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HL-60 neutrophil-like cells expressing Rap1a(G12V) or Radil have an elongated phenotype because of enhanced uropod adhesion as they attempt to migrate on fibronectin. This elongated phenotype driven by Rap1a(G12V) or Radil is reversed by Galphai1(Q204L), but not by WT Galphai1 expression, suggesting that Galphai-GTP also regulates adhesion in immune cells at the level of, or downstream of, Radil.
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these data highlight a signaling pathway in which SHP-1 acts through CrkII to reshape the pattern of Rap1 activation in the immunological synapse.
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Study identifies Epac2-Rap1 signaling as a novel feedback mechanism in the heart, which controls mitochondrial reactive oxygen species production.
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Data show that the Epac-Rap1 signaling axis is involved in triapine resistance.
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Ubc9 is an essential regulator of ADAP where it is required for TCR-induced membrane recruitment of the small GTPase Rap1 and its effector protein RapL.
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These findings provide the first evidence linking Rap1A with ovarian cancer development through the ERK/p38 and Notch signaling pathways, indicating that Rap1A may be used as a novel diagnostic marker or a therapeutic target for ovarian cancer.
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High RAP1 expression is associated with neuroblastoma.
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Rap1 mediates the effects of increased extracellular tension in multiple ways that are capable of contributing to tumor progression when dysregulated.
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Novel mutations in RASGRP2, which encodes CalDAG-GEFI, abrogate Rap1 activation, causing platelet dysfunction
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Unlike Rap1B, phosphorylation in the polybasic region of Rap1A does not detectably inhibit its prenylation or its binding to SmgGDS-607.
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SHANK1 and SHANK3 act as integrin activation inhibitors by sequestering active Rap1 and R-Ras via the SPN domain and thus limiting their bioavailability at the plasma membrane.
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These results suggest that Rap1 activation of ERKs requires PKA phosphorylation and KSR binding.
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These data suggested that HBV-infection could up-regulate the expression of miR-203a, thus down regulated the expression of Rap1a.
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Studies indicate that Rap interacting proteins decide the subcellular localization of Rap, and the interaction modes with downstream Rap effectors.
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A receptor type-protein tyrosine phosphatase alpha-Src family kinase-Rap1 pathway was identified as responsible for recruiting myosin IIB to the zonula adherens in epithelial cells and supporting contractile tension.
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Rap1- and Rac1-GTPase activation have roles in hypoxia/reoxygenation-experienced cancer cell migration and metastasis via the expression of thymosin beta-4
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These findings provide further evidence that a crucial role for miR-203 in inhibiting metastasis of PCa through the suppression of Rap1A expression.
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Our findings suggest that RAP1 may be a useful biomarker for the diagnosis of ical intraepithelial neoplasia .
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RAP1-mediated MEK/ERK pathway defects in Kabuki syndrome.
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Rap1 knockdown attenuates prostacyclin (PC)-induced vascular endothelial cell (EC) monolayer recovery.
