GNAO1 encodes the Go alpha subunit, an abundant neuronal heterotrimeric G protein that switches between GDP- and GTP-bound states to transmit receptor signals. Go participates in neurotransmitter-receptor control of channels, vesicle release and cAMP signaling, with different alpha isoforms and cellular contexts determining the output. Cellular suppression of cAMP can involve beta/gamma availability and pathway coupling rather than direct inhibition of every cyclase isoform. Go is prominent at neuronal plasma membranes and synapses and also regulates endocrine secretory-vesicle docking.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003924 GTPase activity | IEA GO_REF:0000120 | ACCEPT | Summary: GNAO1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. |
| GO:0003924 GTPase activity | ISS GO_REF:0000024 | ACCEPT | Summary: GNAO1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. |
| GO:0003924 GTPase activity | TAS PMID:1899283 Different forms of Go alpha mRNA arise by alternative splici... | ACCEPT | Summary: GNAO1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. |
| GO:0003925 G protein activity | IBA GO_REF:0000033 | ACCEPT | Summary: GNAO1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. |
| GO:0003925 G protein activity | IDA PMID:33408414 Structures of the glucocorticoid-bound adhesion receptor GPR... | ACCEPT | Summary: GNAO1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. |
| GO:0003925 G protein activity | IDA PMID:39103320 A neurodevelopmental disorder mutation locks G proteins in t... | ACCEPT | Summary: GNAO1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. |
| GO:0003925 G protein activity | IEA GO_REF:0000107 | ACCEPT | Summary: GNAO1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. |
| GO:0003925 G protein activity | ISS GO_REF:0000024 | ACCEPT | Summary: GNAO1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. |
| GO:0005515 protein binding | IPI PMID:17500595 Huntingtin interacting proteins are genetic modifiers of neu... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:34685729 Pediatric Encephalopathy: Clinical, Biochemical and Cellular... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:37207277 Using brain cell-type-specific protein interactomes to inter... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005515 protein binding | IPI PMID:37776851 Analysis of proteome-wide degradation dynamics in ALS SOD1 i... | REMOVE | Summary: The physical interactions are not denied. Reason: Remove bare protein binding under the project policy while retaining specific receptor, beta/gamma and effector functions supported independently. |
| GO:0005525 GTP binding | IEA GO_REF:0000120 | ACCEPT | Summary: GNAO1 is a guanine-nucleotide-binding G alpha subunit that switches between GDP- and GTP-bound states and hydrolyzes bound GTP. Reason: Receptor/effector biochemistry and nucleotide-state experiments support the intrinsic molecular switch. This is distinct from the GAP activity of RGS proteins; activated or nucleotide-defective mutants are controls, not substitutes for the wild-type function. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: The G alpha protein is an intracellular peripheral-membrane signaling component with a cytoplasmic pool. Reason: Cytoplasm is compatible with membrane association and, where demonstrated, other intracellular pools; no exclusive localization is inferred. |
| GO:0005834 heterotrimeric G-protein complex | IBA GO_REF:0000033 | ACCEPT | Summary: The GDP-state G alpha subunit associates with a G beta/gamma dimer to form a functional heterotrimer. Reason: Receptor-coupling and structural/reconstitution experiments support this assembly and beta/gamma binding as integral functions. A particular experimental beta/gamma combination does not imply universal interchangeability. |
| GO:0005834 heterotrimeric G-protein complex | IDA PMID:29925951 Cryo-EM structure of the serotonin 5-HT(1B) receptor coupled... | ACCEPT | Summary: The GDP-state G alpha subunit associates with a G beta/gamma dimer to form a functional heterotrimer. Reason: Receptor-coupling and structural/reconstitution experiments support this assembly and beta/gamma binding as integral functions. A particular experimental beta/gamma combination does not imply universal interchangeability. |
| GO:0005886 plasma membrane | IDA PMID:34685729 Pediatric Encephalopathy: Clinical, Biochemical and Cellular... | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: UniProtKB-SubCell:SL-0039 SUPPORTS TRANSFER The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3965444 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3965447 | MODIFY | Summary: The independently supported plasma-membrane signaling pool lies on the cytoplasmic side, already represented separately in this record. Reason: Refine this general membrane location while retaining other independently supported intracellular locations; the refinement does not assert exclusive residence. Proposed replacements: cytoplasmic side of plasma membrane |
| GO:0006936 muscle contraction | TAS PMID:9050846 G alpha(o) is necessary for muscarinic regulation of Ca2+ ch... | KEEP AS NON CORE | Summary: Native mouse Go loss disrupts muscarinic regulation of ventricular L-type calcium currents, providing a signaling mechanism affecting cardiac contraction. Reason: Retain this regulatory contribution to the physiological process, not a claim that Go is part of the contractile filament. Supporting Evidence: |
| GO:0007165 signal transduction | IEA GO_REF:0000002 | MODIFY | Summary: The protein directly transduces signals through heterotrimeric G protein-coupled receptor signaling. Reason: Refine generic signal transduction to the established receptor pathway without excluding additional receptor-independent functions. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: InterPro:IPR011025 SUPPORTS TRANSFER The protein directly transduces signals through heterotrimeric G protein-coupled receptor signaling. Refine generic signal transduction to the established receptor pathway without excluding additional receptor-independent functions. Proposed replacements: G protein-coupled receptor signaling pathway |
| GO:0007186 G protein-coupled receptor signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: Receptor-dependent nucleotide exchange and effector coupling establish direct participation in GPCR signaling. Reason: Individual receptor preferences and physiological contexts must be established separately rather than inferred from the whole G protein family. |
| GO:0007188 adenylate cyclase-modulating G protein-coupled receptor signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: Go modulates cellular cAMP signaling through receptor/cell-dependent mechanisms. Reason: Native neuronal and biochemical experiments separate effects on Gi/beta-gamma coupling from direct cyclase regulation; Go is not a universal direct cyclase inhibitor. |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:29925951 Cryo-EM structure of the serotonin 5-HT(1B) receptor coupled... | ACCEPT | Summary: Receptor-coupled Go supports inhibition of cellular cAMP in defined systems, including wild-type Go/M4 reporter assays and neuronal dopamine signaling. Reason: Purified Go has limited isoform-specific effects, and the cellular phenotype does not establish direct Go inhibition of ADCY6. Structural receptor complexes establish reception, not the downstream enzyme mechanism by themselves. Supporting Evidence: PMID:8119955 Type II adenylyl cyclase appears to be immune to inhibition by these proteins |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:33408414 Structures of the glucocorticoid-bound adhesion receptor GPR... | ACCEPT | Summary: Receptor-coupled Go supports inhibition of cellular cAMP in defined systems, including wild-type Go/M4 reporter assays and neuronal dopamine signaling. Reason: Purified Go has limited isoform-specific effects, and the cellular phenotype does not establish direct Go inhibition of ADCY6. Structural receptor complexes establish reception, not the downstream enzyme mechanism by themselves. Supporting Evidence: PMID:8119955 Type II adenylyl cyclase appears to be immune to inhibition by these proteins |
| GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway | IDA PMID:39103320 A neurodevelopmental disorder mutation locks G proteins in t... | ACCEPT | Summary: Receptor-coupled Go supports inhibition of cellular cAMP in defined systems, including wild-type Go/M4 reporter assays and neuronal dopamine signaling. Reason: Purified Go has limited isoform-specific effects, and the cellular phenotype does not establish direct Go inhibition of ADCY6. Structural receptor complexes establish reception, not the downstream enzyme mechanism by themselves. Supporting Evidence: PMID:8119955 Type II adenylyl cyclase appears to be immune to inhibition by these proteins |
| GO:0007195 adenylate cyclase-inhibiting dopamine receptor signaling pathway | IDA PMID:39103320 A neurodevelopmental disorder mutation locks G proteins in t... | KEEP AS NON CORE | Summary: Native neuronal and receptor-coupling experiments support Go regulation of dopamine-linked cAMP signaling. Reason: Disease-mutant comparisons must be distinguished from wild-type transduction, and Go effects can depend on beta/gamma-mediated cyclase modulation rather than direct catalytic-site inhibition. |
| GO:0007198 adenylate cyclase-inhibiting serotonin receptor signaling pathway | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The 5-HT1B–Go complex and inherited signaling evidence support a serotonin-receptor implementation of the Gi/o-linked inhibitory pathway. Reason: The engineered structural complex is receptor-coupling evidence; cellular inhibition should not be restated as proof of purified Go inhibition of every cyclase. |
| GO:0007198 adenylate cyclase-inhibiting serotonin receptor signaling pathway | IDA PMID:29925951 Cryo-EM structure of the serotonin 5-HT(1B) receptor coupled... | KEEP AS NON CORE | Summary: The 5-HT1B–Go complex and inherited signaling evidence support a serotonin-receptor implementation of the Gi/o-linked inhibitory pathway. Reason: The engineered structural complex is receptor-coupling evidence; cellular inhibition should not be restated as proof of purified Go inhibition of every cyclase. |
| GO:0007212 G protein-coupled dopamine receptor signaling pathway | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Native neuronal and receptor-coupling experiments support Go regulation of dopamine-linked cAMP signaling. Reason: Disease-mutant comparisons must be distinguished from wild-type transduction, and Go effects can depend on beta/gamma-mediated cyclase modulation rather than direct catalytic-site inhibition. |
| GO:0009898 cytoplasmic side of plasma membrane | IDA PMID:33408414 Structures of the glucocorticoid-bound adhesion receptor GPR... | ACCEPT | Summary: The intracellular G alpha–beta/gamma complex contacts the cytoplasmic receptor surface and intracellular effectors. Reason: Receptor-complex structures, membrane targeting and signaling experiments support the cytoplasmic plasma-membrane face. |
| GO:0009898 cytoplasmic side of plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: The intracellular G alpha–beta/gamma complex contacts the cytoplasmic receptor surface and intracellular effectors. Reason: Receptor-complex structures, membrane targeting and signaling experiments support the cytoplasmic plasma-membrane face. |
| GO:0019001 guanyl nucleotide binding | IEA GO_REF:0000002 | MODIFY | Summary: The conserved guanine-nucleotide pocket binds GTP during activation and GDP in the inactive state. Reason: Refine the generic nucleotide-binding term to these two chemically defined ligands, preserving both halves of the switch. Propagation Review Root cause: TERM SCOPING PROBLEM Sources checked: InterPro:IPR001019 SUPPORTS TRANSFER The conserved guanine-nucleotide pocket binds GTP during activation and GDP in the inactive state. Refine the generic nucleotide-binding term to these two chemically defined ligands, preserving both halves of the switch. Proposed replacements: GTP binding GDP binding |
| GO:0030425 dendrite | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse cerebellar and retinal immunolocalization supports dendritic and neuronal-soma pools. Reason: Retain these conserved locations with cell-type and developmental-stage limits. Supporting Evidence: PMID:34248508 preferentially localized on the cytoplasmic face of the plasma membrane |
| GO:0031683 G-protein beta/gamma-subunit complex binding | IEA GO_REF:0000002 | ACCEPT | Summary: The GDP-state G alpha subunit associates with a G beta/gamma dimer to form a functional heterotrimer. Reason: Receptor-coupling and structural/reconstitution experiments support this assembly and beta/gamma binding as integral functions. A particular experimental beta/gamma combination does not imply universal interchangeability. |
| GO:0031852 mu-type opioid receptor binding | IBA GO_REF:0000033 | ACCEPT | Summary: The curated PAINT assertion at PTN000026844 identifies conserved receptor-class binding in the Go clade. Reason: The traced rat primaries measure Go co-precipitation with mu-opioid receptor and CRF receptor; the latter finds no sex/stress difference in Go association, not absence of association. Retain this conserved receptor-class binding with co-complex and species limits rather than claim purified human binary affinity. |
| GO:0042734 presynaptic membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse quantitative immunoelectron microscopy detects Go on neuronal membranes, including pre/post-synaptic compartments, glutamatergic parallel-fiber/Purkinje contacts and GABAB-associated sites. Reason: Retain the conserved synaptic locations without transferring every mouse ultrastructural observation as a direct human measurement. Supporting Evidence: PMID:34248508 preferentially localized on the cytoplasmic face of the plasma membrane |
| GO:0044297 cell body | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse cerebellar and retinal immunolocalization supports dendritic and neuronal-soma pools. Reason: Retain these conserved locations with cell-type and developmental-stage limits. Supporting Evidence: PMID:34248508 preferentially localized on the cytoplasmic face of the plasma membrane |
| GO:0045211 postsynaptic membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse quantitative immunoelectron microscopy detects Go on neuronal membranes, including pre/post-synaptic compartments, glutamatergic parallel-fiber/Purkinje contacts and GABAB-associated sites. Reason: Retain the conserved synaptic locations without transferring every mouse ultrastructural observation as a direct human measurement. Supporting Evidence: PMID:34248508 preferentially localized on the cytoplasmic face of the plasma membrane |
| GO:0046676 negative regulation of insulin secretion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Pancreatic-cell-specific mouse Go deletion enhances insulin secretion and increases docked vesicles without preventing endocrine differentiation. Reason: Retain the conserved inhibitory secretory role with a docking mechanism, not a direct insulin-binding or biosynthetic function. Supporting Evidence: |
| GO:0046929 negative regulation of neurotransmitter secretion | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: PTX-resistant Go rescue in native rat hippocampal neurons establishes participation in receptor-mediated presynaptic inhibition. Reason: RGS-insensitive mutants alter kinetics, supporting regulated signal duration rather than a direct vesicle-cleaving activity. Supporting Evidence: |
| GO:0051430 corticotropin-releasing hormone receptor 1 binding | IBA GO_REF:0000033 | ACCEPT | Summary: The curated PAINT assertion at PTN000026844 identifies conserved receptor-class binding in the Go clade. Reason: The traced rat primaries measure Go co-precipitation with mu-opioid receptor and CRF receptor; the latter finds no sex/stress difference in Go association, not absence of association. Retain this conserved receptor-class binding with co-complex and species limits rather than claim purified human binary affinity. |
| GO:0071867 response to monoamine | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Go transduces dopamine and serotonin receptor signals in direct receptor/cellular studies. Reason: Retain response to monoamine as a peripheral physiological description, not monoamine transport or synthesis. |
| GO:0098688 parallel fiber to Purkinje cell synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse quantitative immunoelectron microscopy detects Go on neuronal membranes, including pre/post-synaptic compartments, glutamatergic parallel-fiber/Purkinje contacts and GABAB-associated sites. Reason: Retain the conserved synaptic locations without transferring every mouse ultrastructural observation as a direct human measurement. Supporting Evidence: PMID:34248508 preferentially localized on the cytoplasmic face of the plasma membrane |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse quantitative immunoelectron microscopy detects Go on neuronal membranes, including pre/post-synaptic compartments, glutamatergic parallel-fiber/Purkinje contacts and GABAB-associated sites. Reason: Retain the conserved synaptic locations without transferring every mouse ultrastructural observation as a direct human measurement. Supporting Evidence: PMID:34248508 preferentially localized on the cytoplasmic face of the plasma membrane |
| GO:0098982 GABA-ergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse quantitative immunoelectron microscopy detects Go on neuronal membranes, including pre/post-synaptic compartments, glutamatergic parallel-fiber/Purkinje contacts and GABAB-associated sites. Reason: Retain the conserved synaptic locations without transferring every mouse ultrastructural observation as a direct human measurement. Supporting Evidence: PMID:34248508 preferentially localized on the cytoplasmic face of the plasma membrane |
| GO:0099170 postsynaptic modulation of chemical synaptic transmission | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native striatal Go loss and optical cAMP measurements establish postsynaptic neuromodulatory effects. Reason: The mechanism involves receptor/cyclase coupling and beta/gamma regulation; it is not reducible to universal direct Go inhibition of cyclase. Supporting Evidence: |
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