Gene interactions and pathways from curated databases and text-mining

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NGF — RAC1

Pathways - manually collected, often from reviews:

Text-mined interactions from Literome

Yamaguchi et al., J Biol Chem 2001 : RhoA inhibits the nerve growth factor induced Rac1 activation through Rho associated kinase dependent pathway ... NGF induced a rapid activation of Rac1 and suppression of RhoA activity ... Constitutively active RhoA, RhoA ( V14 ), or constitutively active Galpha(12) induced endogenous RhoA activation inhibited the NGF induced Rac1 activation without any effect on the NGF induced extracellular signal regulated kinase activation ... Moreover, Y-27632, an inhibitor of Rho associated kinase, completely abolished the RhoA induced down-regulation of the NGF induced Rac1 activation
Nusser et al., J Biol Chem 2002 : Furthermore, inhibition of PI3K significantly reduced NGF- mediated Rac1 activation, whereas dominant negative Rac1 abolished the inhibitory signaling to RhoA
Ng et al., J Biol Chem 2003 : More importantly, whereas NGF induced Rac1 activity is enhanced in antisense-LIFR and dominant negative-LIFR expressing PC12 cells, it is reduced in LIFR expressing PC12 cells
Shin et al., J Biol Chem 2004 : Expression of mutant PIX markedly inhibits both bFGF- and nerve growth factor (NGF) induced activation of Rac1 , indicating that phosphorylation of p85 betaPIX is responsible for activation of this G protein
Fujitani et al., Biochem Biophys Res Commun 2005 : Activation of Rac1 induced by NGF is impaired in cholesterol depleted PC12 cells
Chakrabarti et al., Mol Cell Biol 2005 : Furthermore, elevated Kalirin expression resulted in catalytic activation of TrkA, as demonstrated by in vitro kinase assays and increased NGF stimulated cellular activation of Rac , Mek, and CREB
Puntambekar et al., J Neurochem 2005 : Essential role of Rac1/NADPH oxidase in nerve growth factor induction of TRPV1 expression ... Inhibition of NADPH oxidase by transient transfection of a dominant negative Rac1 mutant ( RacN17 ) plasmid blocked NGF stimulated TRPV1 protein expression, while expression of a constitutively active Rac1 increased basal and NGF stimulated TRPV1 levels
Aoki et al., J Cell Biol 2007 : In agreement with this model, depletion of Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2 ( SHIP2 ) markedly potentiated NGF induced Rac1/Cdc42 activation and PIP ( 3 ) accumulation and considerably increased the number and the length of neurites in phosphate and tensin homologue depleted PC12 cells
Noga et al., Clin Exp Allergy 2007 (Hypersensitivity) : NGF led to decreased RhoA and increased Rac activation, while BDNF affected RhoA and Rac activity in a reciprocal fashion
Kim et al., Neurochem Int 2010 : Additionally, NPPB and SITS, another chloride channel blocker, suppressed NGF induced TrkA phosphorylation and subsequent PI3K/Akt phosphorylation and Rac1 activation in PC12 cells
Shirazi Fard et al., PloS one 2010 : In particular, we report that knockdown of Tiam1 causes a significant reduction in Rac1 activity and neurite outgrowth induced by NGF ... Physical interaction between Tiam1 and active Ras ( Ras-GTP ), but not tyrosine phosphorylation of Tiam1, plays a central role in Rac1 activation by NGF
Alsina et al., PloS one 2012 (MAP Kinase Signaling System) : In this work, we demonstrate that overexpression of wild-type Spry4 causes a significant reduction in MAPK and Rac1 activation and neurite outgrowth induced by NGF ... Together, these findings establish a new physiological mechanism through which Spry4 regulates neurite outgrowth reducing not only the MAPK pathway but also restricting Rac1 activation in response to NGF
Talebian et al., J Mol Neurosci 2013 : Moreover, we find that H-Ras over-expression rescues the loss of neurite outgrowth observed with a Rac minus mutant and that RasGrf1 differentially stimulates NGF dependent activation of Rac or Ras, depending on cell type
Spillane et al., J Neurosci 2012 : The effects of NGF on Rac1 activity and increases in axonal levels of WAVE1 and cortactin were both dependent on phosphoinositide 3-kinase (PI3K) signaling