MAP kinases differentially bind and phosphorylate NOS3 via two unique NOS3 sites.

ABSTRACT: Nitric oxide synthase 3 (NOS3) is a major vasoprotective enzyme that catalyzes the conversion of l-arginine to nitric oxide (NO) in response to a significant number of signaling pathways. Here, we provide evidence that NOS3 interactions with MAP kinases have physiological relevance. Binding interactions of NOS3 with c-Jun N-terminal kinase (JNK1_α1 ), p38α, and ERK2 were characterized using optical biosensing with full-length NOS3 and NOS3 specific peptides and phosphopeptides. Like p38α and ERK2, JNK1_α1 exhibited high-affinity binding to full-length NOS3 (K_D 15 nm). Rate constants exhibited fast-on, slow-off binding (k_on  = 4106 m^-1 s^-1 ; k_off  = 6.2 × 10^-5  s^-1 ). Further analysis using synt

SUBMITTER: Solone XKV 

PROVIDER: S-EPMC9063426 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature