InterPro domain: IPR045098

This entry represents a group of Gid-type RING finger containing proteins, including Rmd5 and Fyv10 from budding yeasts. Rmd5 and Fyv10 form the heterodimeric E3 ligase unit of the Gid (glucose induced degradation deficient) complex, which is involved in the proteasome-dependent degradation of fructose-1,6-bisphosphatase [ 1 , 2 ].

This entry also includes animal MAEA and RMND5A/B, which are core components of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase complex [ 3 ]. The CTLH complex has been linked to several different functions like regulation of cell morphology, proteasome-dependent degradation of non-ubiquitinated alpha-catenin, or modulation of endosome/lysosome-dependent degradation of ubiquitinated proteins via interaction with HRS (hepatocyte growth factor-regulated tyrosine kinase substrate) [ 4 , 5 ].

1. The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism. Mol. Biol. Cell 19, 3323-33
2. Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. FEBS Lett. 585
3. The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation. Elife 7, 3856-61
4. Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes. J. Biol. Chem. 287, 25602-14