F(1,6) bifosfataasin entsymin hajoittaa u´E3 ubikitiiniligaasi, joka hajoaa myös itse proteosomilla.
Muut E3
ubikitiiniligaasit
- HiilihydraattiaineenvaihduntaHiivassa:
Mol
Biol Cell. 2008 Aug; 19(8): 3323–3333.
doi:
[10.1091/mbc.E08-03-0328]
PMCID: PMC2488282
PMID: 18508925
The
Yeast GID Complex, a Novel
Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate
Metabolism
Olivier
Santt,*† Thorsten
Pfirrmann,*†‡ Bernhard
Braun,* Jeannette
Juretschke,* Philipp
Kimmig,* Hartmut
Scheel,§ Kay
Hofmann,§ Michael
Thumm,*‖ and Dieter
H. Wolf*
Thomas Sommer, Monitoring Editor
The Gid complex, a novel ubiquitin ligase (E3) required for the degradation of the key gluconeogenic enzyme fructose-1,6-bisphosphatase. The Gid complex binds to FBPase, when S. cerevisiae cells are growing on an ethanol-containing medium. On shift of cells to glucose, Gid4/Vid24 occurs and activates the complex, which then polyubiquitinates FBPase before its degradation by the proteasome. Gid4/Vid24 is itself degraded by the proteasome.
Gid protein homologues were also found to form a complex in mammals (Kobayashi et al., 2007 ). Although no function for this CTLH complex has been described, one subunit has been implicated in proteasomal degradation of α-catenin (Suzuki et al., 2008 ). This suggests that the CTLH complex, like the Gid complex, might also bear E3 activity.
In conclusion (Figure 8), our study shows that the Gid complex is a new ubiquitin ligase with novel types of subunits involved in catabolite degradation of gluconeogenic enzymes in yeast. We also identify Vid24/Gid4 as an important regulator of its ubiquitin ligase activity.
ENTÄ tämän E3 ubikitiiniligaasihomologin tehtävät ihmisessä?
Löytyy kaksi geeniä
RMD5A, GID2A, CTLH , Kr. 2 required for meiotic division
RMD5B, GID2B, kr.5
required ofr meiotic nuclear division
Katson näistä enemmän tietoa onko niillä yhteyttä sokeriaineenvaihduntaan kuten hiivassa, josa se hajoitaa fruktoosi1,6,-bifosfaataasia.
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