Nitric oxide and heat shock protein 90 activate soluble guanylate cyclase by driving rapid change in its subunit interactions and heme content

Arnab Ghosh, Johannes Peter Stasch, Andreas Papapetropoulos, Dennis J. Stuehr

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

Background: Heme insertion into souble guanylate cyclase (sGC) enables it to bind nitric oxide (NO) for cell signaling. Results: NO triggered a rapid, reversible, and hsp90-dependent heme insertion into sGC-β1 and an association with sGC-α1 subunit. sGC activator BAY 60-2770 did the same. Conclusion: NO dynamically impacts the maturation and stability of active sGC heterodimer. Significance: The data uncover new mechanisms that regulate cellular NO signaling cascades.

Original languageEnglish (US)
Pages (from-to)15259-15271
Number of pages13
JournalJournal of Biological Chemistry
Volume289
Issue number22
DOIs
StatePublished - May 30 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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