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Vol. 12, Issue 4, 943-955, April 2001
and
*Department of Developmental and Molecular Biology,
§Anatomy and Structural Biology, Albert Einstein College
of Medicine, Bronx, New York 10461; Phospholipase D (PLD) hydrolyzes phosphatidylcholine to generate
phosphatidic acid. In mammalian cells this reaction has been implicated
in the recruitment of coatomer to Golgi membranes and release of
nascent secretory vesicles from the trans-Golgi network. These observations suggest that PLD is associated with the Golgi complex; however, to date, because of its low abundance, the
intracellular localization of PLD has been characterized only
indirectly through overexpression of chimeric proteins. We have used
highly sensitive antibodies to PLD1 together with immunofluorescence
and immunogold electron microscopy as well as cell fractionation to
identify the intracellular localization of endogenous PLD1 in several
cell types. Although PLD1 had a diffuse staining pattern, it was
enriched significantly in the Golgi apparatus and was also present in
cell nuclei. On fragmentation of the Golgi apparatus by treatment with nocodazole, PLD1 closely associated with membrane fragments, whereas after inhibition of PA synthesis, PLD1 dissociated from the membranes. Overexpression of an hemagglutinin-tagged form of PLD1 resulted in displacement of the endogenous enzyme from its perinuclear localization to large vesicular structures. Surprisingly, when the
Golgi apparatus collapsed in response to brefeldin A, the nuclear
localization of PLD1 was enhanced significantly. Our data show that the
intracellular localization of PLD1 is consistent with a role in vesicle
trafficking from the Golgi apparatus and suggest that it also functions
in the cell nucleus.
Centre de Recherche
en Rhumatologie et Immunologie, Centre de Recherche du CHUL, Ste-Foy,
Quebec, Canada; and Department of Pharmacology and
Center for Developmental Genetics, State University of New York at
Stony Brook, Stony Brook, New York 11794
Corresponding author. E-mail address:
shields{at}aecom.yu.edu.
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