G‐protein regulator LGN inhibits the activity of nitric oxide receptor soluble guanylyl cyclase

Soluble guanylyl cyclase Immunoprecipitation
DOI: 10.1096/fasebj.25.1_supplement.958.1 Publication Date: 2021-06-21T16:01:04Z
ABSTRACT
Soluble guanylyl cyclase (sGC) is a heme‐containing enzyme which converts GTP to cGMP. SGC referred as nitric oxide (NO) receptor, it strongly stimulated by NO. Although the mechanism of sGC activation NO received lot attention, processes deactivation are less understood. In this report we demonstrate inhibition LGN‐dependent mechanism. LGN known regulator Gα proteins. We identified protein interacting with both α1 and β1 subunits yeast two‐hybrid screening co‐immunoprecipitation from BE2 human neuroblastoma cell line. Transient expression in MDA468 breast cancer cells markedly decreased activity gene‐dose dependent fashion. When effect purified on was tested vitro, found no evidence inhibition, suggesting that does not directly affect function. However, when same experiment performed lysate COS7 cell, observed marked sGC. These data suggest may function an adaptor for additional cellular factors inhibiting Since regulate G‐proteins association subunit, complex consisting sGC, Gα, thus connecting NO‐dependent G‐protein signaling pathways.
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