PROSITE documentation PDOC51867Gid-type RING finger profile
The two major antagonistic pathways of carbon metabolism in cells, glycolysis and gluconeogenesis, are tigthly regulated. In yeast, the switch from gluconeogenesis to glycolysis is brought about by proteasomal degradation of the gluconeogenetic enzyme fructose-1.6-bisphosphate. The ubiquitin ligase responsible for polyubiquitylation of fructose-1,6-bisphophate 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 (see <PDOC00449>) providing E3 ligase activity. The two subunits form the heterodimaric E3 ligase unit of the Gid complex [1,2]. An orthologous complex, called the CTLH complex is found in mammalian cells. The CTLH complex has been linked to several different functions like regulation of cell morphology, proteasome-dependent degradation of non-ubiquitinated α-catenin, or modulation of endosome/lysosome-dependent degradation of ubiquitinated proteins via interaction with HRS (hepatocyte growth factor-regulated tyrosine kinase substrate) [3,4].
The degenerated Gid-type RING finger is characterized by an incomplete series of Zn(2+) 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 [1,2].
The profile we developed covers the entire Gid-type RING finger.
Last update:July 2018 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Santt O. Pfirrmann T. Braun B. Juretschke J. Kimmig P. Scheel H. Hofmann K. Thumm M. Wolf D.H. |
| Title | The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism. | |
| Source | Mol. Biol. Cell. 19:3323-3333(2008). | |
| PubMed ID | 18508925 | |
| DOI | 10.1091/mbc.e08-03-0328 |
| 2 | Authors | Braun B. Pfirrmann T. Menssen R. Hofmann K. Scheel H. Wolf D.H. |
| Title | Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. | |
| Source | FEBS. Lett. 585:3856-3861(2011). | |
| PubMed ID | 22044534 | |
| DOI | 10.1016/j.febslet.2011.10.038 |
| 3 | Authors | Menssen R. Schweiggert J. Schreiner J. Kusevic D. Reuther J. Braun B. Wolf D.H. |
| Title | Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes. | |
| Source | J. Biol. Chem. 287:25602-25614(2012). | |
| PubMed ID | 22645139 | |
| DOI | 10.1074/jbc.M112.363762 |
| 4 | Authors | Lampert F. Stafa D. Goga A. Soste M.V. Gilberto S. Olieric N. Picotti P. Stoffel M. Peter M. |
| Title | The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets the transcription factor Hbp1 for degradation. | |
| Source | Elife 7:0-0(2018). | |
| PubMed ID | 29911972 | |
| DOI | 10.7554/eLife.35528 |
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