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Blood, Vol. 95 No. 3 (February 1), 2000:
pp. 1078-1085
Phosphatidylinositide 3-kinase localizes to cytoplasmic lipid
bodies in human polymorphonuclear leukocytes and other myeloid-derived
cells
Wengui Yu,
Jessica Cassara, and
Peter F. Weller
From Harvard Thorndike Laboratories and the Departments of Medicine,
Beth Israel Deaconess Medical Center, Harvard Medical School, Boston,
MA.
Phosphatidylinositide 3-kinase (PI3K) is a key enzyme implicated in
intracellular signaling of diverse cellular responses including
receptor-mediated responses and neutrophil activation. Several PI3K
subunits have been cloned and shown to be localized to plasma membrane
receptors, the cytosol, or intracellular vesicles or caveolae. We
report the localization of PI3K to a distinct intracellular site,
cytoplasmic lipid bodies, in leukocytes. In U937 monocyte cells, PI3K
p85 regulatory and p110 catalytic subunits were localized to lipid
bodies by immunocytochemistry and/or immunoblotting and enzyme assays
of subcellular fractions. In RAW murine macrophages, p55, p85 , and
p85 PI3K subunits were present at isolated lipid bodies. PI3K p85
was also shown to colocalize and, by co-immunoprecipitation, to be
physically associated with phosphorylated Lyn kinase in lipid bodies
induced to form in human polymorphonuclear leukocytes. These findings,
therefore, indicate a novel site for PI3K compartmentalization and
suggest that PI3K-mediated signaling is active within cytoplasmic lipid
bodies in leukocytes.
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