Álvarez, Yanina D.Belingheri, Ana VerónicaPerez Bay, Andrés E.Javis, Scott E.Tedford, Hugo WilliamZamponi, Gerald W.Marengo, Fernando D.2018-05-292018-05-292013-01-30Álvarez, Y. D., Belingheri, A. V., Perez Bay, A. E., Javis, S. E., Tedford, H. W., Zamponi, G., & Marengo, F. D. (2013). The Immediately Releasable Pool of Mouse Chromaffin Cell Vesicles Is Coupled to P/Q-Type Calcium Channels via the Synaptic Protein Interaction Site. PLoS ONE, 8(1). https://doi.org/10.1371/journal.pone.0054846http://hdl.handle.net/1880/106705https://doi.org/10.11575/PRISM/43734It is generally accepted that the immediately releasable pool is a group of readily releasable vesicles that are closely associated with voltage dependent Ca(2+) channels. We have previously shown that exocytosis of this pool is specifically coupled to P/Q Ca(2+) current. Accordingly, in the present work we found that the Ca(2+) current flowing through P/Q-type Ca(2+) channels is 8 times more effective at inducing exocytosis in response to short stimuli than the current carried by L-type channels. To investigate the mechanism that underlies the coupling between the immediately releasable pool and P/Q-type channels we transiently expressed in mouse chromaffin cells peptides corresponding to the synaptic protein interaction site of Cav2.2 to competitively uncouple P/Q-type channels from the secretory vesicle release complex. This treatment reduced the efficiency of Ca(2+) current to induce exocytosis to similar values as direct inhibition of P/Q-type channels via ω-agatoxin-IVA. In addition, the same treatment markedly reduced immediately releasable pool exocytosis, but did not affect the exocytosis provoked by sustained electric or high K(+) stimulation. Together, our results indicate that the synaptic protein interaction site is a crucial factor for the establishment of the functional coupling between immediately releasable pool vesicles and P/Q-type Ca(2+) channels.enThe immediately releasable pool of mouse chromaffin cell vesicles is coupled to P/Q-type calcium channels via the synaptic protein interaction sitejournal articlehttp://dx.doi.org/10.1371/journal.pone.0054846