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Tyrosine-kinase-dependent recruitment of RGS12 to the N-type calcium channel
- Source :
- Nature. 408:723-727
- Publication Year :
- 2000
- Publisher :
- Springer Science and Business Media LLC, 2000.
-
Abstract
- Gamma-aminobutyric acid (GABA)B receptors couple to Go to inhibit N-type calcium channels in embryonic chick dorsal root ganglion neurons. The voltage-independent inhibition, mediated by means of a tyrosine-kinase pathway, is transient and lasts up to 100 seconds. Inhibition of endogenous RGS12, a member of the family of regulators of G-protein signalling, selectively alters the time course of voltage-independent inhibition. The RGS12 protein, in addition to the RGS domain, contains PDZ and PTB domains. Fusion proteins containing the PTB domain of RGS12 alter the rate of termination of the GABA(B) signal, whereas the PDZ or RGS domains of RGS 12 have no observable effects. Using primary dorsal root ganglion neurons in culture, here we show an endogenous agonist-induced tyrosine-kinase-dependent complex of RGS12 and the calcium channel. These results indicate that RGS12 is a multifunctional protein capable of direct interactions through its PTB domain with the tyrosine-phosphorylated calcium channel. Recruitment of RGS proteins to G-protein effectors may represent an additional mechanism for signal termination in G-protein-coupled pathways.
- Subjects :
- G protein
Recombinant Fusion Proteins
Molecular Sequence Data
PDZ domain
Chick Embryo
N-type calcium channel
Biology
Calcium Channels, N-Type
Dorsal root ganglion
Ganglia, Spinal
medicine
Animals
Humans
Phosphorylation
Cells, Cultured
Neurons
Multidisciplinary
Voltage-dependent calcium channel
Calcium channel
Protein-Tyrosine Kinases
Protein Structure, Tertiary
Rats
Cell biology
medicine.anatomical_structure
Receptors, GABA-B
Biochemistry
Calcium
Phosphotyrosine-binding domain
RGS Proteins
Signal Transduction
Subjects
Details
- ISSN :
- 14764687 and 00280836
- Volume :
- 408
- Database :
- OpenAIRE
- Journal :
- Nature
- Accession number :
- edsair.doi.dedup.....f088b73cc991c8f28f47b6cc5b01d05a