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J. Biol. Chem., Vol. 275, Issue 43, 33379-33387, October 27, 2000
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From the Hormones and growth factors induce in many cell
types the production of phosphatidic acid (PA), which has been proposed
to play a role as a second messenger. We have previously shown in an
acellular system that PA selectively stimulates certain isoforms of
type 4 cAMP-phosphodiesterases (PDE4). Here we studied the effect of
endogenous PA on PDE activity of transiently transfected MA10 cells
overexpressing the PA-sensitive isoform PDE4D3. Cell treatment with
inhibitors of PA degradation, including propranolol, induced an
accumulation of endogenous PA accompanied by a stimulation of PDE
activity and a significant decrease in both cAMP levels and protein
kinase A activity. Furthermore, in FRTL5 cells, which natively express
PDE4D3, pretreatment with compounds inducing PA accumulation prevented
both cAMP increase and cAMP-responsive element-binding protein
phosphorylation triggered by thyroid-stimulating hormone. To
determine the mechanism of PDE stimulation by PA, endogenous
phospholipids were labeled by preincubating MA10 cells overexpressing
PDE4D3 with [32P]orthophosphate. Immuno-
precipitation experiments showed that PA was specifically bound to
PDE4D3, supporting the hypothesis that PDE4D3 activation occurs through
direct binding of PA to the protein. PA binding site on PDE4D3 was
characterized by engineering deletions of selected regions in the
N-terminal regulatory domain of the enzyme. Deletion of amino acid
residues 31-59 suppressed both PA-activating effect and PA binding,
suggesting that this region rich in basic and hydrophobic residues
contains the PA binding site. These observations strongly suggest that
endogenous PA can modulate cAMP levels in intact cells, through a
direct activation of PDE4D3.
The cAMP-specific Phosphodiesterase PDE4D3 Is Regulated by
Phosphatidic Acid Binding
CONSEQUENCES FOR cAMP SIGNALING PATHWAY AND CHARACTERIZATION OF
A PHOSPHATIDIC ACID BINDING SITE*
,
,,, and**
Institut National de la Santé et de la
Recherche Médicale Unité 352, Biochemistry and Pharmacology
Laboratory, INSA-Lyon, 69621 Villeurbanne, France, the
§ Department of Public Health and Cell Biology, University
of Rome-Tor Vergata, 00173 Italy, the ¶ Department of
Histology and Medical Embryology, University of Rome-La Sapienza, 00161 Italy, and the Division of Human Reproduction, Stanford
University Medical Center, Stanford, California 94305
*
This work was supported by the Institut National de la
Santé et de la Recherche Médicale (INSERM, France) and by a
joint grant from the Consiglio Nazionale delle Ricerche (Italy) and INSERM.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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