| Description | The two major antagonistic pathways of carbon metabolism in cells, glycolysis and gluconeogenesis, are tightly regulated. In yeast, the switch from gluconeogenesis to glycolysis is brought about by proteasomal degradation of the gluconeogenic enzyme fructose-1,6-bisphosphate. The ubiquitin ligase responsible for polyubiquitylation of fructose-1,6-bisphosphate is the Gid (glucose induced degradation deficient) complex. This complex consists of seven subunits of which two, Gid2/Rmd5 and Gid9/Fyv10, contain a degenerated RING finger domain providing E3 ligase activity. The two subunits form the heterodimeric E3 ligase unit of the Gid complex [ , ]. The orthologous complex found in mammalian cells is called CTLH, which 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) [, ].This entry represents the degenerated Gid-type RING finger which comprises an incomplete serie of Zn ion-coordinating residues compared with the canonical RING finger, which encompasses eight Cys/His residues coordinating two Zn cations. A complete cysteine and histidine pattern is not necessarily critical for the E3 function [ , ]. | Name | Gid-type RING finger domain |
| Short Name | ZF_RING_GID | Type | Domain |
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