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NOS3 — NOSIP

Pathways - manually collected, often from reviews:

• Reactome Reaction: NOS3 → NOSIP (reaction) Dedio et al., FASEB J 2001*
• Reactome Reaction: NOS3 → NOSIP (indirect_complex) Dedio et al., FASEB J 2001*, Zimmermann et al., Proc Natl Acad Sci U S A 2002*

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: NOS3 — NOSIP (direct interaction, two hybrid) Dedio et al., FASEB J 2001*
• IRef Biogrid Interaction: NOS3 — NOSIP (physical association, affinity chromatography technology) Schleicher et al., Mol Cell Biol 2005*
• IRef Biogrid Interaction: NOS3 — NOSIP (physical association, affinity chromatography technology) Dedio et al., FASEB J 2001*
• IRef Biogrid Interaction: NOS3 — NOSIP (direct interaction, pull down) Dedio et al., FASEB J 2001*
• IRef Hprd Interaction: NOS3 — NOSIP (in vivo) Dedio et al., FASEB J 2001*
• IRef Hprd Interaction: NOS3 — NOSIP (in vitro) Dedio et al., FASEB J 2001*
• IRef Hprd Interaction: NOS3 — NOSIP (two hybrid) Dedio et al., FASEB J 2001*

Text-mined interactions from Literome

Dedio et al., FASEB J 2001 : Stimulation with the calcium ionophore A23187 induced the reversible translocation of eNOS from the detergent-insoluble to the detergent-soluble fractions of CHO-eNOS, and this translocation was completely prevented by transient coexpression of NOSIP in CHO-eNOS ... Subcellular fractionation studies identified eNOS in the caveolin-rich membrane fractions of CHO-eNOS, and coexpression of NOSIP caused a shift of eNOS to intracellular compartments
König et al., J Histochem Cytochem 2005 : Endothelial nitric oxide synthase (eNOS) , the major nitric oxide ( NO ) -generating enzyme of the vasculature, is regulated through multiple interactions with proteins, including caveolin-1, Hsp90, Ca2+-calmodulin, and the recently discovered eNOS interacting protein, NOSIP ... Previous studies indicate that NOSIP may contribute to the intricate regulation of eNOS activity and availability
Schleicher et al., Mol Cell Biol 2005 : Here we report that endogenous NOSIP reduces the enzymatic capacity of eNOS , specifically in the G(2) phase of the cell cycle by targeting eNOS to the actin cytoskeleton