TY - JOUR
T1 - Nitric oxide and heat shock protein 90 activate soluble guanylate cyclase by driving rapid change in its subunit interactions and heme content
AU - Ghosh, Arnab
AU - Stasch, Johannes Peter
AU - Papapetropoulos, Andreas
AU - Stuehr, Dennis J.
PY - 2014/5/30
Y1 - 2014/5/30
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M114.559393
DO - 10.1074/jbc.M114.559393
M3 - Article
C2 - 24733395
AN - SCOPUS:84901717696
SN - 0021-9258
VL - 289
SP - 15259
EP - 15271
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 22
ER -