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Phosphatidic Acid Production by Phospholipase D1 Enhances Translocation of Caveolin to a Perinuclear Compartment
Author(s) -
Stace Catherine Lucy,
Manifava Maria,
Ktistakis Nicholas T
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.lb76-b
Subject(s) - endosome , microbiology and biotechnology , caveolae , phosphatidic acid , endocytosis , golgi apparatus , brefeldin a , phospholipase d , compartment (ship) , biology , internalization , exocytosis , cellular compartment , chromosomal translocation , chemistry , biochemistry , membrane , intracellular , signal transduction , cell , phospholipid , endoplasmic reticulum , oceanography , geology , gene
Caveolae cycle between plasma membrane and the Golgi, and are distinguished from other vesicles by the presence of caveolin on their membrane. We have discovered that caveolin colocalizes with phospholipase D1 (PLD1) to a small perinuclear region upon PMA stimulation of stably‐transfected CHO cell lines inducibly expressing PLD1. Both PMA stimulation and catalytically‐active PLD1 are essential for translocation of caveolin to this compartment, indicating that production of phosphatidic acid (PA) is crucial for the response. This compartment cannot be identified as lysosomal or endosomal, and is resistant to Golgi disruption by Brefeldin A. One hypothesis consistent with these observations is that PA is an essential lipid signal for the formation of a caveosomal‐like compartment. In support of this hypothesis, we found that the glucose transporter Glut4 (which is known to internalize via the caveolar pathway) translocates from the plasma membrane to the same perinuclear compartment under similar activating conditions. On the other hand, a GPI‐linked GFP reporter does not translocate to the compartment under activating conditions. In addition, depletion of plasma membrane cholesterol has no effect on the translocation response. Experiments are in progress to determine whether the PA‐dependent caveolin translocation alters caveolar internalization of a subset of plasma membrane proteins. This work is funded by the Biotechnology and Biological Sciences Research Council (BBSRC)