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NUAK: never underestimate a kinase. NUAK：永远不要低估激酶。
IF 5.6 2区 生物学
Essays in biochemistry Pub Date : 2024-11-18 DOI: 10.1042/EBC20240005
George L Skalka, Declan Whyte, Dominika Lubawska, Daniel J Murphy
{"title":"NUAK: never underestimate a kinase.","authors":"George L Skalka, Declan Whyte, Dominika Lubawska, Daniel J Murphy","doi":"10.1042/EBC20240005","DOIUrl":"10.1042/EBC20240005","url":null,"abstract":"<p><p>NUAK1 and NUAK2 belong to a family of kinases related to the catalytic α-subunits of the AMP-activated protein kinase (AMPK) complexes. Despite canonical activation by the tumour suppressor kinase LKB1, both NUAKs exhibit a spectrum of activities that favour tumour development and progression. Here, we review similarities in structure and function of the NUAKs, their regulation at gene, transcript and protein level, and discuss their phosphorylation of specific downstream targets in the context of the signal transduction pathways and biological activities regulated by each or both NUAKs.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"295-307"},"PeriodicalIF":5.6,"publicationDate":"2024-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11576189/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141467005","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
AMPK and O-GlcNAcylation: interplay in cardiac pathologies and heart failure. AMPK 和 O-GlcNAcylation：心脏病变和心力衰竭中的相互作用。
IF 8.3 2区 生物学
Essays in biochemistry Pub Date : 2024-11-18 DOI: 10.1042/EBC20240003
Ettore Vanni, Christophe Beauloye, Sandrine Horman, Luc Bertrand
{"title":"AMPK and O-GlcNAcylation: interplay in cardiac pathologies and heart failure.","authors":"Ettore Vanni, Christophe Beauloye, Sandrine Horman, Luc Bertrand","doi":"10.1042/EBC20240003","DOIUrl":"10.1042/EBC20240003","url":null,"abstract":"<p><p>Heart failure (HF) represents a multifaceted clinical syndrome characterized by the heart's inability to pump blood efficiently to meet the body's metabolic demands. Despite advances in medical management, HF remains a major cause of morbidity and mortality worldwide. In recent years, considerable attention has been directed toward understanding the molecular mechanisms underlying HF pathogenesis, with a particular focus on the role of AMP-activated protein kinase (AMPK) and protein O-GlcNAcylation. This review comprehensively examines the current understanding of AMPK and O-GlcNAcylation signalling pathways in HF, emphasizing their interplay and dysregulation. We delve into the intricate molecular mechanisms by which AMPK and O-GlcNAcylation contribute to cardiac energetics, metabolism, and remodelling, highlighting recent preclinical and clinical studies that have explored novel therapeutic interventions targeting these pathways.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"363-377"},"PeriodicalIF":8.3,"publicationDate":"2024-11-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142343981","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Catalytic mechanism and kinetics of malate dehydrogenase. 苹果酸脱氢酶的催化机制和动力学。
IF 5.6 2区 生物学
Essays in biochemistry Pub Date : 2024-10-03 DOI: 10.1042/EBC20230086
Laura de Lorenzo, Tyler M M Stack, Kristin M Fox, Katherine M Walstrom
{"title":"Catalytic mechanism and kinetics of malate dehydrogenase.","authors":"Laura de Lorenzo, Tyler M M Stack, Kristin M Fox, Katherine M Walstrom","doi":"10.1042/EBC20230086","DOIUrl":"10.1042/EBC20230086","url":null,"abstract":"<p><p>Malate dehydrogenase (MDH) is a ubiquitous and central enzyme in cellular metabolism, found in all kingdoms of life, where it plays vital roles in the cytoplasm and various organelles. It catalyzes the reversible NAD+-dependent reduction of L-malate to oxaloacetate. This review describes the reaction mechanism for MDH and the effects of mutations in and around the active site on catalytic activity and substrate specificity, with a particular focus on the loop that encloses the active site after the substrates have bound. While MDH exhibits selectivity for its preferred substrates, mutations can alter the specificity of MDH for each cosubstrate. The kinetic characteristics and similarities of a variety of MDH isozymes are summarized, and they illustrate that the KM values are consistent with the relative concentrations of the substrates in cells. As a result of its existence in different cellular environments, MDH properties vary, making it an attractive model enzyme for studying enzyme activity and structure under different conditions.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"73-82"},"PeriodicalIF":5.6,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11461317/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140891441","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Malate dehydrogenase in parasitic protozoans: roles in metabolism and potential therapeutic applications. 寄生原生动物中的苹果酸脱氢酶：在新陈代谢中的作用和潜在的治疗应用。
IF 5.6 2区 生物学
Essays in biochemistry Pub Date : 2024-10-03 DOI: 10.1042/EBC20230075
Amy L Springer, Swati Agrawal, Eric P Chang
{"title":"Malate dehydrogenase in parasitic protozoans: roles in metabolism and potential therapeutic applications.","authors":"Amy L Springer, Swati Agrawal, Eric P Chang","doi":"10.1042/EBC20230075","DOIUrl":"10.1042/EBC20230075","url":null,"abstract":"<p><p>The role of malate dehydrogenase (MDH) in the metabolism of various medically significant protozoan parasites is reviewed. MDH is an NADH-dependent oxidoreductase that catalyzes interconversion between oxaloacetate and malate, provides metabolic intermediates for both catabolic and anabolic pathways, and can contribute to NAD+/NADH balance in multiple cellular compartments. MDH is present in nearly all organisms; isoforms of MDH from apicomplexans (Plasmodium falciparum, Toxoplasma gondii, Cryptosporidium spp.), trypanosomatids (Trypanosoma brucei, T. cruzi) and anaerobic protozoans (Trichomonas vaginalis, Giardia duodenalis) are presented here. Many parasitic species have complex life cycles and depend on the environment of their hosts for carbon sources and other nutrients. Metabolic plasticity is crucial to parasite transition between host environments; thus, the regulation of metabolic processes is an important area to explore for therapeutic intervention. Common themes in protozoan parasite metabolism include emphasis on glycolytic catabolism, substrate-level phosphorylation, non-traditional uses of common pathways like tricarboxylic acid cycle and adapted or reduced mitochondria-like organelles. We describe the roles of MDH isoforms in these pathways, discuss unusual structural or functional features of these isoforms relevant to activity or drug targeting, and review current studies exploring the therapeutic potential of MDH and related genes. These studies show that MDH activity has important roles in many metabolic pathways, and thus in the metabolic transitions of protozoan parasites needed for success as pathogens.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"235-251"},"PeriodicalIF":5.6,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11461325/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141467004","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Phosphorylation of mammalian cytosolic and mitochondrial malate dehydrogenase: insights into regulation. 哺乳动物细胞质和线粒体苹果酸脱氢酶的磷酸化：对调控的见解。
IF 5.6 2区 生物学
Essays in biochemistry Pub Date : 2024-10-03 DOI: 10.1042/EBC20230079
Joseph J Provost, Kathleen A Cornely, Pamela S Mertz, Celeste N Peterson, Sophie G Riley, Harrison J Tarbox, Shree R Narasimhan, Andrew J Pulido, Amy L Springer
{"title":"Phosphorylation of mammalian cytosolic and mitochondrial malate dehydrogenase: insights into regulation.","authors":"Joseph J Provost, Kathleen A Cornely, Pamela S Mertz, Celeste N Peterson, Sophie G Riley, Harrison J Tarbox, Shree R Narasimhan, Andrew J Pulido, Amy L Springer","doi":"10.1042/EBC20230079","DOIUrl":"10.1042/EBC20230079","url":null,"abstract":"<p><p>Malate dehydrogenase (MDH) is a key enzyme in mammalian metabolic pathways in cytosolic and mitochondrial compartments. Regulation of MDH through phosphorylation remains an underexplored area. In this review we consolidate evidence supporting the potential role of phosphorylation in modulating the function of mammalian MDH. Parallels are drawn with the phosphorylation of lactate dehydrogenase, a homologous enzyme, to reveal its regulatory significance and to suggest a similar regulatory strategy for MDH. Comprehensive mining of phosphorylation databases, provides substantial experimental (primarily mass spectrometry) evidence of MDH phosphorylation in mammalian cells. Experimentally identified phosphorylation sites are overlaid with MDH's functional domains, offering perspective on how these modifications could influence enzyme activity. Preliminary results are presented from phosphomimetic mutations (serine/threonine residues changed to aspartate) generated in recombinant MDH proteins serving as a proof of concept for the regulatory impact of phosphorylation. We also examine and highlight several approaches to probe the structural and cellular impact of phosphorylation. This review highlights the need to explore the dynamic nature of MDH phosphorylation and calls for identifying the responsible kinases and the physiological conditions underpinning this modification. The synthesis of current evidence and experimental data aims to provide insights for future research on understanding MDH regulation, offering new avenues for therapeutic interventions in metabolic disorders and cancer.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"183-198"},"PeriodicalIF":5.6,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141305726","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Malate dehydrogenase in plants: evolution, structure, and a myriad of functions. 植物中的苹果酸脱氢酶：进化、结构和多种功能。
IF 5.6 2区 生物学
Essays in biochemistry Pub Date : 2024-10-03 DOI: 10.1042/EBC20230089
Lisa M Baird, Christopher E Berndsen, Jonathan D Monroe
{"title":"Malate dehydrogenase in plants: evolution, structure, and a myriad of functions.","authors":"Lisa M Baird, Christopher E Berndsen, Jonathan D Monroe","doi":"10.1042/EBC20230089","DOIUrl":"10.1042/EBC20230089","url":null,"abstract":"<p><p>Malate dehydrogenase (MDH) catalyzes the interconversion of oxaloacetate and malate coupled to the oxidation/reduction of coenzymes NAD(P)H/NAD(P)+. While most animals have two isoforms of MDH located in the cytosol and mitochondria, all major groups of land plants have at least six MDHs localized to the cytosol, mitochondria, plastids, and peroxisomes. This family of enzymes participates in important reactions in plant cells including photosynthesis, photorespiration, lipid metabolism, and NH4+ metabolism. MDH also helps to regulate the energy balance in the cell and may help the plant cope with various environmental stresses. Despite their functional diversity, all of the plant MDH enzymes share a similar structural fold and act as dimers. In this review, we will introduce readers to our current understanding of the plant MDHs, including their evolution, structure, and function. The focus will be on the MDH enzymes of the model plant Arabidopsis thaliana.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"221-233"},"PeriodicalIF":5.6,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141310385","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Genetics of MDH in humans. 人类 MDH 遗传学。
IF 5.6 2区 生物学
Essays in biochemistry Pub Date : 2024-10-03 DOI: 10.1042/EBC20230078
Adam Haberman, Celeste N Peterson
{"title":"Genetics of MDH in humans.","authors":"Adam Haberman, Celeste N Peterson","doi":"10.1042/EBC20230078","DOIUrl":"10.1042/EBC20230078","url":null,"abstract":"<p><p>Malate dehydrogenase (MDH) performs key roles in metabolism, but little is known about its function specifically in human health and disease. In this minireview, we describe the incomplete state of our knowledge of human MDH genetics. Humans have three MDH genes with a total of four validated isoforms. MDH1 and MDH2 are widely expressed, while MDH1B is only expressed in a small subset of tissues. Many mutations in MDH1 and MDH2 have been identified in patients, but only a few have been studied to determine what symptoms they cause. MDH1 has been associated with cancer and a neurodevelopmental disorder. MDH2 has been associated with diabetes, neurodevelopmental disorders, and cancer.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"107-119"},"PeriodicalIF":5.6,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141733832","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Malate dehydrogenase (MDH) in cancer: a promiscuous enzyme, a redox regulator, and a metabolic co-conspirator. 癌症中的苹果酸脱氢酶（MDH）：一种杂合酶、氧化还原调节器和代谢共谋者。
IF 5.6 2区 生物学
Essays in biochemistry Pub Date : 2024-10-03 DOI: 10.1042/EBC20230088
Betsy Leverett, Shane Austin, Jason Tan-Arroyo
{"title":"Malate dehydrogenase (MDH) in cancer: a promiscuous enzyme, a redox regulator, and a metabolic co-conspirator.","authors":"Betsy Leverett, Shane Austin, Jason Tan-Arroyo","doi":"10.1042/EBC20230088","DOIUrl":"10.1042/EBC20230088","url":null,"abstract":"<p><p>Malate dehydrogenase (MDH) is an essential enzyme in the tricarboxylic acid cycle that functions in cellular respiration and redox homeostasis. Recent studies indicate that MDH facilitates metabolic plasticity in tumor cells, catalyzing the formation of an oncometabolite, contributing to altered epigenetics, and maintaining redox capacity to support the rewired energy metabolism and biosynthesis that enables cancer progression. This minireview summarizes current findings on the unique supporting roles played by MDH in human cancers and provides an update on targeting MDH in cancer chemotherapy.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"135-146"},"PeriodicalIF":5.6,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141305725","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Acetylation, ADP-ribosylation and methylation of malate dehydrogenase. 苹果酸脱氢酶的乙酰化、ADP-核糖基化和甲基化。
IF 5.6 2区 生物学
Essays in biochemistry Pub Date : 2024-10-03 DOI: 10.1042/EBC20230080
Misty L Kuhn, John F Rakus, Delphine Quenet
{"title":"Acetylation, ADP-ribosylation and methylation of malate dehydrogenase.","authors":"Misty L Kuhn, John F Rakus, Delphine Quenet","doi":"10.1042/EBC20230080","DOIUrl":"10.1042/EBC20230080","url":null,"abstract":"<p><p>Metabolism within an organism is regulated by various processes, including post-translational modifications (PTMs). These types of chemical modifications alter the molecular, biochemical, and cellular properties of proteins and allow the organism to respond quickly to different environments, energy states, and stresses. Malate dehydrogenase (MDH) is a metabolic enzyme that is conserved in all domains of life and is extensively modified post-translationally. Due to the central role of MDH, its modification can alter metabolic flux, including the Krebs cycle, glycolysis, and lipid and amino acid metabolism. Despite the importance of both MDH and its extensively post-translationally modified landscape, comprehensive characterization of MDH PTMs, and their effects on MDH structure, function, and metabolic flux remains underexplored. Here, we review three types of MDH PTMs - acetylation, ADP-ribosylation, and methylation - and explore what is known in the literature and how these PTMs potentially affect the 3D structure, enzymatic activity, and interactome of MDH. Finally, we briefly discuss the potential involvement of PTMs in the dynamics of metabolons that include MDH.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"199-212"},"PeriodicalIF":5.6,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11451102/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141589986","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Exploring the uncharted territory of the potential protein-protein interactions of cytosolic malate dehydrogenase. 探索细胞膜苹果酸脱氢酶潜在蛋白质间相互作用的未知领域。
IF 5.6 2区 生物学
Essays in biochemistry Pub Date : 2024-10-03 DOI: 10.1042/EBC20230083
Joseph J Provost, Amy D Parente, Kristin M Slade, Thomas J Wiese
{"title":"Exploring the uncharted territory of the potential protein-protein interactions of cytosolic malate dehydrogenase.","authors":"Joseph J Provost, Amy D Parente, Kristin M Slade, Thomas J Wiese","doi":"10.1042/EBC20230083","DOIUrl":"10.1042/EBC20230083","url":null,"abstract":"<p><p>In this review, we examine the protein-protein interactions of cytosolic malate dehydrogenase (MDH), an under-studied area in cellular metabolism. We provide a comprehensive overview of MDH involvement in metabolism, especially its interactions with metabolic partners and dynamics of changing metabolism. We present an analysis of the biophysical nature of these interactions and the current methods used to study them. Our review includes an assessment of computational docking studies, which offer initial hypotheses about potential MDH interaction partners. Furthermore, we provide a summary of the sparse yet insightful experimental evidence available, establishing a foundation for future research. By integrating biophysical analysis and methodological advancements, this paper aims to illuminate the intricate network of interactions involving cytosolic MDH and their metabolic implications. This work not only contributes to our understanding of MDH's role in metabolism but also highlights the potential impact of these interactions in metabolic disorders.</p>","PeriodicalId":11812,"journal":{"name":"Essays in biochemistry","volume":" ","pages":"83-97"},"PeriodicalIF":5.6,"publicationDate":"2024-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141310384","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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