Abstract
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
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism
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Embryonic Development*
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Gene Expression Regulation, Developmental
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Humans
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Molecular Sequence Data
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Neurogenesis / genetics
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Phylogeny
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Prosencephalon / embryology
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Prosencephalon / metabolism*
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Sequence Alignment
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Ubiquitin-Protein Ligases / chemistry
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Ubiquitin-Protein Ligases / genetics*
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Ubiquitin-Protein Ligases / metabolism*
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Xenopus laevis
Substances
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Carrier Proteins
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RMND5A protein, human
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Ubiquitin-Protein Ligases
Grants and funding
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.