NO rapidly mobilizes cellular heme to trigger assembly of its own receptor | Zendy

Yue Dai | Zendy; Emily Faul | Zendy; Arnab Ghosh | Zendy; Dennis J. Stuehr | Zendy

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NO 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

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 , nitric oxide , microbiology and biotechnology , function (biology) , guanylate cyclase , cell signaling , receptor , chemistry , signal transduction , biochemistry , biology , computational biology , enzyme , organic chemistry

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.

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