protein
| binding partners of MLLT4 |
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RASGRP3 activates RAP1A, which in some cases can antagonize the function of RAS (RAP1A can antagonize the function of RAS, and DGKI regulates RASGRP3 with a predominant effect on RAP1A activity) |
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binds to KRIT1, a guanosine triphosphatase that maintains the integrity of endothelial junctions (RAP1A activity regulated the junctional localization of KRIT1 and its physical association with junction proteins) |
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interacting with RAPGEF3 (interaction of RAPGEF3 with RAN is necessary for the efficient activation of RAP1A by RAPGEF3) |
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binding of MLLT4 to RAP1A regulated the activity of RAP1A in a positive-feedback manner |
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interacting with HRAS and acting dominantly over C-terminal lipid modification of HRAS (essential and sufficient for the plasma membrane localization) |
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interaction of RASSF1 with RAP1A is shown to influence the effect of RASSF1 on microtubule behavior |
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SDC1 restrains migration in lung epithelium by activating RAP1A to slow focal adhesion disassembly |
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RADIL, a novel RAP1A effector, regulates ITGB1, ITGB2 activation and controls neutrophil chemotaxis |
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RADIL is emerging as an important RAP1A effector implicated in cell spreading and migration |
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RAP1A signaling enables plasticity and fear learning by regulating CACNA1D at cortico-amygdala synapses |
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RASIP1 is a RAP1A-effector involved in cell spreading and endothelial barrier function |
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induces integrin activation via an inside-out signaling pathway mediated by APBB1IP |
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MEX3B regulate the cortical level of activated RAP1A, a small G protein controlling phagocytosis and cell-cell interaction, through the activation and transport of RAP1GAP |
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ZSCAN4 functions as a mediator of telomere length through its direct interaction with RAP1A, possibly regulating shelterin complex-controlled telomere elongation in both telomerase positive and alternative lengthening of telomere pathways |
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RAPGEF2 acts on the multipolar-bipolar transition during neuronal migration via a RAP1A/N-cadherin pathway |
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RAP1A effectors RADIL and RASIP1, together with the RHO GTPase activating protein ARHGAP29, mediate RAP1A-induced inhibition of RHO signaling in the processes of epithelial cell spreading and endothelial barrier function |
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two effectors of RAP1A regulate integrins, RASSF5 and APBB1IP |
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RASIP1 can act as a RAP1A and RAS effector and RASIP1 defines a subgroup of dimeric RA domains that could mediate cooperative binding to membrane-associated RAS superfamily members |
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novel roles for PODXL as an important modulator of neutrophil and monocyte formation and of RAP1A activation during stress hematopoiesis |
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UBE2I acts as a functional binding partner of FYB1 and plays a selective role in integrin-mediated T cell adhesion via modulation of RAP1A-RASSF5 membrane recruitment and RAC1 activation |