{"type": "root", "children": [{"type": "t", "text": "<head>\n <meta charset=\"UTF-8\">\n <title>CSKMT Function Summary</title>\n </head>\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n CSKMT is a mitochondrial methyltransferase that specifically targets citrate synthase, catalyzing the methylation of a key lysine residue (Lys-368) in the enzyme. Although this post‐translational modification occurs near the active site, experimental evidence indicates that the methylation does not alter citrate synthase’s enzymatic activity. Instead, the modification is proposed to play a role in the organization of citric acid cycle metabolons by potentially influencing protein–protein interactions or substrate channelling among TCA cycle enzymes. In this context, CSKMT contributes to the fine‐tuning of mitochondrial metabolism without directly compromising the catalytic function of citrate synthase. Proteomic studies using mitochondrial fractionation approaches have identified CSKMT (encoded by METTL12) as a member of the low‐abundance mitochondrial protein cohort, implicating it in the broader regulatory network that underpins metabolic activity and cellular bioenergetics."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Virginie F Rhein, Joe Carroll, Shujing Ding, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human METTL12 is a mitochondrial methyltransferase that modifies citrate synthase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/1873-3468.12649"}], "href": "https://doi.org/10.1002/1873-3468.12649"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28391595"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28391595"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Jędrzej Małecki, Magnus E Jakobsson, Angela Y Y Ho, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Uncovering human METTL12 as a mitochondrial methyltransferase that modulates citrate synthase activity through metabolite-sensitive lysine methylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M117.808451"}], "href": "https://doi.org/10.1074/jbc.M117.808451"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28887308"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28887308"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Maurizio Ronci, Luisa Pieroni, Viviana Greco, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Sequential Fractionation Strategy Identifies Three Missing Proteins in the Mitochondrial Proteome of Commonly Used Cell Lines."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Proteome Res (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/acs.jproteome.8b00422"}], "href": "https://doi.org/10.1021/acs.jproteome.8b00422"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30284448"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30284448"}]}]}]}