NDLI: $Ca^{2+}-dependent$ and -independent interactions of the isoforms of the $α_{1A}$ subunit of brain $Ca^{2+}$ channels with presynaptic SNARE proteins

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$Ca^{2+}-dependent$ and -independent interactions of the isoforms of the $α_{1A}$ subunit of brain $Ca^{2+}$ channels with presynaptic SNARE proteins

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$Ca^{2+}-dependent$ and -independent interactions of the isoforms of the $α_{1A}$ subunit of brain $Ca^{2+}$ channels with presynaptic SNARE proteins

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kim, D. K. Catterall, W. A.
Description	Author Affiliation: Kim DK ( Department of Pharmacology, University of Washington, Seattle, WA 98195, USA.);
Abstract	Fast neurotransmission requires that docked synaptic vesicles be located near the presynaptic N-type or P/Q-type calcium channels. Specific protein-protein interactions between a synaptic protein interaction (synprint) site on N-type and P/Q-type channels and the presynaptic SNARE proteins syntaxin, SNAP-25, and synaptotagmin are required for efficient, synchronous neurotransmitter release. Interaction of the synprint site of N-type calcium channels with syntaxin and SNAP-25 has a biphasic calcium dependence with maximal binding at 10-20 microM. We report here that the synprint sites of the BI and rbA isoforms of the alpha1A subunit of P/Q-type Ca2+ channels have different patterns of interactions with synaptic proteins. The BI isoform of alpha1A specifically interacts with syntaxin, SNAP-25, and synaptotagmin independent of Ca2+ concentration and binds with high affinity to the C2B domain of synaptotagmin but not the C2A domain. The rbA isoform of alpha1A interacts specifically with synaptotagmin and SNAP-25 but not with syntaxin. Binding of synaptotagmin to the rbA isoform of alpha1A is Ca2+-dependent, with maximum affinity at 10-20 microM Ca2+. Although the rbA isoform of alpha1A binds well to both the C2A and C2B domains of synaptotagmin, only the interaction with the C2A domain is Ca2+-dependent. These differential, Ca2+-dependent interactions of Ca2+ channel synprint sites with SNARE proteins may modulate the efficiency of transmitter release triggered by Ca2+ influx through these channels.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	26
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Brain Metabolism Calcium Channels Calcium-Binding Proteins Calcium Membrane Glycoproteins Membrane Proteins Nerve Tissue Proteins Animals Escherichia Coli Presynaptic Terminals Qa-SNARE Proteins Synaptosomal-Associated Protein 25 Synaptotagmins Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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