Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Identification of four candidate cGMP targets in Dictyostelium.
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GbpC is a nine-domain protein containing leucine-rich repeats, a Ras (Roc) domain, a MEK/MAP3K-like kinase, RasGEF-N, DEP, RasGEF, and two cGMP-binding domains flanking a GRAM domain.
"GbpC contains the following nine domains (in order): leucine-rich repeats, Ras, MEK kinase, Ras guanine nucleotide exchange factor N-terminal (RasGEF-N), DEP, RasGEF, cGMP-binding, GRAM, and a second cGMP-binding domain"
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Disruption of gbpC removes all high-affinity cGMP-binding activity in the soluble fraction, identifying GbpC as the principal cGMP receptor.
"Disruption of the gbpC gene results in loss of all high-affinity cGMP-binding activity present in the soluble cellular fraction"
RasGEF-containing proteins GbpC and GbpD have differential effects on cell polarity and chemotaxis in Dictyostelium.
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gbpC-null cells display strongly reduced chemotaxis because they cannot polarize in a chemotactic gradient.
"gbpC-null cells display strongly reduced chemotaxis, because they are unable to polarise effectively in a chemotactic gradient"
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cGMP activates GbpC to mediate chemoattractant-induced cell polarity through myosin, whereas GbpD promotes substrate attachment.
"cGMP activates GbpC, mediating the chemoattractant-induced establishment of cell polarity through myosin"
Myosin light chain kinase A is activated by cGMP-dependent and cGMP-independent pathways.
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Activation of myosin light chain kinase A during chemotaxis depends on cGMP levels and on GbpC.
"MLCK-A activation during chemotaxis is highly responsive to cellular cGMP levels and the cGMP-binding protein GbpC"
The Legionella pneumophila phosphatidylinositol-4 phosphate-binding type IV substrate SidC recruits endoplasmic reticulum vesicles to a replication-permissive vacuole.
Intramolecular activation mechanism of the Dictyostelium LRRK2 homolog Roco protein GbpC.
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The GbpC RasGEF domain specifically accelerates GDP/GTP exchange on its own Roc domain and on no other tested Ras/Rap GTPase.
"the RasGEF domain of GbpC specifically accelerates the GDP/GTP exchange of the Roc domain"
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cGMP binding stimulates GbpC binding to GTP-agarose, indicating cGMP-stimulated GDP/GTP exchange at the Roc domain.
"cGMP binding to GbpC strongly stimulates the binding of GbpC to GTP-agarose"
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GbpC operates as a four-step intramolecular cascade from cGMP binding through GEF activation and Roc exchange to MAP3K activation.
"a four-step intramolecular activation mechanism of the Roco protein GbpC: cGMP binding to the cyclic nucleotide-binding domains, activation of the GEF domain, GDP/GTP exchange of Roc, and activation of the MAPKKK domain"
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GbpC is the only high-affinity cGMP target in Dictyostelium; functional GEF, Roc, and kinase domains are all required in vivo.
"Mutants that lack a functional guanine exchange factor (GEF), Roc, or kinase domain are inactive in vivo"
Switching direction in electric-signal-induced cell migration by cyclic guanosine monophosphate and phosphatidylinositol signaling.
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Genetic modulation of GbpC together with guanylyl cyclases can reverse the direction of migration during electrotaxis.
"the preferential direction of migration during electrotaxis in Dictyostelium cells can be reversed by genetically modulating both guanylyl cyclases (GCases) and the cyclic guanosine monophosphate (cGMP)-binding protein C (GbpC)"
Multiple regulatory mechanisms for the Dictyostelium Roco protein GbpC.
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GbpC is cytoplasmic in resting cells and translocates to the cell boundary upon cAMP stimulation.
"In resting cells, the protein is present in the cytoplasm, but GbpC rapidly translocates to the cell boundary upon stimulation with the chemoattractant cAMP"
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The GRAM domain binds phospholipids and mediates GbpC translocation to the plasma membrane and cell cortex.
"cAMP induces a GRAM-dependent translocation of GbpC toward the plasma membrane and cell cortex"
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cGMP-mediated GbpC activation is essential for proper regulation of myosin II during chemotaxis.
"cGMP-mediated GbpC activation is essential for the proper regulation of myosin II during chemotaxis"
Microtubule-Mediated Inositol Lipid Signaling Plays Critical Roles in Regulation of Blebbing.
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gbpC/gbpD-deficient cells extend blebs more frequently than wild type, implicating GbpC in regulation of blebbing.
"cells deficient in gbpC-/gbpD (guanylate cyclases), pkgB (serine/threonine-protein kinase), iplA (Ca2+ channel), or pi3k (phosphatidylinositol 3-kinase) extended blebs more frequently than wild type cells"