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Vol. 13, Issue 11, 3930-3942, November 2002
and
§
*Departments of Developmental and Molecular Biology and
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 PLD2, 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, herein 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 colocalized with caveolin-1 and the plasma membrane. On treatment
with brefeldin A, PLD2 translocated into the nucleus in a manner
similar to PLD1, suggesting a potential role in nuclear signaling. Most
significantly, cryoimmunogold electron microscopy demonstrated that in
pituitary GH3 cells >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.
Anatomy and Structural Biology, Albert Einstein College
of Medicine, Bronx, New York 10461; and Centre de
Recherche en Rhumatologie et Immunologie, Centre de Recherche du CHUL,
Ste-Foy, Quebec, Canada G1V 4G2
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