Key roles of GAPDH, Hsp90, and NO in heme trafficking. J Inorg Biochem 2026 Jan;274:113066
Date
09/18/2025Pubmed ID
40961740Pubmed Central ID
PMC13292358DOI
10.1016/j.jinorgbio.2025.113066Scopus ID
2-s2.0-105015835663 (requires institutional sign-in at Scopus site) 1 CitationAbstract
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.
Author List
Stuehr DJ, Biswas P, Dai Y, Jayaram DT, Sinha PD, 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
Humans
Mitochondria
Nitric Oxide
Protein Transport
