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A more recent version of this article appeared on November 1, 2002
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Submitted on April 22, 2002
Revised on August 20, 2002
Accepted on August 22, 2002
1 Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York 10461
2 Centre de Recherche en Rhumatologie et Immunologie,
Centre de Recherche du CHUL, Ste-Foy Quebec, Canada
3 Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461
* Corresponding author. E-mail address: shields{at}aecom.yu.edu.
Phospholipase D (PLD) hydrolyzes phosphatidylcholine to generate phosphatidic acid, a molecule known to have multiple physiological roles including release of nascent secretory vesicles from the trans-Golgi network. In mammalian cells two forms of the enzyme, PLD1 and -2 have been described. We recently demonstrated that PLD1 is localized to the Golgi apparatus, nuclei and to a lesser extent, plasma membrane. Due to its low abundance, the intracellular localization of PLD2 has been characterized only indirectly through overexpression of chimeric proteins. Using antibodies specific to PLD2, together with immunofluorescence microscopy, here we demonstrate that a significant fraction of endogenous PLD2 localized to the perinuclear Golgi region and was also distributed throughout cells in dense cytoplasmic puncta; a fraction of which co-localized with caveolin-1 and the plasma membrane. Upon treatment with brefeldin A, PLD2 translocated into the nucleus in a manner similar to PLD1 suggesting a potential role in nuclear signaling. Most significantly, cryo-immunogold electron microscopy demonstrated that in pituitary GH3 cells greater than 90% of PLD2 present in the Golgi apparatus was localized to cisternal rims and peri-Golgi vesicles exclusively. The data are consistent with a model whereby PLD2 plays a role in Golgi vesicular transport.
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