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Resources » Paper

Nasrin Babadi et al. (2007) International Worm Meeting "Controlling axon branching: A new physiological role for peptide N-glycanase, png-1."

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  • Comments on Nasrin Babadi et al. (2007) International Worm Meeting "Controlling axon branching: A new physiological role for peptide N-glycanase, png-1." (0)

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    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00030137

    Nasrin Babadi, Anna Su, & Antonio Colavita (2007). Controlling axon branching: A new physiological role for peptide N-glycanase, png-1 presented in International Worm Meeting. Unpublished information; cite only with author permission.

    The development of a complex neuronal ciruitry in the nervous system is dependant on neuronal axons migrating and branching at their targets. The VC and HSN neurons are among few neurons that branch at the vulva to regulate egg laying in C.elegans. Visualized by the cat-1::gfp reporter, the VC4 and VC5 display the most branching morphology of all the VCs. We isolated peptide N-glycanase, (png-1) in a genetic screen for mutants with excessive axon branching defects at the vulva. png-1 encodes a protein that consists of three domains, an N-terminal thioredoxin domain, a central conserved PNGase domain, and a conserved C-terminal domain. Cell rescue studies suggest that png-1 acts cell non-autonomously in vulval cells to regulate axon branching, while png-1 transcriptional reporter show wide expression in the hypodermis, other neurons, and cell types. In addition to the VC4 and VC5, png-1 also displays branching defects in the AVL and DVB motor neurons near the vulva region. Functional analysis of each of PNG-1 domains show that the thioredoxin and PNGase domains are necessary to rescue axon branching defects in png-1 mutants. Cytoplasmic PNGases are highly conserved proteins and they are involved in the processing of misfolded glycoproteins in yeast and mammalian cells through their activity in ER associated degradation (ERAD). Thioredoxin also belongs to a family of highly conserved proteins with various enzymatic activities. We have identified the first worm homologue of PNGase, with a novel role in controlling axon branching. Currently we are working to identify the mechanism through which png-1 controls axon branching at the vuvla, and the role of thioredoxin and PNGase domains in this process. Also, we are using a candidate gene approach and biochemical studies to investigate png-1 interaction with other genes and their effect on axon branching.


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