Article
SUCLA2 mutations cause global protein succinylation contributing to the pathomechanism of a hereditary mitochondrial disease.
Nature communications - 23 Nov 2020
Gut Philipp, Matilainen Sanna, Meyer Jesse G, Pällijeff Pieti, Richard Joy, Carroll Christopher J, Euro Liliya, Jackson Christopher B, Isohanni Pirjo, Minassian Berge A, Alkhater Reem A, Østergaard Elsebet, Civiletto Gabriele, Parisi Alice, Thevenet Jonathan, Rardin Matthew J, He Wenjuan, Nishida Yuya, Newman John C, Liu Xiaojing, Christen Stefan, Moco Sofia, Locasale Jason W, Schilling Birgit, Suomalainen Anu, Verdin Eric
Abstract excerpt
Mitochondrial acyl-coenzyme A species are emerging as important sources of protein modification and damage. Succinyl-CoA ligase (SCL) deficiency causes a mitochondrial encephalomyopathy of unknown pathomechanism. Here, we show that succinyl-CoA accumulates in cells derived from patients with recessive mutations in the tricarboxylic acid cycle (TCA) gene succinyl-CoA ligase subunit-β (SUCLA2), causing global...
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