Dennis J. Stuehr , Pranjal Biswas , Yue Dai , Dhanya Thamaraparambil Jayaram , Priya Das Sinha , Elizabeth A. Sweeny , Arnab Ghosh
{"title":"Key roles of GAPDH, Hsp90, and NO in heme trafficking","authors":"Dennis J. Stuehr , Pranjal Biswas , Yue Dai , Dhanya Thamaraparambil Jayaram , Priya Das Sinha , Elizabeth A. Sweeny , Arnab Ghosh","doi":"10.1016/j.jinorgbio.2025.113066","DOIUrl":null,"url":null,"abstract":"<div><div>Intracellular trafficking of mitochondrial heme to create functional heme proteins presents a fundamental challenge in animal cells. This article provides some background on heme allocation, discusses some of the concepts, and then reviews research from the last two decades that has uncovered unexpected and important roles for glyceraldehyde 3-phosphate dehydrogenase (GAPDH), heat shock protein 90 (Hsp90), and nitric oxide (NO) in enabling and regulating cell heme allocations to hemeproteins that mature and function outside of the mitochondria. A model for how hemeprotein heme contents and functions in cells can be regulated through the coordinate participation of GAPDH, Hsp90, and NO is presented.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"274 ","pages":"Article 113066"},"PeriodicalIF":3.2000,"publicationDate":"2025-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Inorganic Biochemistry","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0162013425002466","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Intracellular trafficking of mitochondrial heme to create functional heme proteins presents a fundamental challenge in animal cells. This article provides some background on heme allocation, discusses some of the concepts, and then reviews research from the last two decades that has uncovered unexpected and important roles for glyceraldehyde 3-phosphate dehydrogenase (GAPDH), heat shock protein 90 (Hsp90), and nitric oxide (NO) in enabling and regulating cell heme allocations to hemeproteins that mature and function outside of the mitochondria. A model for how hemeprotein heme contents and functions in cells can be regulated through the coordinate participation of GAPDH, Hsp90, and NO is presented.
期刊介绍:
The Journal of Inorganic Biochemistry is an established international forum for research in all aspects of Biological Inorganic Chemistry. Original papers of a high scientific level are published in the form of Articles (full length papers), Short Communications, Focused Reviews and Bioinorganic Methods. Topics include: the chemistry, structure and function of metalloenzymes; the interaction of inorganic ions and molecules with proteins and nucleic acids; the synthesis and properties of coordination complexes of biological interest including both structural and functional model systems; the function of metal- containing systems in the regulation of gene expression; the role of metals in medicine; the application of spectroscopic methods to determine the structure of metallobiomolecules; the preparation and characterization of metal-based biomaterials; and related systems. The emphasis of the Journal is on the structure and mechanism of action of metallobiomolecules.