The exocytosis of salivary proteins is mainly regulated by cAMP, although soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), which mediate cAMP-dependent exocytic membrane fusion, have remained unidentified. Here we examined the effect of isoproterenol (ISO) and cytochalasin D (CyD) on the level of SNARE complexes in rat parotid glands. When SNARE complexes were immunoprecipitated by anti-SNAP23, the coprecipitation of VAMP2 was significantly increased in response to ISO and/or CyD, although the coprecipitation of VAMP8 or syntaxin 4 was scarcely augmented. These results suggest that the SNAP23-VAMP2 interaction plays a key role in cAMP-mediated exocytosis from parotid glands. Structured summary of protein interactions: Snap23 physically interacts with Vamp8, Vamp3 and Syn-4 by anti bait coimmunoprecipitation (View Interaction: 1, 2, 3) Vamp2 physically interacts with Syn-4, Syn-3 and Snap23 by anti bait coimmunoprecipitation (View interaction) Syn-3 physically interacts with Snap23 by anti bait coimmunoprecipitation (View interaction) Vamp2 physically interacts with Snap23 and Syn-4 by anti bait coimmunoprecipitation (View interaction) Snap23 physically interacts with Vamp8, Syn-4 and Vamp2 by anti bait coimmunoprecipitation (View interaction: 1, 2).
- Cytochalasin D
- Parotid gland
- Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)