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Requirement for the Synaptic Protein Interaction Site for Reconstitution of Synaptic Transmission by P/Q-Type Calcium Channels

Sumiko Mochida, Ruth E. Westenbroek, Charles T. Yokoyama, Huijun Zhong, Scott J. Myers, Todd Scheuer, Kanako Itoh and William A. Catterall
Proceedings of the National Academy of Sciences of the United States of America
Vol. 100, No. 5 (Mar. 4, 2003), pp. 2819-2824
Stable URL: http://www.jstor.org/stable/3139611
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Requirement for the Synaptic Protein Interaction Site for Reconstitution of Synaptic Transmission by P/Q-Type Calcium Channels
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Abstract

Cav2.1 channels, which conduct P/Q-type Ca2+ currents, were expressed in superior cervical ganglion neurons in cell culture, and neurotransmission initiated by these exogenously expressed Ca2+ channels was measured. Deletions in the synaptic protein interaction (synprint) site in the intracellular loop between domains II and III of Cav2.1 channels reduced their effectiveness in synaptic transmission. Surprisingly, this effect was correlated with loss of presynaptic localization of the exogenously expressed channels. Cav1.2 channels, which conduct L-type Ca2+ currents, are ineffective in supporting synaptic transmission, but substitution of the synprint site from Cav2.1 channels in Cav1.2 was sufficient to establish synaptic transmission initiated by L-type Ca2+ currents through the exogenous Cav1.2 channels. Substitution of the synprint site from Cav2.2 channels, which conduct N-type Ca2+ currents, was even more effective than Cav2.1. Our results show that localization and function of exogenous Ca2+ channels in nerve terminals of superior cervical ganglion neurons require a functional synprint site and suggest that binding of soluble NSF attachment protein receptor (SNARE) proteins to the synprint site is a necessary permissive event for nerve terminal localization of presynaptic Ca2+ channels.

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