Redox modifications of protein–thiols: Emerging roles in cell signaling

Biswas, Saibal K; Chida, Asiya Seema; Rahman, Irfan

doi:10.1016/j.bcp.2005.10.044

Cited by 519 publications

(388 citation statements)

References 88 publications

Supporting

Mentioning

376

Contrasting

Unclassified

Order By: Relevance

“…Immunolocalization with antibodies against CHS and chalcone isomerase suggests that the enzymes of flavonoid synthesis are localized to the nucleus in Arabidopsis roots (Saslowsky et al, 2005). The nuclear localization of flavonols is consistent with the notion that ROS can regulate gene expression through interaction with redox-sensitive transcription factors (TFs) in plants (Wu et al, 2012), such as the wellestablished redox-sensitive TF described in bacteria and mammals (Aslund et al, 1999;Biswas et al, 2006). Flavonols are a likely candidate to modulate the activity of redox-sensitive TFs, because of their increased accumulation in the nuclei; however, it is unlikely that they are the only antioxidant present in this organelle.…”

Section: Discussionsupporting

confidence: 64%

Ethylene-Induced Flavonol Accumulation in Guard Cells Suppresses Reactive Oxygen Species and Moderates Stomatal Aperture

2014

View full text Add to dashboard Cite

Guard cell swelling controls the aperture of stomata, pores that facilitate gas exchange and water loss from leaves. The hormone abscisic acid (ABA) has a central role in regulation of stomatal closure through synthesis of second messengers, which include reactive oxygen species (ROS). ROS accumulation must be minimized by antioxidants to keep concentrations from reaching damaging levels within the cell. Flavonols are plant metabolites that have been implicated as antioxidants; however, their antioxidant activity in planta has been debated. Flavonols accumulate in guard cells of Arabidopsis thaliana, but not surrounding pavement cells, as visualized with a flavonolspecific dye. The expression of a reporter driven by the promoter of CHALCONE SYNTHASE, a gene encoding a flavonol biosynthetic enzyme, in guard cells, but not pavement cells, suggests guard cell-specific flavonoid synthesis. Increased levels of ROS were detected using a fluorescent ROS sensor in guard cells of transparent testa4-2, which has a null mutation in CHALCONE SYNTHASE and therefore synthesizes no flavonol antioxidants. Guard cells of transparent testa4-2 show more rapid ABA-induced closure than the wild type, suggesting that flavonols may dampen the ABA-dependent ROS burst that drives stomatal closing. The levels of flavonols are positively regulated in guard cells by ethylene treatment in the wild type, but not in the ethylene-insensitive2-5 mutant. In addition, in both ethyleneoverproducing1 and ethylene-treated wild-type plants, elevated flavonols lead to decreasing ROS and slower ABA-mediated stomatal closure. These results are consistent with flavonols suppressing ROS accumulation and decreasing the rate of ABA-dependent stomatal closure, with ethylene-induced increases in guard cell flavonols modulating these responses.

show abstract

Section: Discussionsupporting

confidence: 64%

Ethylene-Induced Flavonol Accumulation in Guard Cells Suppresses Reactive Oxygen Species and Moderates Stomatal Aperture

2014

View full text Add to dashboard Cite

show abstract

“…Oxidative modification of protein thiols is now considered as an emerging role in cell signaling. It has been well recognized that the thiol oxidation state of reactive cysteine residues in proteins controls the function of the proteins and the pathways that they are part of [49][50][51][52][53][54] . We hypothesize that, during the biphasic redox sensing, the different cysteines of a given protein molecule might be sequentially oxidized by different levels of ROS, thus leading to different conformational characteristics and functional statuses of the protein.…”

Section: Discussionmentioning

confidence: 99%

The biphasic redox sensing of SENP3 accounts for the HIF-1 transcriptional activity shift by oxidative stress

Wang

Yang

et al. 2012

Acta Pharmacol Sin

View full text Add to dashboard Cite

“…Voltage-dependent anion channel and cardiolipin can be oxidized [19,20], which may promote cytochrome c release and collapse of the mitochondrial transmembrane potential. Because ROS may have multiple targets, signaling events that control the balance between pro-and anti-apoptotic factors may also be modulated by oxidative modification of thiols [21,22].…”

Section: Discussionmentioning

confidence: 99%

Oxidative modification of caspase-9 facilitates its activation via disulfide-mediated interaction with Apaf-1

et al. 2009

View full text Add to dashboard Cite

Intracellular reactive oxygen species (ROS) are known to regulate apoptosis. Activation of caspase-9, the initial caspase in the mitochondrial apoptotic cascade, is closely associated with ROS, but it is unclear whether ROS regulate caspase-9 via direct oxidative modification. The present study aims to elucidate the molecular mechanisms by which ROS mediate caspase-9 activation. Our results show that the cellular oxidative state facilitates caspase-9 activation. Hydrogen peroxide treatment causes the activation of caspase-9 and apoptosis, and promotes an interaction between caspase-9 and apoptotic protease-activating factor 1 (Apaf-1) via disulfide formation. In addition, in an in vitro mitochondria-free system, the thiol-oxidant diamide promotes auto-cleavage of caspase-9 and the caspase-9/ Apaf-1 interaction by facilitating the formation of disulfide-linked complexes. Finally, a point mutation at C403 of caspase-9 impairs both H 2 O 2 -promoted caspase-9 activation and interaction with Apaf-1 through the abolition of disulfide formation. The association between cytochrome c and the C403S mutant is significantly weaker than that between cytochrome c and wild-type caspase-9, indicating that oxidative modification of caspase-9 contributes to apoptosome formation under oxidative stress. Taken together, oxidative modification of caspase-9 by ROS can mediate its interaction with Apaf-1, and can thus promote its auto-cleavage and activation. This mechanism may facilitate apoptosome formation and caspase-9 activation under oxidative stress.

show abstract

Redox modifications of protein–thiols: Emerging roles in cell signaling

Cited by 519 publications

References 88 publications

Ethylene-Induced Flavonol Accumulation in Guard Cells Suppresses Reactive Oxygen Species and Moderates Stomatal Aperture

Ethylene-Induced Flavonol Accumulation in Guard Cells Suppresses Reactive Oxygen Species and Moderates Stomatal Aperture

The biphasic redox sensing of SENP3 accounts for the HIF-1 transcriptional activity shift by oxidative stress

Oxidative modification of caspase-9 facilitates its activation via disulfide-mediated interaction with Apaf-1

Contact Info

Product

Resources

About