ArticleMethods in enzymology2009
Functional characterization of a mitochondrial Ser/Thr protein phosphatase in cell death regulation.
Article in Methods in enzymology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 32 citations in OpenAlex.
- Branched-chain α-keto acids impair glucose-stimulated insulin secretion in pancreatic β-cells under diabetes by reactivating the LDHA-lactate axis.Nature communications · 2026Article
- Phosphatase activity-based PPM1K: a key player in the regulation of mitochondrial function and its multifaceted impact in diseases.Molecular and cellular biochemistry · 2025Review
- 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
- Bicalutamide Exhibits Potential to Damage Kidney via Destroying Complex I and Affecting Mitochondrial Dynamics.Journal of clinical medicine · 2021Article
- p107 mediated mitochondrial function controls muscle stem cell proliferative fates.Nature communications · 2021Article
- Regulation of PP2Cm expression by miRNA-204/211 and miRNA-22 in mouse and human cells.Acta pharmacologica Sinica · 2015Article
- Branched-chain amino acids in metabolic signalling and insulin resistance.Nature reviews. Endocrinology · 2014Review
- Adipose transplant for inborn errors of branched chain amino acid metabolism in mice.Molecular genetics and metabolism · 2013Article
- Cardiac mitochondrial matrix and respiratory complex protein phosphorylation.American journal of physiology. Heart and circulatory physiology · 2012Review
- NOX4-Dependent Hydrogen Peroxide Overproduction in Human Atrial Fibrillation and HL-1 Atrial Cells: Relationship to Hypertension.Frontiers in physiology · 2012Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Protein phosphorylation is a major form of posttranslational modification critical to cell signaling that also occurs in mitochondrial proteome. Yet, only very limited studies have been performed to characterize mitochondrial-targeted protein kinases or phosphatases. Recently, we identified a novel member of PP2C family (PP2Cm) that is a resident mitochondrial protein phosphatase which plays an important role in normal development and cell survival. In this chapter, we will describe the methods applied in the identification of PP2Cm as a resident mitochondrial protein phosphatase based on sequence analysis and biochemical characterization. We will also provide experimental protocols used to establish the intracellular localization of PP2Cm, to achieve loss and gain function of PP2Cm in cultured cells and intact tissue, and to assess the impact of PP2Cm deficiency on cell death, mitochondria oxidative phosphorylation and permeability transition pore opening.
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Registered trials
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