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- W3013020157 endingPage "815" @default.
- W3013020157 startingPage "815" @default.
- W3013020157 abstract "Mitochondrial fusion and fission tailors the mitochondrial shape to changes in cellular homeostasis. Players of this process are the mitofusins, which regulate fusion of the outer mitochondrial membrane, and the fission protein DRP1. Upon specific stimuli, DRP1 translocates to the mitochondria, where it interacts with its receptors FIS1, MFF, and MID49/51. Another fission factor of clinical relevance is GDAP1. Here, we identify and discuss cysteine residues of these proteins that are conserved in phylogenetically distant organisms and which represent potential sites of posttranslational redox modifications. We reveal that worms and flies possess only a single mitofusin, which in vertebrates diverged into MFN1 and MFN2. All mitofusins contain four conserved cysteines in addition to cysteine 684 in MFN2, a site involved in mitochondrial hyperfusion. DRP1 and FIS1 are also evolutionarily conserved but only DRP1 contains four conserved cysteine residues besides cysteine 644, a specific site of nitrosylation. MFF and MID49/51 are only present in the vertebrate lineage. GDAP1 is missing in the nematode genome and contains no conserved cysteine residues. Our analysis suggests that the function of the evolutionarily oldest proteins of the mitochondrial fusion and fission machinery, the mitofusins and DRP1 but not FIS1, might be altered by redox modifications." @default.
- W3013020157 created "2020-04-03" @default.
- W3013020157 creator A5000971841 @default.
- W3013020157 creator A5025319223 @default.
- W3013020157 creator A5026145290 @default.
- W3013020157 creator A5029963523 @default.
- W3013020157 creator A5038398867 @default.
- W3013020157 creator A5055066185 @default.
- W3013020157 creator A5056462204 @default.
- W3013020157 creator A5071652372 @default.
- W3013020157 date "2020-03-27" @default.
- W3013020157 modified "2023-10-13" @default.
- W3013020157 title "Redox Modifications of Proteins of the Mitochondrial Fusion and Fission Machinery" @default.
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