Gutenberg Open Science: Redox modifications of proteins of the mitochondrial fusion and fission machinery

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-5090

Full metadata record

DC Field	Value	Language
dc.contributor.author	Wolf, Christina	-
dc.contributor.author	López del Amo, Víctor	-
dc.contributor.author	Arndt, Sabine	-
dc.contributor.author	Bueno, Diones	-
dc.contributor.author	Tenzer, Stefan	-
dc.contributor.author	Hanschmann, Eva-Maria	-
dc.contributor.author	Berndt, Carsten	-
dc.contributor.author	Methner, Axel	-
dc.date.accessioned	2020-08-27T07:30:17Z	-
dc.date.available	2020-08-27T07:30:17Z	-
dc.date.issued	2020	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/5094	-
dc.description.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. Keywords: mitochondria; fusion; fission; redox; metabolism; thiol switch	en_GB
dc.description.sponsorship	DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin Mainz	-
dc.language.iso	eng	de
dc.rights	CC BY	de_DE
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	-
dc.subject.ddc	570 Biowissenschaften	de_DE
dc.subject.ddc	570 Life sciences	en_GB
dc.subject.ddc	610 Medizin	de_DE
dc.subject.ddc	610 Medical sciences	en_GB
dc.title	Redox modifications of proteins of the mitochondrial fusion and fission machinery	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-5090	-
jgu.type.contenttype	Scientific article	de
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 04 Medizin	de
jgu.organisation.number	2700	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	Cells	de
jgu.journal.volume	9	de
jgu.journal.issue	4	de
jgu.pages.alternative	815	de
jgu.publisher.year	2020	-
jgu.publisher.name	MDPI	de
jgu.publisher.place	Basel	-
jgu.publisher.uri	https://doi.org/10.3390/cells9040815	de
jgu.publisher.issn	2073-4409	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	570	de
jgu.subject.ddccode	610	de
jgu.publisher.doi	10.3390/cells9040815
jgu.organisation.ror	https://ror.org/023b0x485
Appears in collections:	JGU-Publikationen

Files in This Item:

	File	Description	Size	Format
	wolf_christina-redox_modifica-20200820171211822.pdf		1.46 MB	Adobe PDF	View/Open

Show simple item record