| Structural highlights
Function
RMD5_YEAST E3 ubiquitin-protein ligase component of the GID complex (PubMed:12686616, PubMed:18508925). Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:9737955, PubMed:18508925). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:9737955, PubMed:12686616, PubMed:18508925, PubMed:28126757).[1] [2] [3] [4]
References
- ↑ Regelmann J, Schule T, Josupeit FS, Horak J, Rose M, Entian KD, Thumm M, Wolf DH. Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell. 2003 Apr;14(4):1652-63. doi: 10.1091/mbc.e02-08-0456. PMID:12686616 doi:https://dx.doi.org/10.1091/mbc.e02-08-0456
- ↑ Santt O, Pfirrmann T, Braun B, Juretschke J, Kimmig P, Scheel H, Hofmann K, Thumm M, Wolf DH. The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism. Mol Biol Cell. 2008 Aug;19(8):3323-33. doi: 10.1091/mbc.e08-03-0328. Epub 2008, May 28. PMID:18508925 doi:https://dx.doi.org/10.1091/mbc.e08-03-0328
- ↑ Chen SJ, Wu X, Wadas B, Oh JH, Varshavsky A. An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes. Science. 2017 Jan 27;355(6323). pii: 355/6323/eaal3655. doi:, 10.1126/science.aal3655. PMID:28126757 doi:https://dx.doi.org/10.1126/science.aal3655
- ↑ Hammerle M, Bauer J, Rose M, Szallies A, Thumm M, Dusterhus S, Mecke D, Entian KD, Wolf DH. Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. J Biol Chem. 1998 Sep 25;273(39):25000-5. doi: 10.1074/jbc.273.39.25000. PMID:9737955 doi:https://dx.doi.org/10.1074/jbc.273.39.25000
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