Glutathione transferases, regulators of cellular metabolism and physiology

Board, Philip G.; Menon, Deepthi

doi:10.1016/j.bbagen.2012.11.019

Cited by 345 publications

(296 citation statements)

References 338 publications

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“…We have found the association of GSTO1-1 with Akt (total/phosphorylated) and ASK1 proteins. The Akt kinase family is considered to be the main survival pathway in a various cell types, whereas ASK1 is a member of MAP kinase family and as such is involved in proapoptotic signaling [8,20]. We hypothesised that, similarly to GSTP1, which has a 2wide variety of substrate for S-glutathionylase activity [21], the above-mentioned proteins also might be the targets for GSTO1 deglutathionylase activity.…”

Section: Discussionmentioning

confidence: 99%

Upregulated glutathione transferase omega-1 correlates with progression of urinary bladder carcinoma

et al. 2017

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Section: Discussionmentioning

confidence: 99%

Upregulated glutathione transferase omega-1 correlates with progression of urinary bladder carcinoma

et al. 2017

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“…In vivo GSTPi occurs in monomer-dimer equilibrium and monomer can bind to and regulate JNK and TRAF, which are proteins involved in regulation of apoptosis and cell proliferation. Exposure of the cell to a range of stresses can change the redox potential in the cell causing the dissociation of the complex and oligomerisation of GSTPi [17]. In S. cerevisiae Ure2p was assumed to interact with Gln3p which is a transcription activator in the nitrogen metabolism [18].…”

Section: Discussionmentioning

confidence: 99%

Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium

et al. 2013

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a b s t r a c tGlutathione transferases (GSTs) are known to transfer glutathione onto small hydrophobic molecules in detoxification reactions. The GST Ure2pB1 from Phanerochaete chrysosporium exhibits atypical features, i.e. the presence of two glutathione binding sites and a high affinity towards oxidized glutathione. Moreover, PcUre2pB1 is able to efficiently deglutathionylate GS-phenacylacetophenone. Catalysis is not mediated by the cysteines of the protein but rather by the one of glutathione and an asparagine residue plays a key role in glutathione stabilization. Interestingly PcUre2pB1 interacts in vitro with a GST of the omega class. These properties are discussed in the physiological context of wood degrading fungi. Structured summary of protein interactions:PcUre2pB1 and PcUre2pB1 bind by X-ray crystallography (View interaction) PcUre2pB1 enzymaticly reacts PcGTO3 by enzymatic study (View interaction)

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“…The highly conserved detoxification factors BdGST24 (Board and Menon, 2013), BdCSD2 (Kliebenstein et al, 1998;Alscher et al, 2002;Chu et al, 2005), BdGSC1 (Arabidopsis thaliana MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN1 [MRP1] homolog; Lu et al, 1997), BdGPX6 (BrigeliusFlohé, Maiorino, 2013), BdSOD1 (Kliebenstein et al, 1998;Alscher et al, 2002), and BdMSD1 (Kliebenstein et al, 1998;Alscher et al, 2002) were transcriptionally up-regulated to various levels in B. distachyon leaf or callus tissue under conditions of oxidative stress through sodium arsenite treatment (Fig. 1A, soil application), heavy-metal copper sulfate treatment (Fig.…”

Section: Identification Of Oxidative Stress Transcriptional Reportersmentioning

confidence: 99%

Enhanced Oxidative Stress Resistance through Activation of a Zinc Deficiency Transcription Factor inBrachypodium distachyon

et al. 2014

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Identification of viable strategies to increase stress resistance of crops will become increasingly important for the goal of global food security as our population increases and our climate changes. Considering that resistance to oxidative stress is oftentimes an indicator of health and longevity in animal systems, characterizing conserved pathways known to increase oxidative stress resistance could prove fruitful for crop improvement strategies. This report argues for the usefulness and practicality of the model organism Brachypodium distachyon for identifying and validating stress resistance factors. Specifically, we focus on a zinc deficiency B. distachyon basic leucine zipper transcription factor, BdbZIP10, and its role in oxidative stress in the model organism B. distachyon. When overexpressed, BdbZIP10 protects plants and callus tissue from oxidative stress insults, most likely through distinct and direct activation of protective oxidative stress genes. Increased oxidative stress resistance and cell viability through the overexpression of BdbZIP10 highlight the utility of investigating conserved stress responses between plant and animal systems.

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Glutathione transferases, regulators of cellular metabolism and physiology

Cited by 345 publications

References 338 publications

Upregulated glutathione transferase omega-1 correlates with progression of urinary bladder carcinoma

Upregulated glutathione transferase omega-1 correlates with progression of urinary bladder carcinoma

Atypical features of a Ure2p glutathione transferase from Phanerochaete chrysosporium

Enhanced Oxidative Stress Resistance through Activation of a Zinc Deficiency Transcription Factor inBrachypodium distachyon

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