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New roles for GAPDH, Hsp90, and NO in regulating heme allocation and hemeprotein function in mammals

Dennis J. Stuehr, Yue Dai, Pranjal Biswas, Elizabeth A. Sweeny, Arnab Ghosh

2022Biological Chemistry24 citationsDOIOpen Access PDF

Abstract

The intracellular trafficking of mitochondrial heme presents a fundamental challenge to animal cells. This article provides some background on heme allocation, discusses some of the concepts, and then reviews research done over the last decade, much in the author's laboratory, that is uncovering unexpected and important roles for glyceraldehyde 3-phosphate dehydrogenase (GAPDH), heat shock protein 90 (hsp90), and nitric oxide (NO) in enabling and regulating the allocation of mitochondrial heme to hemeproteins that mature and function outside of the mitochondria. A model for how hemeprotein functions can be regulated in cells through the coordinate participation of GAPDH, hsp90, and NO in allocating cellular heme is presented.

Topics & Concepts

HemeHemeproteinFunction (biology)ChemistryGlyceraldehyde 3-phosphate dehydrogenaseBiochemistryCell biologyHsp90BiologyEnzymeDehydrogenaseHeat shock proteinGeneHeme Oxygenase-1 and Carbon MonoxideHigh Altitude and HypoxiaAdipose Tissue and Metabolism
New roles for GAPDH, Hsp90, and NO in regulating heme allocation and hemeprotein function in mammals | Litcius