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EPHB2 — MYLK

Text-mined interactions from Literome

Mansfield et al., Blood 2000 : The isolated ERK2 was incubated with PMNL cytosol as a source of unactivated MLCK and with MLCK substrate ; under these conditions ERK2 activated MLCK , resulting in phosphorylation of the MLCK substrate or of the myosin light chain itself
Savkovic et al., Am J Physiol Gastrointest Liver Physiol 2001 (Inflammation...) : Although ERK1/2 can activate MLCK , its inhibition had no impact on EPEC disruption of the tight junction barrier
Takayama et al., J Biol Chem 2003 : Treatment of fibroblasts with Lf enhanced the phosphorylation of ERK1/2 and the activation of MLC kinase (MLCK)
Roovers et al., Mol Cell Biol 2003 (MAP Kinase Signaling System) : Inhibition of either MLCK or Rho kinase blocked sustained ERK signaling, but only Rho kinase inhibition allowed for the induction of cyclin D1 and activation of cdk4 via Rac/Cdc42
Bessard et al., Hepatology 2006 : Inhibition of either MLCK or RhoK did not block ERK1/2 phosphorylation, whereas MLCK regulated ERK2 dependent p70S6K activation
Muralidharan-Chari et al., Curr Biol 2009 (Neoplasm Invasiveness) : To enable microvesicle shedding, ARF6-GTP dependent activation of phospholipase D promotes the recruitment of the extracellular signal regulated kinase ( ERK ) to the plasma membrane where, in turn, ERK phosphorylates and activates myosin light-chain kinase (MLCK)