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EZR — PRKAR2A

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Bind Interaction: PRKAR2A — EZR Sun et al., J Biol Chem 2000*, Sitaraman et al., J Biol Chem 2002*, Dransfield et al., EMBO J 1997*
• IRef Bind_translation Interaction: PRKAR2A — EZR (coimmunoprecipitation) Sun et al., J Biol Chem 2000*, Sitaraman et al., J Biol Chem 2002*
• IRef Bind_translation Interaction: PRKAR2A — EZR (experimental interaction detection) Sun et al., J Biol Chem 2000*, Dransfield et al., EMBO J 1997*
• IRef Bind_translation Interaction: PRKAR2A — EZR (experimental interaction detection) Sun et al., J Biol Chem 2000*
• IRef Bind_translation Interaction: PRKAR2A — EZR (coimmunoprecipitation) Sun et al., J Biol Chem 2000*
• IRef Hprd Interaction: PRKAR2A — EZR (in vivo) Sitaraman et al., J Biol Chem 2002*
• IRef Ophid Interaction: PRKAR2A — EZR (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Zhou et al., J Biol Chem 2003 : In addition, expression of S66A mutant ezrin in cultured parietal cells attenuates the dilation of apical vacuolar membrane associated with stimulation by histamine, indicating that PKA mediated phosphorylation of ezrin is necessary for acid secretion ... These data suggest that PKA mediated phosphorylation of ezrin plays an important role in mediating the remodeling of the apical membrane cytoskeleton associated with acid secretion in parietal cells
Wang et al., Biochem Biophys Res Commun 2005 : Our recent studies demonstrate the functional relevance of PKA mediated phosphorylation of ezrin in parietal cell secretion [ R. Zhou, X. Cao, C. Watson, Y. Miao, Z. Guo, J.G. Forte, X. Yao, Characterization of protein kinase A-mediated phosphorylation of ezrin in gastric parietal cell activation, J. Biol. Chem. 278 ( 2003 ) 35651 ]
Jin et al., Biochem Biophys Res Commun 2006 : In addition, our study shows that PKA mediated phosphorylation of ezrin is essential and sufficient for the apical localization of WWOX protein as disruption of ezrin-WWOX interaction eliminated the apical localization of WWOX
Wang et al., Cell Res 2009 (Neoplasms) : Importantly, PKA mediated phosphorylation of ezrin promotes the NK cell internalization process