Transformation of cells overexpressing a tyrosine kinase by phospholipase D1 and D2.

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Biochemical and biophysical research communications, ISSN: 0006-291X, Vol: 289, Issue: 5, Page: 1019-24

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Troy Joseph; Roger Wooden; Annika Bryant; Minghao Zhong; Zhimin Lu; David A. Foster
Elsevier BV
Biochemistry, Genetics and Molecular Biology
article description
Phospholipase D (PLD) activity is elevated in response to most mitogenic signals. Two mammalian PLD genes (PLD1 and PLD2) have been cloned and their gene products have been characterized. PLD1 is a downstream target of the Ras/RalA GTPase cascade implicated in mitogenic and oncogenic signaling. Consistent with a role in mitogenic signaling, elevated expression of PLD1 transforms cells overexpressing the epidermal growth factor (EGF) receptor (EGFR). However, PLD2 colocalizes with the EGFR in caveolin-enriched light membrane microdomains. We therefore investigated whether PLD2 could also contribute to the transformation of cells overexpressing a tyrosine kinase. We report here that elevated expression of PLD2 transforms rat fibroblasts overexpressing either the EGFR or c-Src. Since overexpression of a tyrosine kinase is a common genetic alteration in several human cancers, these data suggest that elevation of either PLD1 or PLD2 may contribute to the progression to a malignant phenotype in cells with elevated tyrosine kinase activity.