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The samples were sonicated in a water bath for 5 min and frozen for a short time before being homogenised using Disruptor Genie at maximal speed on 2800 rpm for 2 min, incubated on ice for 2 min, repeating these steps five times. The samples were then centrifuged at 14,000 g for 10 min at 4°C. The supernatant was collected, and the probe sonicated for 40 s with 20% amplitude 2-2 s on/off before protein concentration was determined by BCA assay (Pierce). Samples were prepared according to the protocol published previously [bioRxiv 2023.08.31.555796; doi: https://doi.org/10.1101/2023.08.31.555796]. For expression proteomics, an aliquot of 25 µg samples was supplemented with 50 mM Tris-HCl to 100 µl and reduced with 2 µl of 0.5M dithiothreitol (DTT) at 37°C for 30 min, then alkylated with 6.5 µl of iodoacetamide (IAA) at 25°C for 1 h in the dark. The excess of IAA was quenched with 4.5 µl of 0.5M DTT at 25°C for 30 min, followed by protein precipitation with chilled acetone at -20°C overnight. Pellets were solubilised in 12.5 µl of 8M urea and sonicated in a water bath for 10 min before adding 87.5 µl of Tris-HCl buffer. Samples were digested with 0.5 µg of sequencing-grade modified trypsin (Promega) and incubated for 16 h at 37°C. The digestion was stopped with 6 µl cc-formic acid (FA), incubating the solutions for 5 min. The sample was cleaned on a C18 Hypersep plate with 40 µl bed volume (Thermo Fisher Scientific) and dried using a vacuum concentrator (Eppendorf). For redox proteomics, another aliquot of 50 µg samples was first supplemented with 20 mM EPPS, pH 8.5 up to 100 µl and alkylated with 6.4 µl of 0.5M IAA at 25°C for 1 h in the dark. Proteins were precipitated with chloroform/methanol. Pellets were solubilised in 12.5 µl of 8M urea and sonicated in a water bath for 10 min before adding 40 µl of 20 mM EPPS, pH 7.2. Oxidised cysteines were reduced then with 3.4 µl of 0.5 DTT and incubated at 25°C for 45 min before adding 56 µl of 100 mM N-ethylmaleimide in 20 mM EPPS, pH 7.2 and incubated at 25°C for 2 h in the dark. Fully alkylated proteins were precipitated with chloroform/methanol and resuspended with 12.5 µl of 8M urea. Following sonication in a water bath for 10 min, the solutions were supplemented with 87.5 µl of 20 mM EPPS, pH 8.5 to increase pH above neutral, and 1 µg trypsin was added and incubated for 6 h at 25°C. The sample was cleaned on a C18 Hypersep plate with 40 µl bed volume (Thermo Fisher Scientific) and dried using a vacuum concentrator (Eppendorf). All twelve samples were solubilised in 70 µl of 50 mM triethylammonium bicarbonate buffer, and 125 µg of TMTpro reagent in 30 µl anhydrous acetonitrile (ACN) was added and incubated at room temperature for 2 h before quenching with 0.5% hydroxylamine for 15 min. Samples were combined and dried in a vacuum before being dissolved in 41 µl of 20 mM ammonium hydroxide and were loaded onto an XBridge bridged ethyl hybrid C18 UPLC column (2.1 mm inner diameter × 250 mm, 2.5 μm particle size, Waters), and profiled with a linear gradient of 5–60% 20 mM ammonium hydroxide in ACN (pH 10.0) over 48 min, at a flow rate of 200 µl/min. The chromatographic performance was monitored by sampling eluate with a UV detector (Ultimate 3000 UPLC, Thermo Fisher Scientific) scanning at 214 nm. Fractions were collected at 30 s intervals into a 96-well plate and combined in 12 samples, concatenating 8-8 fractions representing peak peptide elution before drying in a vacuum. Peptides were reconstituted in solvent A and approximately two µg samples were injected on a 50 cm long EASY-Spray C18 column (Thermo Fisher Scientific) connected to an Ultimate 3000 nanoUPLC system (Thermo Fisher Scientific) using a 90 min long gradient: 4-26% of solvent B (98% acetonitrile, 0.1% FA) in 90 min, 26-95% in 5 min, and 95% of solvent B for 5 min at a flow rate of 300 nL/min. Mass spectra were acquired on a Q Exactive HF hybrid quadrupole-Orbitrap mass spectrometer (Thermo Fisher Scientific) ranging from m/z 375 to 1500 at a resolution of R=120,000 (at m/z 200) targeting 5x106 ions for maximum injection time of 80 ms, followed by data-dependent higher-energy collisional dissociation (HCD) fragmentations of precursor ions with a charge state 2+ to 7+, using 45 s dynamic exclusion. The tandem mass spectra of the top 18 precursor ions were acquired with a resolution of R=60,000, targeting 2x105 ions for a maximum injection time of 54 ms, setting quadrupole isolation width to 1.4 Th and normalised collision energy to 33%."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Acquired raw data files were analysed using Proteome Discoverer v3.0 (Thermo Fisher Scientific) with Mascot Server v2.5.1 (Matrix Science Ltd., UK) search engine against mouse protein database (SwissProt). A maximum of two missed cleavage sites were allowed for complete tryptic digestion while setting the precursor and the fragment ion mass tolerance to 10 ppm and 0.02 Da, respectively. Carbamidomethylation and N-ethylmaleimide modification of cysteine, TMTpro on lysine and N-termini, oxidation of methionine, as well as deamidation of asparagine and glutamine were set as dynamic modifications. Initial search results at the peptide level were filtered with 5% FDR using the Percolator node in Proteome Discoverer. Quantification was based on the TMT-reporter ion intensities. RStudio was used for downstream analysis."],"omics_type":["Proteomics"],"labhead":["Akos Vegvari"],"instrument_platform":[""],"labhead_affiliation":["Karolinska Institutet"],"species":["Mus Musculus (mouse)"],"submission_type":["PARTIAL"],"publication":["Not available"],"submitter_mail":["akos.vegvari@ki.se"],"submitter_affiliation":["Karolinska Institutet"],"submitter_country":["Sweden"],"additional_accession":[]},"is_claimable":false,"name":"Loss of the Mitochondrial SAM Transporter Reveals a Lipoylation-Dependent Metabolic Vulnerability in the Postnatal Heart","description":"SLC25A26 encodes the sole mitochondrial S-adenosylmethionine carrier (SAMC). Inside mitochondria, SAM functions as a methyl group donor for various methyltransferases and as a substrate for radical SAM enzymes. Variants in SAMC are associated with mitochondrial disease, and we previously demonstrated that the mitochondrial methylation potential links the one-carbon pool to energy metabolism, but tissue-specific responses are poorly understood. Here, we studied the physiological, molecular, and metabolic consequences of a SAMC deficiency in heart or skeletal muscle. While SAMC ablation in skeletal muscle causes a progressive decline resembling other mitochondrial myopathies, cardiac-specific deletion causes a severe and sudden cardiac phenotype driven by a rapid loss of lipoylation of 2-oxoacid dehydrogenases. This collapse coincides with the transition from milk to solid food, causing a natural reduction in medium-chain fatty acids. We demonstrate that octanoic acid becomes rate-limiting during this transition, exposing a critical requirement for lipoic acid during cardiac maturation.","dates":{"publication":"2026-07-03","submission":"2024-03-08"},"accession":"PXD050486","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:37919","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:291146","NEWT:29466","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:2003758","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:9900","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:232021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