Catabolite Degradation of Fructose-1,6-bisphosphatase in the Yeast<i>Saccharomyces cerevisiae</i>: A Genome-wide Screen Identifies Eight Novel<i>GID</i>Genes and Indicates the Existence of Two Degradation Pathways

Regelmann, Jochen; Schüle, Thomas; Josupeit, Frank S.; Horák, J.; Rose, Matthias; Entian, Karl‐Dieter; Thumm, Michael; Wolf, Dieter H.

doi:10.1091/mbc.e02-08-0456

Cited by 143 publications

(192 citation statements)

References 41 publications

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“…As is shown in Fig. 6, ⌬gid2 and ⌬gid8 mutants blocked FBPase degradation in 1-day-starved cells, a result that is consistent with earlier reports (28). However, FBPase degradation was also blocked in these strains when they were starved for 3 days.…”

Section: Fig 2 Fbpase Is Targeted To the Vacuole When 3-day-starvedsupporting

confidence: 92%

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Degradation of the Gluconeogenic Enzymes Fructose-1,6-bisphosphatase and Malate Dehydrogenase Is Mediated by Distinct Proteolytic Pathways and Signaling Events

Hung

Brown

Wolfe

et al. 2004

Journal of Biological Chemistry

109

143

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The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is subjected to catabolite inactivation and degradation when glucose-starved cells are replenished with fresh glucose. In various studies, the proteasome and the vacuole have each been reported to be the major site of FBPase degradation. Because different growth conditions were used in these studies, we examined whether variations in growth conditions could alter the site of FBPase degradation. Here, we demonstrated that FBPase was degraded outside the vacuole (most likely in the proteasome), when glucose was added to cells that were grown in low glucose media for a short period of time. By contrast, cells that were grown in the same low glucose media for longer periods of time degraded FBPase in the vacuole in response to glucose. Another gluconeogenic enzyme malate dehydrogenase (MDH2) showed the same degradation characteristics as FBPase in that the short term starvation of cells led to a non-vacuolar degradation, whereas long term starvation resulted in the vacuolar degradation of this protein.The N-terminal proline is required for the degradation of FBPase and MDH2 for both the vacuolar and nonvacuolar proteolytic pathways. The cAMP signaling pathway and the phosphorylation of glucose were needed for the vacuolar-dependent degradation of FBPase and MDH2. By contrast, the cAMP-dependent signaling pathway was not involved in the non-vacuolar degradation of these proteins, although the phosphorylation of glucose was required.

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Section: Fig 2 Fbpase Is Targeted To the Vacuole When 3-day-starvedsupporting

confidence: 92%

“…some (25). Interestingly, a recent genome-wide search has also identified a number of VID genes, including VID24, VID28, and VID30, that are also involved in the proteasomal-dependent degradation of FBPase (28). This suggests that common components exist for both proteolytic pathways.…”

Section: Fig 2 Fbpase Is Targeted To the Vacuole When 3-day-starvedmentioning

confidence: 99%

Degradation of the Gluconeogenic Enzymes Fructose-1,6-bisphosphatase and Malate Dehydrogenase Is Mediated by Distinct Proteolytic Pathways and Signaling Events

Hung

Brown

Wolfe

et al. 2004

Journal of Biological Chemistry

109

143

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“…The mechanism by which Fbp1 is translocated into the completed Vid vesicles remains unknown. The UPS can also target Fbp1 (Horak et al 2002;Regelmann et al 2003;Hung et al 2004) and many other proteins, principally those with a short half-life (Ravid and Hochstrasser 2008). The targets are again individual proteins, but in this case they are tagged with ubiquitin chains and are not sequestered within a vesicle, but rather are recognized by, and degraded within, the proteasome, a multisubunit protein channel that includes deubiquitinating enzymes and proteases.…”

mentioning

confidence: 99%

Autophagic Processes in Yeast: Mechanism, Machinery and Regulation

2013

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Autophagy refers to a group of processes that involve degradation of cytoplasmic components including cytosol, macromolecular complexes, and organelles, within the vacuole or the lysosome of higher eukaryotes. The various types of autophagy have attracted increasing attention for at least two reasons. First, autophagy provides a compelling example of dynamic rearrangements of subcellular membranes involving issues of protein trafficking and organelle identity, and thus it is fascinating for researchers interested in questions pertinent to basic cell biology. Second, autophagy plays a central role in normal development and cell homeostasis, and, as a result, autophagic dysfunctions are associated with a range of illnesses including cancer, diabetes, myopathies, some types of neurodegeneration, and liver and heart diseases. That said, this review focuses on autophagy in yeast. Many aspects of autophagy are conserved from yeast to human; in particular, this applies to the gene products mediating these pathways as well as some of the signaling cascades regulating it, so that the information we relate is relevant to higher eukaryotes. Indeed, as with many cellular pathways, the initial molecular insights were made possible due to genetic studies in Saccharomyces cerevisiae and other fungi. TABLE OF CONTENTS Abstract 341Introduction 342

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“…The GID/MRCTLH protein complex was first discovered in yeast (S. cerevisiae), where it was named GID (glucoseinduced degradation deficient) (Regelmann et al, 2003). GID complex is a 600 kDa assembly of seven proteins (GID1 (VID30), GID2, GID4 (VID24), GID5 (VID28), GID7, GID8 and GID9).…”

Section: Introductionmentioning

confidence: 99%

Integrative meta-analysis of protein interaction data identified multiple GID/MRCTLH protein complexes in plants

Miquel¹,

Vicient²

2017

Plant Omics

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GID/MRCTLH is a protein complex involved in the regulation of several cellular processes through the polyubiquitination and proteosome degradation. It has been described in yeast and mammals. Genes coding for homologous proteins are also present in plant genomes but have been little studied. BLAST analyses revealed that genes coding for members of the GID/MRCTLH complex are found in multiple copies in plants, compared to mammals and yeast. The potential structure of the Arabidopsis GID/MRCTLH complex was estimated based on the Arabidopsis protein interaction database Interactome 2.0. According to these data, Arabidopsis may contain two GID/MRCTLH complexes instead of the one described in yeast and mammals. The structure of the two Arabidopsis complexes seem to be similar to the yeast GID complex, and seem to interact with several other proteins out of the complex. These data suggest that, similarly to yeast and mammals, the plant GID/MRCTLH complexes are involved in the regulation of several cellular processes through proteosome protein degradation.

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Catabolite Degradation of Fructose-1,6-bisphosphatase in the YeastSaccharomyces cerevisiae: A Genome-wide Screen Identifies Eight NovelGIDGenes and Indicates the Existence of Two Degradation Pathways

Cited by 143 publications

References 41 publications

Degradation of the Gluconeogenic Enzymes Fructose-1,6-bisphosphatase and Malate Dehydrogenase Is Mediated by Distinct Proteolytic Pathways and Signaling Events

Degradation of the Gluconeogenic Enzymes Fructose-1,6-bisphosphatase and Malate Dehydrogenase Is Mediated by Distinct Proteolytic Pathways and Signaling Events

Autophagic Processes in Yeast: Mechanism, Machinery and Regulation

Integrative meta-analysis of protein interaction data identified multiple GID/MRCTLH protein complexes in plants

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