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PLoS One 2015 Mar 16;103:e0120342. doi: 10.1371/journal.pone.0120342.
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RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development.

Pfirrmann T , Villavicencio-Lorini P , Subudhi AK , Menssen R , Wolf DH , Hollemann T .

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.

PubMed ID: 25793641
PMC ID: PMC4368662
Article link: PLoS One

Species referenced: Xenopus laevis
Genes referenced: actl6a armc8 cat.1 emx1 en2 herpud1 nkx2-1 odc1 pax6 prkg1 rmnd5a slc5a5 sox2 tubb2b
Antibodies: armc8 AB1 rmnd5a Ab1
Morpholinos: rmnd5a MO1

Phenotypes: Xla Wt + rmnd5a MO (fig.3.A.d) [+]

Article Images: [+] show captions
References [+] :
Andréasson, Hsp110 is a nucleotide-activated exchange factor for Hsp70. 2008, Pubmed