New roles for GAPDH, Hsp90, and NO in regulating heme allocation and hemeprotein function in mammals. Biol Chem 2022 Nov 25;403(11-12):1005-1015
Date
09/25/2022Pubmed ID
36152339Pubmed Central ID
PMC10184026DOI
10.1515/hsz-2022-0197Scopus ID
2-s2.0-85139392791 (requires institutional sign-in at Scopus site) 9 CitationsAbstract
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.
Author List
Stuehr DJ, Dai Y, Biswas P, Sweeny EA, Ghosh AAuthor
Elizabeth Sweeny PhD Assistant Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsGlyceraldehyde-3-Phosphate Dehydrogenases
HSP90 Heat-Shock Proteins
Heme
Hemeproteins
Mammals
Nitric Oxide
