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BPNT1 — PLD4

Text-mined interactions from Literome

Huang et al., Mol Cell Biochem 1999 (Carcinoma, Hepatocellular) : It was found that phospholipase D was marginally activated by phosphatidyl-4-phosphate (PIP) and phosphatidylethanolamine ( PE ) ... The activation of phospholipase D by PIP2 was dose dependent up to 50 microM of PIP2
Kurz et al., J Mol Cell Cardiol 2004 : The addition of PIP2 restored the sensitivity of solubilized PLD to neomycin inhibition, indicating that neomycin inhibits PLD activity by binding to endogenous PIP2 ... Our results demonstrate a critical role for PIP2 in human cardiac PLD activity and suggest that PIP2 synthesis ( by phosphatidylinositol 4-phosphate 5-kinase ) and hydrolysis ( by PIP2-specific PLC ) could be important determinants in regulating PLD signal transduction in the human heart
Ohguchi et al., J Biol Chem 1996 : The PKC mediated PLD activation was completely inhibited by neomycin, a high affinity ligand for PIP2, and this suppression was recovered by the addition of exogenous PIP2
Mayr et al., FEBS Lett 1996 : In contrast, the Ca ( 2+ ) -dependent PLD described here is not affected by PIP2 and does not catalyze transphosphatidylation
Liscovitch et al., J Lipid Mediat Cell Signal 1996 : Neomycin, a high affinity ligand of PIP2 , inhibits membrane PLD activity, presumably by binding to endogenous PIP2