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Facilitation of Endosomal Recycling by an IRG Protein Homolog Maintains Apical Tubule Structure in Caenorhabditis elegans.

Kelly A GrussendorfChristopher J TrezzaAlexander T SalemHikmat Al-HashimiBrendan C MattinglyDrew E KampmeyerLiakot A KhanDavid H HallVerena GöbelBrian D AckleyMatthew Buechner
Published in: Genetics (2016)
Determination of luminal diameter is critical to the function of small single-celled tubes. A series of EXC proteins, including EXC-1, prevent swelling of the tubular excretory canals in Caenorhabditis elegans In this study, cloning of exc-1 reveals it to encode a homolog of mammalian IRG proteins, which play roles in immune response and autophagy and are associated with Crohn's disease. Mutants in exc-1 accumulate early endosomes, lack recycling endosomes, and exhibit abnormal apical cytoskeletal structure in regions of enlarged tubules. EXC-1 interacts genetically with two other EXC proteins that also affect endosomal trafficking. In yeast two-hybrid assays, wild-type and putative constitutively active EXC-1 binds to the LIM-domain protein EXC-9, whose homolog, cysteine-rich intestinal protein, is enriched in mammalian intestine. These results suggest a model for IRG function in forming and maintaining apical tubule structure via regulation of endosomal recycling.
Keyphrases
  • immune response
  • wild type
  • binding protein
  • protein protein
  • amino acid
  • oxidative stress
  • dendritic cells
  • mass spectrometry
  • high throughput
  • small molecule
  • high resolution
  • optic nerve