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Papers In Press, published online ahead of print August 19, 2004
J. Biol. Chem, 10.1074/jbc.M407206200
Submitted on June 28, 2004
Revised on August 19, 2004
Accepted on August 19, 2004

Regulation of type VI adenylyl cyclase by snapin, a SNAP25-binding protein

Jui-ling Chou, Chuen-Lin Huang, Hsing-Lin Lai, Amos C. Hung, Chen-Li Chien, Yu-Ya Kao, and Yijuang Chern

Division of Neuroscience, Academia Sinica, Taipei, Taipei 11529

Corresponding Author: bmychern{at}ibms.sinica.edu.tw

In the present study, we used the N terminus (amino acids 1~160) of type VI adenylyl cyclase (ACVI) as the bait to screen a mouse brain cDNA library and identified Snapin as a novel ACVI-interacting molecule. Snapin is a binding protein of SNAP25, a component of the SNARE complex. Co-immunoprecipitation analyses confirmed the interaction between Snapin and full-length ACVI. Mutational analysis revealed that the interaction domains of ACVI and Snapin were located within amino acids (aa) 1~86 of ACVI and aa 33-51 of Snapin, respectively. Co-localization of ACVI and Snapin was observed in primary hippocampal neurons. Moreover, expression of Snapin specifically eliminated PKC-mediated suppression of ACVI, but not that of PKA or calcium. Mutation of the potential PKC and PKA phosphorylation sites of Snapin did not affect Snapin’s ability to reverse PKC's inhibitory effect on ACVI. Phosphorylation of Snapin by PKC or PKA therefore might not be crucial for Snapin's action on ACVI. In contrast, Snapin33-51 which harbors an internal deletion of aa 33 to 51 did not affect PKC-mediated inhibition of ACVI, supporting that aa 33 to 51 of Snapin comprises the ACVI-interacting region. Consistently, Snapin exerted no effect on PKC-mediated inhibition of an ACVI mutant (ACVI-DA87) which lacked the Snapin-interacting region (aa 1- 86). Snapin thus reverses its action via direct interaction with the N-terminus of ACVI. Collectively, we demonstrate herein that in addition to its association with the SNARE complex, Snapin also functions as a regulator of an important cAMP synthesis enzyme in the brain.


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