Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
RasGEF-containing proteins GbpC and GbpD have differential effects on cell polarity and chemotaxis in Dictyostelium.
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GbpD induces substrate-attached pseudopodia that increase adhesion and suppress cell polarity.
"GbpD induces the formation of substrate-attached pseudopodia, resulting in increased attachment and suppression of polarity"
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gbpD-null cells are hyperpolar, chemotax better, and make few lateral pseudopodia; the phenotype is opposite to overexpression.
"gbpD-null mutants exhibit the opposite phenotype: cells display improved chemotaxis and appear hyperpolar, because cells make very few lateral pseudopodia"
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The GbpD adhesion/polarity phenotype is independent of intracellular cGMP or cAMP.
"This GbpD phenotype is not dependent on intracellular cGMP or cAMP"
Characterization of the GbpD-activated Rap1 pathway regulating adhesion and cell polarity in Dictyostelium discoideum.
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GbpD activates Rap1 specifically (not the other five characterized Ras proteins) both in vivo and in vitro.
"Here we demonstrate that GbpD activates Rap1 both in vivo and in vitro but not any of the five other characterized Ras proteins"
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GbpD overexpression yields flat, strongly adhesive cells with many bifurcated and lateral pseudopodia.
"Cells overexpressing GbpD are flat, exhibit strongly increased cell-substrate attachment, and extend many bifurcated and lateral pseudopodia"
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Phg2 is the Rap1 effector required for adhesion downstream of GbpD.
"identified Phg2 as Rap1 effector necessary for adhesion, but not cell polarity"
Microtubule-Mediated Inositol Lipid Signaling Plays Critical Roles in Regulation of Blebbing.
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Cells deficient in gbpC/gbpD extended blebs more frequently than wild-type in a microsurgery blebbing screen.
"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"
Excitable Ras dynamics-based screens reveal RasGEFX is required for macropinocytosis and random cell migration.
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RasGEFU is the same protein as cGMP-binding protein D (GbpD) and its overexpression enhances cell-substrate adhesion.
"RasGEFU enhanced cell adhesion to substrates, consistent with previous reports of cGMP-binding protein D (GbpD), which is the same as RasGEFU"
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RasGEFU/GbpD localizes almost uniformly to the plasma membrane without traveling waves.
"RasGEFU localized almost uniformly to the membrane and did not exhibit traveling waves"
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RasGEFU overexpression increases adhesion and enlarges pseudopods while reducing motility.
"RasGEFU-GFP-expressing cells showed increased adhesion to the substrates and thus less motility as their expression increased"