@article{IgualGilJariusvonKriesetal.2017,
  author    = {Igual Gil, Carla and Jarius, Mirko and von Kries, Jens P. and Rohlfing, Anne-Kartin},
  title     = {Neuronal Chemosensation and Osmotic Stress Response Converge in the Regulation of aqp-8 in C. elegans},
  series = {Frontiers in physiology},
  volume    = {8},
  journal   = {Frontiers in physiology},
  publisher = {Frontiers Research Foundation},
  address   = {Lausanne},
  issn      = {1664-042X},
  doi       = {10.3389/fphys.2017.00380},
  pages     = {12},
  year      = {2017},
  abstract  = {Aquaporins occupy an essential role in sustaining the salt/water balance in various cells types and tissues. Here, we present new insights into aqp-8 expression and regulation in Caenorhabditis elegans. We show, that upon exposure to osmotic stress, aqp-8 exhibits a distinct expression pattern within the excretory cell compared to other C. elegans aquaporins expressed. This expression is correlated to the osmolarity of the surrounding medium and can be activated physiologically by osmotic stress or genetically in mutants with constitutively active osmotic stress response. In addition, we found aqp-8 expression to be constitutively active in the TRPV channel mutant osm-9(ok1677). In a genome-wide RNAi screen we identified additional regulators of aqp-8. Many of these regulators are connected to chemosensation by the amphid neurons, e.g., odr-10 and gpa-6, and act as suppressors of aqp-8 expression. We postulate from our results, that aqp-8 plays an important role in sustaining the salt/water balance during a secondary response to hyper-osmotic stress. Upon its activation aqp-8 promotes vesicle docking to the lumen of the excretory cell and thereby enhances the ability to secrete water and transport osmotic active substances or waste products caused by protein damage. In summary, aqp-8 expression and function is tightly regulated by a network consisting of the osmotic stress response, neuronal chemosensation as well as the response to protein damage. These new insights in maintaining the salt/water balance in C. elegans will help to reveal the complex homeostasis network preserved throughout species.},
  language  = {en}
}
@article{JedrusikBodeStudenckaSmolkaetal.2013,
  author    = {Jedrusik-Bode, Monika and Studencka, Maja and Smolka, Christian and Baumann, Tobias and Schmidt, Henning and Kampf, Jan and Paap, Franziska and Martin, Sophie and Tazi, Jamal and M{\"u}ller, Kristian M. and Kr{\"u}ger, Marcus and Braun, Thomas and Bober, Eva},
  title     = {The sirtuin SIRT6 regulates stress granule formation in C. elegans and mammals},
  series = {Journal of cell science},
  volume    = {126},
  journal   = {Journal of cell science},
  number    = {22},
  publisher = {Company of Biologists Limited},
  address   = {Cambridge},
  issn      = {0021-9533},
  doi       = {10.1242/jcs.130708},
  pages     = {5166 -- +},
  year      = {2013},
  abstract  = {SIRT6 is a NAD(+)-dependent deacetylase that modulates chromatin structure and safeguards genomic stability. Until now, SIRT6 has been assigned to the nucleus and only nuclear targets of SIRT6 are known. Here, we demonstrate that in response to stress, C. elegans SIR-2.4 and its mammalian orthologue SIRT6 localize to cytoplasmic stress granules, interact with various stress granule components and induce their assembly. Loss of SIRT6 or inhibition of its catalytic activity in mouse embryonic fibroblasts impairs stress granule formation and delays disassembly during recovery, whereas deficiency of SIR-2.4 diminishes maintenance of P granules and decreases survival of C. elegans under stress conditions. Our findings uncover a novel, evolutionary conserved function of SIRT6 in the maintenance of stress granules in response to stress.},
  language  = {en}
}