mutation, and the expression and distribution of MEC-4 in vivo. Both proteins are likely needed for the proper folding or assembly of MEC-4 channels in vivo as measured by FRET. MEC-6 detectably increases the rate of MEC-4 accumulation on theXenopusoocyte plasma membrane. These results suggest that MEC-6 and POML-1 interact with MEC-4 to facilitate expression and localization of MEC-4 on the cell surface. Thus MEC-6 and POML-1 act more like chaperones for MEC-4 than channel components.
authors.affiliation: Department of Biological Sciences, Columbia University, New York, NY 10027.
authors.forename: Yushu
authors.initials: Y
authors.lastname: Chen
authors.affiliation: Department of Molecular and Cell Biology and Helen Wills Neuroscience Institute, University of California, Berkeley, Berkeley, CA 94720.
authors.forename: Shashank
authors.initials: S
authors.lastname: Bharill
authors.affiliation: Department of Neuroscience and Psychiatry, Albert Einstein College of Medicine, Bronx, NY 10461.
authors.forename: Zeynep
authors.initials: Z
authors.lastname: Altun
authors.affiliation: Department of Genetics, Rutgers, The State University of New Jersey, Piscataway, NJ 08854.
authors.forename: Robert
authors.initials: R
authors.lastname: O'Hagan
authors.affiliation: Department of Biological Sciences, Columbia University, New York, NY 10027.
authors.forename: Brian
authors.initials: B
authors.lastname: Coblitz
authors.affiliation: Department of Molecular and Cell Biology and Helen Wills Neuroscience Institute, University of California, Berkeley, Berkeley, CA 94720.
authors.forename: Ehud Y
authors.initials: EY
authors.lastname: Isacoff
authors.affiliation: Department of Biological Sciences, Columbia University, New York, NY 10027 mc21@columbia.edu.
authors.forename: Martin
authors.initials: M
authors.lastname: Chalfie
mesh_terms: D000818:Animals; D030801:Animals, Genetically Modified; D043303:Aryldialkylphosphatase / Q000235:genetics / Q000378:metabolism*; D017173:Caenorhabditis elegans / Q000235:genetics / Q000378:metabolism; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005260:Female; D031541:Fluorescence Resonance Energy Transfer; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D009474:Neurons / Q000378:metabolism / Q000473:pathology; D009865:Oocytes / Q000378:metabolism; D014982:Xenopus laevis
chemical_list: D029742:Caenorhabditis elegans Proteins; C115871:Mec-4 protein, C elegans; D008565:Membrane Proteins; C470181:MEC-6 protein, C elegans; D043303:Aryldialkylphosphatase; C000613450:POML-1 protein, C elegans