Cysteine String Protein Regulates G Protein Modulation of N-Type Calcium Channels
| Autor: | Scott E. Jarvis, Michelle I. Arnot, Gerald W. Zamponi, Johanna Magga, Janice E. A. Braun |
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| Rok vydání: | 2000 |
| Předmět: |
Models
Molecular Patch-Clamp Techniques animal structures GTPase-activating protein G protein Neuroscience(all) Immunoblotting In Vitro Techniques Neurotransmission Hippocampus complex mixtures Cell Line Potassium Chloride Adenosine Triphosphate Calcium Channels N-Type GTP-binding protein regulators GTP-Binding Proteins Heterotrimeric G protein parasitic diseases Animals Humans Ion Transport Voltage-dependent calcium channel Chemistry General Neuroscience C-terminus fungi Membrane Proteins HSP40 Heat-Shock Proteins Calcium Channel Blockers Secretory Vesicle Rats Protein Subunits Cross-Linking Reagents Biochemistry Biophysics Protein Binding |
| Zdroj: | Neuron. 28:195-204 |
| ISSN: | 0896-6273 |
| DOI: | 10.1016/s0896-6273(00)00096-9 |
| Popis: | Cysteine string proteins (CSPs) are secretory vesicle proteins bearing a "J domain" and a palmitoylated cysteine-rich "string" region that are critical for neurotransmitter release. The precise role of CSP in neurotransmission is controversial. Here, we demonstrate a novel interaction between CSP, receptor-coupled trimeric GTP binding proteins (G proteins), and N-type Ca 2+ channels. G α subunits interact with the J domain of CSP in an ATP-dependent manner; in contrast, G βγ subunits interact with the C terminus of CSP in both the presence and absence of ATP. The interaction of CSP with both G proteins and N-type Ca 2+ channels results in a tonic G protein inhibition of the channels. In view of the crucial importance of N-type Ca 2+ channels in presynaptic vesicle release, our data attribute a key role to CSP in the fine tuning of neurotransmission. |
| Databáze: | OpenAIRE |
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