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Resources » Paper

Rademakers, Suzanne et al. (2021) International Worm Meeting "Identifying novel interactors of the guanylate cyclase GCY-22 involved in NaCl chemotaxis"

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  • Comments on Rademakers, Suzanne et al. (2021) International Worm Meeting "Identifying novel interactors of the guanylate cyclase GCY-22 involved in NaCl chemotaxis" (0)

  • Overview

    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00063167

    Rademakers, Suzanne, & Jansen, Gert (2021). Identifying novel interactors of the guanylate cyclase GCY-22 involved in NaCl chemotaxis presented in International Worm Meeting. Unpublished information; cite only with author permission.

    C. elegans senses salts in their environment using the ASE neurons. Detection of salts occurs in sensory organelles, called primary cilia. cGMP signalling plays an important role in salt detection. The receptor-type guanylate cyclase (rGC) GCY-22 is involved in the response to NaCl in the environment. We generated a full-length GFP knock-in the gcy-22 gene. GCY-22::GFP shows unique localization to the ciliary tip and periciliary membrane compartment (PCMC) of one ciliated neuron, ASER. Our goal is to understand the molecular mechanisms that regulate its trafficking and unique localization. To identify proteins that physically interact with GCY-22, we performed mass spectrometry after immunoprecipitation to identify proteins bound to GFP-tagged GCY-22. Next, we study where the identified candidate interacting proteins are expressed and localized. Mutants are used to investigate their role in salt detection, GCY-22::GFP trafficking towards the cilium and localization to the ciliary tip. The most prominent candidate interacting protein is GCY-19. GCY-19::GFP is expressed in ASER and colocalized with GCY-22. Loss-of-function of gcy-19 resulted in lower levels of GCY-22::GFP at the ciliary tip. Similarly, gcy-22 loss-of-function animals showed lower levels of GCY-19::GFP at the tip of the ASER cilium . We also found GCY-4 and GCY-5 as possible interactors of GCY-22. As rGCs are thought to act as dimers, these findings suggests that GCY-22 might be a common subunit for heterodimeric complexes possibly to achieve ion-selectivity. In addition, we identified DAF-25 in our GCY-22::GFP IP-MS experiments. DAF-25 is the ortholog of the mammalian ankyrin repeat and Mynd domain containing protein Ankmy2. DAF-25 has been reported previously to be important for rGC transport. Mutants lacking DAF-25 show no ciliary tip localization of GCY-22::GFP and do not respond to NaCl. Other candidate genes are currently being investigated. This work will allow us to gain insight in the molecular mechanisms that regulate ciliary tip localization of GCY-22.

    Affiliation:
    - Erasmus MC, Rotterdam, The Netherlands


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