Regulation of phosphatidic acid phosphohydrolase by epidermal growth factor: Reduced association with the EGF receptor followed by increased association with protein kinase Cε

Youwei Jiang, Zhimin Lu, Qun Zang, David A. Foster

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26 Citations (Scopus)

Abstract

An important component of receptor-mediated intracellular signal transduction is the generation of lipid second messengers. Lipid second messenger production is a complex process involving a variety of regulatory enzymes that control the intracellular response to the extracellular signal. Phosphatidic acid (PA) is generated in response to phospholipase D and can be converted to other lipid second messengers including diacylglycerol (DG) and lysophosphatidic acid. PA is converted to DG by PA phosphohydrolase (PAP). We report here that PAP activity can be detected in epidermal growth factor (EGF) receptor immunoprecipitates. Following treatment with EGF, there is a substantial reduction in the PAP activity that co-precipitates with the EGF receptor. The loss of EGF receptor-associated PAP activity occurs with a concomitant increase in PAP activity associated with the ε isoform of protein kinase C (PKC). The PAP activity associated with PKCε was dependent upon the PKC co-factors phosphatidylserine and DG but was independent of the kinase activity of PKCε. These data suggest a novel signaling mechanism for the regulation of lipid second messenger production and implicate PAP as an important regulatory component for lipid second messenger production in receptor-mediated intracellular signaling.

Original languageEnglish (US)
Pages (from-to)29529-29532
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number47
DOIs
StatePublished - 1996

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Phosphatidate Phosphatase
Phosphoric Monoester Hydrolases
Epidermal Growth Factor Receptor
Epidermal Growth Factor
Protein Kinase C
Second Messenger Systems
Association reactions
Diglycerides
Lipids
Phosphatidic Acids
Phospholipase D
Signal transduction
Phosphatidylserines
Precipitates
Signal Transduction
Protein Isoforms
Phosphotransferases
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

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title = "Regulation of phosphatidic acid phosphohydrolase by epidermal growth factor: Reduced association with the EGF receptor followed by increased association with protein kinase Cε",
abstract = "An important component of receptor-mediated intracellular signal transduction is the generation of lipid second messengers. Lipid second messenger production is a complex process involving a variety of regulatory enzymes that control the intracellular response to the extracellular signal. Phosphatidic acid (PA) is generated in response to phospholipase D and can be converted to other lipid second messengers including diacylglycerol (DG) and lysophosphatidic acid. PA is converted to DG by PA phosphohydrolase (PAP). We report here that PAP activity can be detected in epidermal growth factor (EGF) receptor immunoprecipitates. Following treatment with EGF, there is a substantial reduction in the PAP activity that co-precipitates with the EGF receptor. The loss of EGF receptor-associated PAP activity occurs with a concomitant increase in PAP activity associated with the ε isoform of protein kinase C (PKC). The PAP activity associated with PKCε was dependent upon the PKC co-factors phosphatidylserine and DG but was independent of the kinase activity of PKCε. These data suggest a novel signaling mechanism for the regulation of lipid second messenger production and implicate PAP as an important regulatory component for lipid second messenger production in receptor-mediated intracellular signaling.",
author = "Youwei Jiang and Zhimin Lu and Qun Zang and Foster, {David A.}",
year = "1996",
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T1 - Regulation of phosphatidic acid phosphohydrolase by epidermal growth factor

T2 - Reduced association with the EGF receptor followed by increased association with protein kinase Cε

AU - Jiang, Youwei

AU - Lu, Zhimin

AU - Zang, Qun

AU - Foster, David A.

PY - 1996

Y1 - 1996

N2 - An important component of receptor-mediated intracellular signal transduction is the generation of lipid second messengers. Lipid second messenger production is a complex process involving a variety of regulatory enzymes that control the intracellular response to the extracellular signal. Phosphatidic acid (PA) is generated in response to phospholipase D and can be converted to other lipid second messengers including diacylglycerol (DG) and lysophosphatidic acid. PA is converted to DG by PA phosphohydrolase (PAP). We report here that PAP activity can be detected in epidermal growth factor (EGF) receptor immunoprecipitates. Following treatment with EGF, there is a substantial reduction in the PAP activity that co-precipitates with the EGF receptor. The loss of EGF receptor-associated PAP activity occurs with a concomitant increase in PAP activity associated with the ε isoform of protein kinase C (PKC). The PAP activity associated with PKCε was dependent upon the PKC co-factors phosphatidylserine and DG but was independent of the kinase activity of PKCε. These data suggest a novel signaling mechanism for the regulation of lipid second messenger production and implicate PAP as an important regulatory component for lipid second messenger production in receptor-mediated intracellular signaling.

AB - An important component of receptor-mediated intracellular signal transduction is the generation of lipid second messengers. Lipid second messenger production is a complex process involving a variety of regulatory enzymes that control the intracellular response to the extracellular signal. Phosphatidic acid (PA) is generated in response to phospholipase D and can be converted to other lipid second messengers including diacylglycerol (DG) and lysophosphatidic acid. PA is converted to DG by PA phosphohydrolase (PAP). We report here that PAP activity can be detected in epidermal growth factor (EGF) receptor immunoprecipitates. Following treatment with EGF, there is a substantial reduction in the PAP activity that co-precipitates with the EGF receptor. The loss of EGF receptor-associated PAP activity occurs with a concomitant increase in PAP activity associated with the ε isoform of protein kinase C (PKC). The PAP activity associated with PKCε was dependent upon the PKC co-factors phosphatidylserine and DG but was independent of the kinase activity of PKCε. These data suggest a novel signaling mechanism for the regulation of lipid second messenger production and implicate PAP as an important regulatory component for lipid second messenger production in receptor-mediated intracellular signaling.

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