Nitric oxide (NO) is a potent mediator in biologic processes such as neurotransmission, inflammatory response, and vascular homeostasis. NOSTRIN binds the enzyme responsible for NO production, endothelial NO synthase (ENOS), and triggers the translocation of ENOS from the plasma membrane to vesicle-like subcellular structures, thereby attenuating ENOS-dependent NO production.

NOSTRIN overexpression induced a redistribution of ENOS from the plasma membrane to vesicle-like structures matching the NOSTRIN localization pattern and, at the same time, led to significant inhibition of NO release. Deletion of the CDC15 domain of NOSTRIN disrupted the subcellular distribution of both NOSTRIN and ENOS in these cells.