Open AccessNO rapidly mobilizes cellular heme to trigger assembly of its own receptor
Author(s) -
Yue Dai,
Emily Faul,
Arnab Ghosh,
Dennis J. Stuehr
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2115774119
Subject(s) - heme , hemeprotein , cofactor , intracellular , microbiology and biotechnology , function (biology) , nitric oxide , biochemistry , cell signaling , biology , receptor , signal transduction , soluble guanylyl cyclase , guanylate cyclase , chemistry , enzyme , endocrinology
Significance Nitric oxide (NO) performs many biological functions, but how it operates at the molecular and cellular levels is not fully understood. We discovered that cell NO generation at physiologic levels triggers a rapid redeployment of intracellular heme, an iron-containing cofactor, and we show that this drives the assembly of the natural NO receptor protein, soluble guanylyl cyclase, which is needed for NO to perform its biological signaling functions. Our study uncovers a way that NO can shape biological signaling processes and a way that cells may use NO to control their hemeprotein activities through deployment of the heme cofactor. These concepts broaden our understanding of NO function in biology and medicine.