ArticleThe Journal of biological chemistry2012
Tissue-specific and nutrient regulation of the branched-chain α-keto acid dehydrogenase phosphatase, protein phosphatase 2Cm (PP2Cm).
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.
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Who cites it
32 citing papers in PubMed, 1 synthesis or guideline pooled it, 70 citations in OpenAlex.
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- The Role of Sirt3 in Kidney Health and Disease.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Phosphatase activity-based PPM1K: a key player in the regulation of mitochondrial function and its multifaceted impact in diseases.Molecular and cellular biochemistry · 2025Review
- BCAA metabolism: the Achilles' heel of ovarian cancer, polycystic ovary syndrome, and premature ovarian failure.Frontiers in endocrinology · 2025Review
- Primary Roles of Branched Chain Amino Acids (BCAAs) and Their Metabolism in Physiology and Metabolic Disorders.Molecules (Basel, Switzerland) · 2024Review
- Assessment of the dietary amino acid profiles and the relative biomarkers for amino acid balance in the low-protein diets for broiler chickens.Journal of animal science and biotechnology · 2024Article
- Protein phosphatase 2Cm-regulated branched-chain amino acid catabolic defect in dorsal root ganglion neurons drives pain sensitization.Acta neuropathologica communications · 2024Article
- Metabolic adaptations in pressure overload hypertrophic heart.Heart failure reviews · 2024Review
- Mitochondrial Alpha-Keto Acid Dehydrogenase Complexes: Recent Developments on Structure and Function in Health and Disease.Sub-cellular biochemistry · 2024Review
- Acute Encephalopathy in a 10-Year-Old Patient With Maple Syrup Urine Disease: A Challenging Diagnosis.Cureus · 2024Article
- PPM1K mediates metabolic disorder of branched-chain amino acid and regulates cerebral ischemia-reperfusion injury by activating ferroptosis in neurons.Cell death & disease · 2023Article
- Small molecule branched-chain ketoacid dehydrogenase kinase (BDK) inhibitors with opposing effects on BDK protein levels.Nature communications · 2023Article
- High doses of rosuvastatin induce impaired branched-chain amino acid catabolism and lead to insulin resistance.Experimental physiology · 2023Article
- Downregulation of extramitochondrial BCKDH and its uncoupling from AMP deaminase in type 2 diabetic OLETF rat hearts.Physiological reports · 2023Article
- Article
- Branched-Chain Amino Acids and Insulin Resistance, from Protein Supply to Diet-Induced Obesity.Nutrients · 2022Review
- Role of branched-chain amino acid metabolism in the pathogenesis of obesity and type 2 diabetes-related metabolic disturbances BCAA metabolism in type 2 diabetes.Nutrition & diabetes · 2022Review
- A Gain-of-Function Mutation onGenes · 2022Article
- The role of serine/threonine phosphatases in human development: Evidence from congenital disorders.Frontiers in cell and developmental biology · 2022Review
- Oral administration of branched-chain amino acids ameliorates high-fat diet-induced metabolic-associated fatty liver diseaseFrontiers in microbiology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Branched-chain amino acid (BCAA) homeostasis is maintained through highly regulated catabolic activities where the rate-limiting step is catalyzed by branched-chain α-keto dehydrogenase (BCKD). Our previous study has identified a mitochondria-targeted protein phosphatase, PP2Cm, as the BCKD phosphatase and thus serves as a key regulator for BCAA catabolism. In this report, we performed comprehensive molecular and biochemical studies of PP2Cm regulation using both in vivo and in vitro systems. We show that PP2Cm expression is highly enriched in brain, heart, liver, kidney, and diaphragm, but low in skeletal muscle. The PP2Cm expression is regulated at the transcriptional level in response to nutrient status. Furthermore, we have established that PP2Cm interacts with the BCKD E2 subunit and competes with the BCKD kinase in a substrate-dependent and mutually exclusive manner. These data suggest that BCAA homeostasis is at least in part contributed by nutrient-dependent PP2Cm expression and interaction with the BCKD complex. Finally, a number of human PP2Cm single nucleotide polymorphic changes as identified in the public data base can produce either inactive or constitutive active mutant phosphatases, suggesting that putative PP2Cm mutations may contribute to BCAA catabolic defects in human.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.