Gene interactions and pathways from curated databases and text-mining

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EPHB2 — RHOA

Pathways - manually collected, often from reviews:

Text-mined interactions from Literome

Jo et al., J Biol Chem 2002 : Paradoxically, Y-27632 and RhoA-N19 increased ERK phosphorylation in MCF-7 cells, providing further evidence that ERK activation alone does not promote cell migration when Rho kinase is antagonized
Singh et al., J Biol Chem 2003 (MAP Kinase Signaling System) : Using C-3 exoenzyme ( RhoA inhibitor ) or monodansylcadaverine ( TGase inhibitor ), we show that transamidated RhoA regulates cytoskeletal rearrangement and activation of ERK1/2 and p38gamma MAP kinases
Tanaka et al., EMBO J 2003 : The inhibition of RhoA activity in animal caps significantly prevents the EphB2- and ephrin-B1 mediated cell sorting
Andresen et al., Hypertension 2003 (MAP Kinase Signaling System) : Furthermore, T19N RhoA inhibited Ang II-mediated ERK phosphorylation, whereas T19N RhoA had significantly less effect on EGF mediated ERK phosphorylation
Zuckerbraun et al., Circulation 2003 : The purpose of this investigation was to examine whether RhoA regulates ERK downstream signaling and cellular proliferation through its effects on the cytoskeleton and the nuclear localization of ERK ... RhoA inhibition increased levels of phosphorylated ERK in the cell nucleus
Vial et al., Cancer Cell 2003 (Colonic Neoplasms...) : ERK-MAPK signaling coordinately regulates activity of Rac1 and RhoA for tumor cell motility
Krepinsky et al., J Am Soc Nephrol 2003 : In primary rat MC subjected to cyclic mechanical strain, RhoA activity was maximally increased ( 2.4-fold ) after 1 min of stretch, and Erk activation temporally followed ... The authors conclude that the early activation of RhoA is essential for stretch induced actin stress fiber formation and Erk activation in MC, events which are prevented by NO and cGMP through their action on RhoA
Reuveny et al., FEBS Lett 2004 : Here, we show that inhibition of RhoA prevents the phosphorylation of Akt, but does not affect the phosphorylation of ERK
Wallert et al., Cell Signal 2005 : The data indicate that ERK activation is essential for phenylephrine stimulation of NHE1, and that ERK and RhoA are involved in LPA stimulation of NHE1 by more than one mechanism ... These studies indicate a direct involvement of ERK in the alpha ( 1 ) -adrenergic activation of NHE1 and a significant role for both ERK and RhoA in LPA stimulation of NHE1 in CCL39 fibroblasts
Moeller et al., J Biol Chem 2006 : Finally, EphB mediated RhoA activation is disrupted by FAK knock-down
Kim et al., Exp Mol Med 2005 : Inhibition of ERK1/2 , p38 MAPK, phosphatidyl inositol 3-kinase did not block translocation of RhoA to membranes, suggesting that RhoA is upstream to these kinases
Ogawa et al., J Cell Sci 2006 : Interestingly, we found that EphB signaling induces RhoA activation and Rac1 inactivation as well as cell retraction, enlargement of focal adhesions and prominent stress fibers in primary cultures of medullary tubule cells
Chapados et al., Circ Res 2006 (Disease Progression...) : Indeed, SMCs on denatured collagen possessed higher levels of RhoA activity than those on native collagen, and blocking RhoA or ROCK activities attenuated SMC spreading, ERK1/2 activity, and TN-C expression in SMCs on denatured collagen
Yano et al., Circ Res 2007 (Inflammation) : However, DN-RhoA and DN-Cdc42 activated p38 MAPK, but not ERK1/2
Wu et al., J Biol Chem 2007 (MAP Kinase Signaling System) : Instead, knock down of the novel oxidase Nox4 completely suppressed Tat dependent Ras and ERK activation downstream of Rac1 and RhoA
Li et al., Bioinformatics 2009 : We examined whether RhoA can substantially affect ERK activity via this MEKK1 mediated crosstalk between RhoA and EGFR-ERK pathway ... Our results indicated possible roles of RhoA in affecting ERK activities via MEKK1 mediated crosstalk, which seems to be supported by indications from several experimental studies that may also implicate the collective regulation of cell fate and progression of cancer and other diseases
Khatiwala et al., J Bone Miner Res 2009 (MAP Kinase Signaling System) : Inhibition of RhoA and ROCK in MC3T3-E1 pre-osteoblasts cultured on substrates of varying compliance reduced ERK activity, whereas constitutively active RhoA enhanced it
Notcovich et al., Exp Cell Res 2010 : On the other hand, H1R induced ERK1/2 activation was inhibited by U73122 but not affected by C3 or beta2-chimaerin, suggesting that ERK1/2 activation was dependent on PLC and independent of RhoA or Rac
Pattabiraman et al., Am J Physiol Cell Physiol 2010 (Mechanotransduction, Cellular) : Collectively, data on RhoA induced changes in actomyosin contractile activity, ECM synthesis/assembly, and Erk activation, along with fibronectin induced alpha-SMA expression in TM cells, reveal a potential molecular interplay between actomyosin cytoskeletal tension and ECM synthesis/assembly
Kakiashvili et al., J Biol Chem 2011 (MAP Kinase Signaling System) : EGF treatment mimicked the effects of TNF-a, as it elicited potent, ERK dependent GEF-H1 and RhoA activation
Buonomo et al., J Cell Physiol 2012 (Diabetes Mellitus, Type 2...) : Inhibition of ERK1/2 activity by PD98059 restored RhoA activation, cytoskeleton organization and cell motility, and almost completely rescued wound closure of TgPED fibroblasts
Chaturvedi et al., Am J Physiol Cell Physiol 2011 (MAP Kinase Signaling System...) : Role of RhoA and its effectors ROCK and mDia1 in the modulation of deformation induced FAK, ERK , p38, and MLC motogenic signals in human Caco-2 intestinal epithelial cells ... RhoA , ROCK inhibition, or RhoA, ROCK1, ROCK2, mDia1, and FAK reduction by siRNA blocked deformation induced nuclear ERK phosphorylation without preventing ERK phosphorylation in the cytoplasmic protein fraction
Obara et al., PloS one 2011 : LPI increased intracellular Ca ( 2+ ) concentration and RhoA activity, and induced ERK1/2 phosphorylation, whereas endogenous and synthetic cannabinoids did not, thereby suggesting that cannabinoids are not GPR55 agonists
Tang et al., Int J Biochem Cell Biol 2012 : RhoA-V14 , a constitutively active form of RhoA, could activate the MEK/ERK/Runx2 signaling
Loureiro et al., Exp Cell Res 2013 (Amino Acid Metabolism, Inborn Errors) : Accordingly, these antioxidants were able to prevent the remodeling of the actin cytoskeleton, RhoA increased levels and ERK1/2 phosphorylation in response to high Pro exposure