Title : RhoA inactivation by S-nitrosylation regulates vascular smooth muscle contractive signaling.

Pub. Date : 2018 Apr 1

PMID : 29355776






5 Functional Relationships(s)
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1 Since small G protein RhoA contains cysteine residues in the GTP-binding domain which is critical for its function, modification these thiols may alter RhoA activity and lead to changes in the downstream signaling such as myosin light chain phosphorylation. Guanosine Triphosphate ras homolog family member A Homo sapiens
2 Since small G protein RhoA contains cysteine residues in the GTP-binding domain which is critical for its function, modification these thiols may alter RhoA activity and lead to changes in the downstream signaling such as myosin light chain phosphorylation. Guanosine Triphosphate ras homolog family member A Homo sapiens
3 In this study we show that S-nitroso-L-cysteine (CSNO) blocked RhoA activation as determined by either GDP/GTP exchange, active RhoA binding to rhotekin or RhoA translocation. Guanosine Triphosphate ras homolog family member A Homo sapiens
4 Together, these data suggest that S-nitrosothiols regulate myosin light chain phosphorylation by inhibiting RhoA/Rho-kinase signaling through modification of RhoA cysteine residues at 16 and 20 in its GTP-binding domain, which might be an important therapeutic target for diseases with imbalanced vascular resistance. Guanosine Triphosphate ras homolog family member A Homo sapiens
5 Together, these data suggest that S-nitrosothiols regulate myosin light chain phosphorylation by inhibiting RhoA/Rho-kinase signaling through modification of RhoA cysteine residues at 16 and 20 in its GTP-binding domain, which might be an important therapeutic target for diseases with imbalanced vascular resistance. Guanosine Triphosphate ras homolog family member A Homo sapiens