2012
DOI: 10.1074/jbc.m112.363762
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Exploring the Topology of the Gid Complex, the E3 Ubiquitin Ligase Involved in Catabolite-induced Degradation of Gluconeogenic Enzymes

Abstract: Background:The Gid ubiquitin ligase of yeast is composed of seven subunits that contain several remarkable motifs. Results: Using a series of deletion mutants we performed co-immunoprecipitation studies to unravel the arrangement of the subunits. Conclusion: An initial model of the topology of the Gid complex is created. Significance: The model provides the basis to understand the functionality of the Gid complex.

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Cited by 87 publications
(133 citation statements)
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“…In this report, Varshavsky and colleagues demonstrated that Gid4 subunit of the GID E3 ubiquitin ligase is the major recognin responsible for targeting substrates with an Nterminal proline. This report builds upon previous investigations on protein degradation of these enzymes during the switch from gluconeogenesis to glycolysis which had identified the dependence of protein degradation on the N-terminal proline (Hammerle et al 1998) and suggested this was dependent on Gid1 (Menssen et al 2012;Santt et al 2008). While these key elements were previously identified, the identification and determination of the essential role of Gid4 in substrate recognition was not reported.…”
Section: Ac-n-end Rulementioning
confidence: 99%
“…In this report, Varshavsky and colleagues demonstrated that Gid4 subunit of the GID E3 ubiquitin ligase is the major recognin responsible for targeting substrates with an Nterminal proline. This report builds upon previous investigations on protein degradation of these enzymes during the switch from gluconeogenesis to glycolysis which had identified the dependence of protein degradation on the N-terminal proline (Hammerle et al 1998) and suggested this was dependent on Gid1 (Menssen et al 2012;Santt et al 2008). While these key elements were previously identified, the identification and determination of the essential role of Gid4 in substrate recognition was not reported.…”
Section: Ac-n-end Rulementioning
confidence: 99%
“…Although one subunit (Apc2) of APC/C contains a cullin-like domain, the overall ligase architecture is very different from that of true CRLs. Detailed studies of other RING domain proteins (Table 2) may identify additional multisubunit E3s as has been shown for the seven-subunit Gid (glucose-induced degradation-deficient) E3, which controls the metabolic switch between glycolysis and gluconeogenesis (Santt et al 2008;Menssen et al 2012). APC/C: APC/C is perhaps the most complex ubiquitin ligase.…”
Section: Ring Domain Ubiquitin Ligasesmentioning
confidence: 99%
“…When S. cerevisiae grow on ethanol as a carbon source, gluconeogenic enzymes such as Mdh2 are expressed and long-lived. Transition to a medium containing glucose inhibits the synthesis of gluconeogenic enzymes and induces their degradation, which is mediated by the multisubunit GID Ub ligase (54,78,79). Gid4, a subunit of GID, was recently identified as the N-recognin of a distinct N-end rule pathway, termed the Pro/N-end rule pathway ( Fig.…”
Section: The Promoter Reference Technique (Prt)mentioning
confidence: 99%
“…S1C) (Fig. S1C) (54,78,79). Degradation assays of the present study focus on Mdh2, a physiological substrate of the Pro/N-end rule pathway (Fig.…”
Section: Prt Vis-à-vis the Pro/n-end Rule Pathwaymentioning
confidence: 99%