Abstract
We found that a scaffold protein, spinophilin (SPL), can interact with M2 and M3-muscarinic acetylcholine receptors (mAChRs). As SPL can also bind to RGS8 by using the different region of SPL, we investigated the effects of SPL on the function of RGS8 regulating signals from M2 and M3 receptors. M2 receptor-mediated Gi-signaling was studied by monitoring G-protein-coupled inwardly rectifying K+ channels, and M3 receptor-mediated Gq-signaling was monitored by the increase of Ca2+-activated Cl(-) current. The expression of SPL could enhance the regulatory function of RGS8 on the M3-mAChR, but the acceleration function of RGS8 on the M2-mediated signaling could not be enhanced by SPL. Results showed that the recruitment of RGS8 to the receptor differentially affects the function of RGS8 among receptors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Calcium / metabolism
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Cell Line
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Cell Membrane / metabolism
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Chlorides / metabolism
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G Protein-Coupled Inwardly-Rectifying Potassium Channels / metabolism
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GTP-Binding Protein alpha Subunits, Gi-Go / metabolism
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GTP-Binding Protein alpha Subunits, Gq-G11 / metabolism
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Humans
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Microfilament Proteins / metabolism*
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Nerve Tissue Proteins / metabolism*
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RGS Proteins / metabolism*
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Rats
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Receptor, Muscarinic M1 / metabolism
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Receptor, Muscarinic M2 / metabolism*
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Receptor, Muscarinic M3 / metabolism*
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Signal Transduction
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Xenopus
Substances
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Chlorides
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G Protein-Coupled Inwardly-Rectifying Potassium Channels
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Microfilament Proteins
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Nerve Tissue Proteins
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RGS Proteins
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Receptor, Muscarinic M1
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Receptor, Muscarinic M2
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Receptor, Muscarinic M3
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neurabin
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GTP-Binding Protein alpha Subunits, Gi-Go
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GTP-Binding Protein alpha Subunits, Gq-G11
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Calcium