Regulation of phospholipase D by tyrosine kinases

Natarajan, Viswanathan; Scribner, William M.; Vepa, Suryanarayana

doi:10.1016/0009-3084(96)02548-0

Cited by 64 publications

(42 citation statements)

References 128 publications

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“…Several studies indicate that PTKs participate in the PLD activation via an unidentified mechanism (38). However, the biological significance of phosphorylation as one of the activation mechanisms of PLD still remains to be determined, since PLD activity has not been correlated with its phosphorylation level in many studies (18,32).…”

Section: Discussionmentioning

confidence: 99%

Transmodulation between Phospholipase D and c-Src Enhances Cell Proliferation

Ahn

Kim

et al. 2003

Molecular and Cellular Biology

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Section: Discussionmentioning

confidence: 99%

Transmodulation between Phospholipase D and c-Src Enhances Cell Proliferation

Ahn

Kim

et al. 2003

Molecular and Cellular Biology

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“…Regulation of total PLD activity in cell homogenates by tyrosyl phosphorylation has been previously documented [15][16][17][18]. In HL-60 granulocytes, the isoform PLD1 is tyrosyl phosphorylated in response to peroxides of vanadate [19].…”

Section: Introductionmentioning

confidence: 91%

The uncovering of a novel regulatory mechanism for PLD2: Formation of a ternary complex with protein tyrosine phosphatase PTP1B and growth factor receptor-bound protein GRB2

Horn¹,

López²,

Miller³

et al. 2005

Biochemical and Biophysical Research Communications

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The regulation of PLD2 activation is poorly understood at present. Transient transfection of COS-7 with a mycPLD2 construct results in elevated levels of PLD2 enzymatic activity and tyrosyl phosphorylation. To investigate whether this phosphorylation affects PLD2 enzymatic activity, anti-myc immunoprecipitates were treated with recombinant protein tyrosine phosphatase PTP1B. Surprisingly, lipase activity and PY levels both increased over a range of PTP1B concentrations. These increases occurred in parallel to a measurable PTP1B-associated phosphatase activity. Inhibitor studies demonstrated that an EGF-receptor type kinase is involved in phosphorylation. In a COS-7 cell line created in the laboratory that stably expressed myc-PLD2, PTP1B induced a robust (>6-fold) augmentation of myc-PLD2 phosphotyrosine content. The addition of growth factor receptor-bound protein 2 (Grb2) to cell extracts also elevated PY levels of myc-PLD (>10-fold). Systematic co-immunoprecipitation-immunoblotting experiments pointed at a physical association between PLD2, Grb2 and PTP1B in both physiological conditions and in overexpressed cells. This is the first report of a demonstration of the mammalian isoform PLD2 existing in a ternary complex with a protein tyrosine phosphatase, PTP1b, and the docking protein Grb2 which greatly enhances tyrosyl phosphorylation of the lipase.

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“…Many growth factors for receptor tyrosine kinases, including the epidermal growth factor (EGF), platelet-derived growth factor (PDGF), v-Src, fibroblast growth factor (FGF), and insulin-like growth factor (IGF), have been shown to activate PLD activity [9][10][11][12][13][14]. Activation of non-receptor tyrosine kinase v-Src has also been shown to activate PLD activity [15].…”

Section: Introductionmentioning

confidence: 99%