2020
DOI: 10.1105/tpc.19.00535
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Matrix Redox Physiology Governs the Regulation of Plant Mitochondrial Metabolism through Posttranslational Protein Modifications

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Cited by 78 publications
(73 citation statements)
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“…Ascorbate is very important in mitochondrial metabolism where it participates in the ascorbate-glutathione cycle that removes H 2 O 2 produced by the respiratory chain e.g., [ 37 ]. The last step in ascorbate biosynthesis takes place on the outer surface of the IMM [ 38 ], but to date no ascorbate transporter has been identified in the IMM.…”
Section: The Different Transporter Classes and Familiesmentioning
confidence: 99%
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“…Ascorbate is very important in mitochondrial metabolism where it participates in the ascorbate-glutathione cycle that removes H 2 O 2 produced by the respiratory chain e.g., [ 37 ]. The last step in ascorbate biosynthesis takes place on the outer surface of the IMM [ 38 ], but to date no ascorbate transporter has been identified in the IMM.…”
Section: The Different Transporter Classes and Familiesmentioning
confidence: 99%
“…In shotgun proteomics, many mitochondrial transporters have been observed to have PTMs of various types: (i) oxidations to give carbonylated side chains on primarily Lys and Pro or sulfoxide on Met [ 18 ], although the latter is probably an analytical artefact in some cases; (ii) phosphorylation of Ser, Thr, and Tyr [ 50 , 51 , 52 ]; (iii) acetylation of Lys [ 53 ]; and (iv) conjugation of Lys side chains with oxidative degradation products of polyunsaturated fatty acids, for instance, 4-hydroxynonenal (HNE) [ 54 , 55 ]. Many of these modifications are no doubt regulatory, while others are damaging and lead to proteolytic degradation [ 37 , 56 , 57 ].…”
Section: Posttranslational Modifications Of Transportersmentioning
confidence: 99%
“…It is becoming widely acknowledged that many PTMs detected using advanced and highly sensitive MS techniques constitute biochemical noise of the system, not regulatory mechanisms [47,48]. Separating bona fide regulatory sites from biochemical noise now presents a major technological hurdle.…”
Section: Discussionmentioning
confidence: 99%
“…Another important mechanism affecting S-nitrosation state of proteins may be through TRX activity, which similarly to GSNOR, can degrade S-nitrosothiols to increase their turnover ratio ( Benhar et al, 2008 ). Several S-nitrosated enzymes that are summarized in this review have been also shown to be targets of mitochondrial TRX (see review in Møller et al, 2020 ). From plant S-nitrosation studies under abiotic stresses ( Fares et al, 2011 ; Camejo et al, 2013 ; Puyaubert et al, 2014 ), it could be suggested that under those conditions, the effect of the stress does not produce large changes on the S-nitrosation status of the cells, probably due to other mechanisms that could be competing with the S-nitrosation process.…”
Section: Mitochondrial Targets Of S-oxidation S-glutathionylation Smentioning
confidence: 99%