RMD5B, GID2B (5q35.3) E3 ubikitiiniligaasi, tärkeä tuman meioottiselle jaolle.

https://www.ncbi.nlm.nih.gov/gene

Preferred Names

E3 ubiquitin-protein transferase RMND5B; protein RMD5 homolog B

Names

GID complex subunit 2 homolog B

Related articles in PubMed

1. RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development. Pfirrmann T, et al. PLoS One, 2015. PMID 25793641, Free PMC Article
2. Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin. Pope SN, et al. J Steroid Biochem Mol Biol, 2005 Feb. PMID 15862967
3. A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system. van Wijk SJ, et al. Mol Syst Biol, 2009. PMID 19690564, Free PMC Article
4. The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation. Lampert F, et al. Elife, 2018 Jun 18. PMID 29911972, Free PMC Article Abstract
   In yeast, the glucose-induced degradation-deficient (GID) E3 ligase selectively degrades superfluous gluconeogenic enzymes. Here, we identified all subunits of the mammalian GID/CTLH complex and provide a comprehensive map of its hierarchical organization and step-wise assembly. Biochemical reconstitution demonstrates that the mammalian complex possesses inherent E3 ubiquitin ligase activity, using Ube2H as its cognate E2. Deletions of multiple GID subunits compromise cell proliferation, and this defect is accompanied by deregulation of critical cell cycle markers such as the retinoblastoma (Rb) tumor suppressor, phospho-Histone H3 and Cyclin A. We identify the negative regulator of pro-proliferative genes Hbp1 as a bonafide GID/CTLH proteolytic substrate. Indeed, Hbp1 accumulates in cells lacking GID/CTLH activity, and Hbp1 physically interacts and is ubiquitinated in vitro by reconstituted GID/CTLH complexes. Our biochemical and cellular analysis thus demonstrates that the GID/CTLH complex prevents cell cycle exit in G1, at least in part by degrading Hbp1. KEYWORDS: E3 ubiquitin ligase; N-end rule; S. cerevisiae; biochemistry; cell biology; cell proliferation; chemical biology; human; metabolism; mouse; transcription factors
5. The SOX2-interactome in brain cancer cells identifies the requirement of MSI2 and USP9X for the growth of brain tumor cells. Cox JL, et al. PLoS One, 2013. PMID 23667531, Free PMC Article

See all (18) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene