RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development

PLoS One. 2015 Mar 20;10(3):e0120342. doi: 10.1371/journal.pone.0120342. eCollection 2015.


In Saccharomyces cerevisiae the Gid-complex functions as an ubiquitin-ligase complex that regulates the metabolic switch between glycolysis and gluconeogenesis. In higher organisms six conserved Gid proteins form the CTLH protein-complex with unknown function. Here we show that Rmnd5, the Gid2 orthologue from Xenopus laevis, is an ubiquitin-ligase embedded in a high molecular weight complex. Expression of rmnd5 is strongest in neuronal ectoderm, prospective brain, eyes and ciliated cells of the skin and its suppression results in malformations of the fore- and midbrain. We therefore suggest that Xenopus laevis Rmnd5, as a subunit of the CTLH complex, is a ubiquitin-ligase targeting an unknown factor for polyubiquitination and subsequent proteasomal degradation for proper fore- and midbrain development.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Embryonic Development*
  • Gene Expression Regulation, Developmental
  • Humans
  • Molecular Sequence Data
  • Neurogenesis / genetics
  • Phylogeny
  • Prosencephalon / embryology
  • Prosencephalon / metabolism*
  • Sequence Alignment
  • Ubiquitin-Protein Ligases / chemistry
  • Ubiquitin-Protein Ligases / genetics*
  • Ubiquitin-Protein Ligases / metabolism*
  • Xenopus laevis


  • Carrier Proteins
  • RMND5A protein, human
  • Ubiquitin-Protein Ligases

Grant support

The project was supported by funding from the Fonds der Chemischen Industrie, Frankfurt and the Wilhelm Roux program (FKZ 26/22), Halle (Saale). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.