RT Journal Article SR Electronic T1 C. elegans paraoxonase-like proteins control the functional expression of DEG/ENaC mechanosensory proteins JF bioRxiv FD Cold Spring Harbor Laboratory SP 040337 DO 10.1101/040337 A1 Yushu Chen A1 Shashank Bharill A1 Zeynep Altun A1 Robert O’Hagan A1 Brian Coblitz A1 Ehud Y. Isacoff A1 Martin Chalfie YR 2016 UL http://biorxiv.org/content/early/2016/02/19/040337.abstract AB Caenorhabditis elegans senses 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, for the neurodegeneration caused by the mec-4(d) mutation, and for 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 the Xenopus oocyte 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.Abbreviations usedTRNstouch receptor neuronsPONsparaoxonasesPOML-1paraoxonaseMEC-6-likegene 1ERendoplasmic reticulum