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MetabolomicsMitochondrial KMT9 methylates DLAT to control pyruvate dehydrogenase activity and prostate cancer growth

Prostate cancer (PCa) growth depends on de novo lipogenesis controlled by the mitochondrial pyruvate dehydrogenase complex (PDC). In this study, we identified lysine methyltransferase (KMT)9 as a novel regulator of PDC activity. KMT9 is localized in mitochondria of PCa cells, but not in mitochond...

2024-12-10 | MTBLS2452 | MetaboLights
ProteomicsDepletion of histone methyltransferase KMT9 inhibits lung cancer cell proliferation by inducing non-apoptotic cell death
Background: Lung cancer is the leading cause of cancer related death worldwide. Over the past 15 years no major improvement of survival rates could be accomplished. The recently discovered histone methyltransferase KMT9 as epigenetic regulator of prostate tumor growth has now raised hopes of enablin...
ORGANISM(S): Homo sapiens (Human) 
2020-05-26 | PXD014145 | Pride
Kmt9 Non-small cell lung cancer Proteomics Epigenetics Histone methyltransferase Lung cancer A549 Transcriptomics 
ProteomicsMitochondrial KMT9 methylates DLAT to control pyruvate dehydrogenase activity, de novo lipogenesis, and prostate cancer growth
Prostate cancer (PCa) growth depends on de novo lipogenesis controlled by the mitochondrial pyruvate dehydrogenase complex (PDC). In this study, we identified lysine methyltransferase (KMT)9 as a novel regulator of PDC activity. KMT9 is localized in mitochondria of PCa cells, but not in mitochondria...
ORGANISM(S): Homo sapiens (Human) 
2024-12-03 | PXD053942 | Pride
Protein methylation Metabolism Mitochondria 
ProteomicsKMT9 writes the histone mark H4K12me1 and controls metabolism and proliferation of castration-resistant prostate cancer cells
Posttranslational modifications of histones such as methylation regulate chromatin structure and gene expression. Methylation of histone lysine residues is generally performed by SET domain methyltransferases. Here, we identify the heterodimeric C21orf127/TRMT112 complex as a specific histone methyl...
ORGANISM(S): Homo sapiens (Human) 
2019-03-11 | PXD008965 | Pride
Kmt9 Lysine methylation H4k12me1 Prostate cancer Methyl-silac Chromatin Methyltransferase Trmt112 
GenomicsKMT9 is an actionable target in muscle-invasive bladder cancer
KMT9 is an actionable target in muscle-invasive bladder cancer
PRJNA1074717 | ENA
UnknownStructure-Guided Design of a KMT9 Inhibitor Prodrug with Cellular Activity.
Not available
S-EPMC12257510 | biostudies-literature
UnknownMitochondrial KMT9 methylates DLAT to control pyruvate dehydrogenase activity and prostate cancer growth.
Not available
S-EPMC11782658 | biostudies-literature
UnknownStructure-guided design of a selective inhibitor of the methyltransferase KMT9 with cellular activity.
Not available
S-EPMC10762027 | biostudies-literature
UnknownLysine Methyltransferase 9 (KMT9) Is an Actionable Target in Muscle-Invasive Bladder Cancer.
Not available
S-EPMC11049522 | biostudies-literature
GenomicsStructure-guided design of a selective inhibitor of the methyltransferase KMT9 with cellular activity
Structure-guided design of a selective inhibitor of the methyltransferase KMT9 with cellular activity
PRJNA986527 | ENA
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