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Activation of phospholipase D is not mediated by direct phosphorylation on tyrosine residues
Journal article   Peer reviewed

Activation of phospholipase D is not mediated by direct phosphorylation on tyrosine residues

Sanjoy Mehta, Jeff Maglio, Mike S Kobayashi, Andrea M Sipple and Joel Horwitz
Biochimica et biophysica acta. Molecular and cell biology of lipids, v 1631(3)
2003
PMID: 12668176

Abstract

PC12 cell Tyrosine kinase Phospholipase D
The activation of phospholipase D (PLD) in PC12/PC2 pheochromocytoma cells involves a tyrosine kinase. However, it is not clear whether this is due to direct phosphorylation of the enzyme or some other intermediary protein. In this manuscript, we examined this issue by two methods: (1) immunoprecipitation of phosphotyrosine containing proteins and assay of phospholipase D; (2) overexpression of HA–phospholipase D2 and susbsequent immunoprecipitation. The only agent that caused phosphorylation of phospholipase D on tyrosine residues was the phosphatase inhibitor, peroxyvanadate. Other agents that activate phospholipase D, including bradykinin, ionomycin, and phorbol dibutyrate did not cause phosphorylation of the enzyme. In addition, there was a lack of correlation between the peroxyvanadate-mediated phosphorylation and activation of phospholipase D, both in terms of time course and concentration dependence. These data demonstrate that phospholipase D is directly phosphorylated on tyrosine residues. However, phosphorylation of tyrosine residues does not correlate with activation of the enzyme.

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Web of Science research areas
Biochemistry & Molecular Biology
Biophysics
Cell Biology
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