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Required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. Additionally we are shipping RASIP1 Antibodies (37) and RASIP1 Kits (4) and many more products for this protein.
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Results show that Rasip1 RA domain formed a dimer that can bind two Rap1 or Ras molecules and solved the Rap1-RRA complex and found that Rasip1 binds Rap1 in the Switch I region, and Rap1 binding induces few conformation changes to Rasip1 stabilizing a beta strand and an unstructured loop.
These studies establish that the binding of HEG1 to Rasip1 mediates Rap1-dependent recruitment of Rasip1 to and stabilization of endothelial cell cell-cell junctions.
results reveal an effector pathway for Rap1 in the modulation of Rho signaling and actin dynamics, through which Rap1 modulates endothelial barrier function
Rain is a novel protein that can serve as an effector of endomembrane-localized Ras
Rasip1 regulates Cdc42 activity to regulate cell junctions and cytoskeleton organization, which are both activities required for lymphatic lumen maintenance
Rasip1 controls different pools of GTPases, which in turn regulates blood vessel tubulogenesis.
Rasip1 is necessary in growing embryonic blood vessels.
we summarize recent developments in understanding the small G protein RAP1 and its effector RASIP1 as critical mediators of endothelial junction stabilization.
RASIP1 regulates the integrity of newly formed blood vessels as an effector of EPAC1-RAP1 signaling.
Mice lacking Rasip1 fail to form patent lumens in all blood vessels, including the early endocardial tube. Rasipl null angioblasts fail to properly localize the polarity determinant Par3 and display defective cell polarity.
Rasip1 expression is undetectable in VEGFR2 null embryos, which lack endothelial cells, suggesting that Rasip1 is endothelial specific. siRNA-mediated reduction of Rasip1 severely impairs angiogenesis and motility in endothelial cell cultures
Required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. Acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Regulates the activity of Rho GTPases in part by recruiting ARHGAP29 and suppressing RhoA signaling and dampening ROCK and MYH9 activities in endothelial cells. May act as effector for Golgi-bound HRAS and other Ras-like proteins. May promote HRAS-mediated transformation.
Ras interacting protein 1
, ras-interacting protein 1