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

Thorsten Pfirrmann; Pablo Villavicencio-Lorini; Abinash K Subudhi; Ruth Menssen; Dieter H Wolf; Thomas Hollemann

doi:10.1371/journal.pone.0120342

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.

Authors

Thorsten Pfirrmann¹, Pablo Villavicencio-Lorini², Abinash K Subudhi¹, Ruth Menssen³, Dieter H Wolf³, Thomas Hollemann¹

Affiliations

¹ Martin-Luther University Halle-Wittenberg, Institute of Physiological Chemistry, Halle, Germany.
² Martin Luther University Halle-Wittenberg, Institute of Human Genetics, Halle, Germany.
³ University of Stuttgart, Institute of Biochemistry, Pfaffenwaldring 55, 70569 Stuttgart, Germany.

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

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

Substances

Carrier Proteins
RMND5A protein, human
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.