Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

Carujo, Sonia; Estanyol, Josep Marı́a; Ejarque, Ana; Agell, Neus; Bachs, Oriol; Pujol, María Jesús

doi:10.1038/sj.onc.1209433

Cited by 66 publications

(49 citation statements)

References 47 publications

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“…Furthermore the treated cells showed a marked increase of the expression of both glyceraldehyde 3-phosphate dehydrogenase (Gapdh) and enolase. These two proteins are involved in energy metabolism and Gapdh has also been shown to bind the β-amyloid precursor protein [18] and to be involved in transcriptional regulation of cell-cycle [19]. Finally, we observed an increase in the expression level of actin as previously shown in cell exposed to the intracellular domain of the β-amyloid precursor protein [20].…”

Section: Biochimica Et Biophysica Acta 1794 (2009) 1243-1250supporting

confidence: 65%

“…This protein plays a central role in glycolysis, catalyzing the reversible conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. More recent studies have highlighted unexpected non-glycolytic functions of Gapdh in physiological and pathological processes, including transcriptional regulation of cell-cycle [19]. In addition two spots corresponding to actin were up-regulated.…”

Section: Protein Expression Changes In Cells Exposed For 5 H To Hypf-mentioning

confidence: 98%

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Proteomic analysis of cells exposed to prefibrillar aggregates of HypF-N

Magherini

Pieri

Guidi

et al. 2009

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Several human diseases are associated with the deposition of stable ordered protein aggregates known as amyloid fibrils. In addition, a large wealth of data shows that proteins not involved in amyloidoses, are able to form, in vitro, amyloid-like prefibrillar and fibrillar assemblies indistinguishable from those grown from proteins associated with disease. Previous studies showed that early prefibrillar aggregates of the N-terminal domain of the prokaryotic hydrogenase maturation factor HypF (HypF-N) are cytotoxic, inducing early mitochondria membrane depolarization, activation of caspase 9 and eventually cell death. To gain knowledge on the molecular basis of HypF-N aggregate cytotoxicity, we performed a differential proteomic analysis of NIH-3T3 cells exposed to HypF-N prefibrillar aggregates in comparison with control cells. Two-dimensional gel electrophoresis followed by protein identification by MALDI-TOF MS, allowed us to identify 21 proteins differentially expressed. The changes of the expression level of proteins involved in stress response (Hsp60 and 78 kDa glucose-regulated protein) and in signal transduction (Focal adhesion kinase1) appear particularly interesting as possible determinants of the cell fate. The levels of some of the differently expressed proteins were modified also in similar studies carried out on cells exposed to Aβ or α-synuclein aggregates, supporting the existence of shared features of amyloid cytotoxicity.

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Section: Biochimica Et Biophysica Acta 1794 (2009) 1243-1250supporting

confidence: 65%

Section: Protein Expression Changes In Cells Exposed For 5 H To Hypf-mentioning

confidence: 98%

Proteomic analysis of cells exposed to prefibrillar aggregates of HypF-N

Magherini

Pieri

Guidi

et al. 2009

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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“…In contrast, glycolytic pathway enzymes-glyceraldehyde 3-phosphate dehydrogenase and pyruvate kinase M2-were found to be significantly increased in AA/E7 compared with E6/E7 PHFKs (Table 2, Figure 9). In addition, the protein SET (a nuclear oncogene), which is known to bind to glyceraldehyde 3-phosphate dehydrogenase (Carujo et al, 2006), was also expressed significantly higher in AA/E7 compared with E6/E7 PHFKs (Table 2, Figure 9). Finally, we observed a significant reduction in phosphoglucomutase-2 (regulatory enzyme in cellular glucose utilization) and the aldo-ketoreductase protein (AKR1C1) (a 20-a hydroxysteroid dehydrogenase involved in the reduction and elimination of progesterone) in AA/E7 compared with E6/E7 PHFKs (Table 2, Figure 9).…”

Section: Hpv16 E6 Variants C Richard Et Almentioning

confidence: 99%

The immortalizing and transforming ability of two common human papillomavirus 16 E6 variants with different prevalences in cervical cancer

et al. 2010

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Persistent infection with high-risk human papillomaviruses (HPVs), especially type 16 has been undeniably linked to cervical cancer. The Asian-American (AA) variant of HPV16 is more common in the Americas than the prototype in cervical cancer. The different prevalence is based on three amino acid changes within the E6 protein denoted Q14H/H78Y/L83V. To investigate the mechanism(s) behind this observation, both E6 proteins, in the presence of E7, were evaluated for their ability to extend the life span of and transform primary human foreskin keratinocytes (PHFKs). Longterm cell culture studies resulted in death at passage 9 of vector-transduced PHFKs (negative control), but survival of both E6 PHFKs to passage 65 (and beyond). Compared with E6/E7 PHFKs, AA/E7 PHFKs were significantly faster dividing, developed larger cells in monolayer cultures, showed double the epithelial thickness and expressed cytokeratin 10 when grown as organotypic raft cultures. Telomerase activation and p53 inactivation, two hallmarks of immortalization, were not significantly different between the two populations. Both were resistant to anoikis at later passages, but only AA/E7 PHFKs acquired the capacity for in vitro transformation. Proteomic analysis revealed markedly different protein patterns between E6/E7 and AA/E7, particularly with respect to key cellular metabolic enzymes. Our results provide new insights into the reasons underlying the greater prevalence of the AA variant in cervical cancer as evidenced by characteristics associated with higher oncogenic potential.

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“…GAPDH regulates cyclin B-cdk1 activity and thereby the cell cycle progression [39]. It also plays an indispensable role during the S phase-dependent transcription of histone H2B by directly interacting with the DNA binding transcription factor OCT1 while serving a redox sensing role in the H2B gene transcription [40].…”

Section: Diverse Function Of Glyceraldehyde-3-phosphate Dehydrogenasementioning

confidence: 99%

Nuclear GAPDH: changing the fate of Müller cells in diabetes

Jayaguru

Mohr

2011

j ocul biol dis inform

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Müller cells, the primary glial cells are a crucial component of the retinal tissue performing a wide range of functions including maintaining the blood-retinal barrier. Several studies suggest that diabetes leads to Müller cell dysfunction and loss. The pathophysiology of hyperglycemiainduced cellular injury of Müller cells remains only poorly understood. Recently, the concept that translocation of the predominantly cytosolic glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to the nucleus and its accumulation in this cellular compartment alters transcriptional events associated with cell death induction has gained major interest. High glucose conditions induce nuclear translocation and accumulation of GAPDH in the nucleus of Müller cells in vivo and in vitro. With regards to Müller cell dysfunction, the effects of nuclear accumulation of GAPDH are multifaceted. Considering the functional versatility of GAPDH including gene regulation, DNA repair, telomere protection, etc., it is of immense importance to explore possible GAPDH actions to unravel the mysteries around the role of GAPDH in hyperglycemia-induced cellular changes in order to develop novel therapeutic strategies. Therefore, this review focuses on the molecular events associated with the nuclear translocation of GAPDH and how it affects the fate of Müller cells in diabetes.

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Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

Cited by 66 publications

References 47 publications

Proteomic analysis of cells exposed to prefibrillar aggregates of HypF-N

Proteomic analysis of cells exposed to prefibrillar aggregates of HypF-N

The immortalizing and transforming ability of two common human papillomavirus 16 E6 variants with different prevalences in cervical cancer

Nuclear GAPDH: changing the fate of Müller cells in diabetes

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