High impact information on Snapap

• A novel role for snapin in dendrite patterning: interaction with cypin [1].
• EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin [2].
• We also show that snapin competes with tubulin for binding to cypin, resulting in decreased microtubule assembly [1].
• Using a yeast two-hybrid screen of a rat brain cDNA library with cypin lacking the carboxyl terminal eight amino acids as bait, we identified snapin as a cypin binding partner [1].
• The conjunction between EBAG9 and Snapin adds an additional layer of control on exocytosis processes; in addition, mechanistic evidence is provided that inhibition of phosphorylation has a regulatory function in exocytosis [2].

Biological context of Snapap

• Moreover, snapin is regulated by phosphorylation and enhances synaptotagmin binding to SNAREs [3].

Anatomical context of Snapap

• Snapin is ubiquitously expressed at low levels with no detectable enrichment in the brain or in synaptic vesicles [3].
• Furthermore, snapin and C-terminal snapin fragments have been effective in changing the release properties of neurons and chromaffin cells [3].

Other interactions of Snapap

• Snapin, a 15-kDa protein, has been identified recently as a binding partner of SNAP-25 [3].

Analytical, diagnostic and therapeutic context of Snapap

• Using non-equilibrium and equilibrium assays including pulldown experiments, co-immunoprecipitations, and CD and fluorescence anisotropy spectroscopy, we were unable to detect any specific interaction between snapin and SNAP-25 [3].
• Here, we show by affinity chromatography and coimmunoprecipitation that the carboxyl-terminal coiled-coil domain (H2) of snapin is required for cypin binding [1].

References