BAIT

NRX-1

CELE_C29A12.4
Protein NRX-1
GO Process (0)
GO Function (0)
GO Component (1)

Gene Ontology Cellular Component

Caenorhabditis elegans
PREY

PNG-1

CELE_F56G4.5, bam-1, F56G4.5
png-1 encodes a peptide-N[4]-(N-acetyl-beta-D-glucosaminyl) asparagine amidase (i.e., peptide:N-glycanase or PNGase) orthologous to budding yeast PNG1 and human NGLY1; PNG-1 is atypically organized, with an N-terminal thioredoxin-like domain, a central transglutaminase domain, and a C-terminal DUF750 domain, while lacking the PUB domain found in mammalian or insect PNGases; both in vitro and in vivo, PNG-1 shows both protein disulfide reductase and PNGase activities, which require its N-terminal and central domains respectively; PNG-1 has PNGase activity on denatured but not natively folded RNAse B, and releases both high mannose- and sialo-complex-type N-glycans from glycopeptides and denatured glycoproteins; in vivo, the png-1(cy8) mutation C251Y (predicted to destroy the PNGase active site) abolishes PNGase activity while leaving PNG-1's reductase activity intact; conversely, PNG-1's reductase activity is abolished by the dual missense mutation C34S/C37S, which alters its predicted N-terminal active site; by orthology, PNG-1 is expected to aid proteasomal degradation of misfolded proteins; PNG-1 activity is inhibited by Zn(2+) and the caspase inhibitor z-VAD-fmk, but not by EDTA; PNG-1 is expressed in renal gland cells and intestine; although W04G5.5 and Y50D4B.7 have some similarity to the transglutaminase domain of PNG-1, they lack a predicted catalytic triad active site.
Caenorhabditis elegans

Proximity Label-MS

An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

Publication

Characterization of the intracellular neurexin interactome by in vivo proximity ligation suggests its involvement in presynaptic actin assembly.

Schaan Profes M, Tiroumalechetty A, Patel N, Lauar SS, Sidoli S, Kurshan PT

Neurexins are highly spliced transmembrane cell adhesion molecules that bind an array of partners via their extracellular domains. However, much less is known about the signaling pathways downstream of neurexin's largely invariant intracellular domain (ICD). Caenorhabditis elegans contains a single neurexin gene that we have previously shown is required for presynaptic assembly and stabilization. To gain insight into the signaling ... [more]

PLoS Biol Jan. 01, 2024; 22(1);e3002466 [Pubmed: 38252619]

Throughput

  • High Throughput

Additional Notes

  • BioID
  • High confidence hits were identified relative to the specific endogenous control strain (neurexin-deltaPBM-TurboID) which differs only in its subcellular neurexin localization pattern (loss of synaptic enrichment).
  • TurboID proximity labeling method to identify protein interactors of neurexin's (NRX-1) intracellular domain.

Curated By

  • BioGRID