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Vol. 13, Issue 5, 1582-1593, May 2002
and
*Medical Research Council Laboratory for Molecular Cell Biology,
Cell Biology Unit, and Department of Biochemistry and Molecular
Biology, University College London, London WC1E 6BT, United Kingdom;
von Willebrand factor (vWF) is a large, multimeric protein
secreted by endothelial cells and involved in hemostasis. When expressed in AtT-20 cells, vWF leads to the de novo formation of
cigar-shaped organelles similar in appearance to the Weibel-Palade bodies of endothelial cells in which vWF is normally stored before regulated secretion. The membranes of this vWF-induced organelle, termed the pseudogranule, are uncharacterized. We have examined the
ability of these pseudogranules, which we show are secretagogue responsive, to recruit membrane proteins. Coexpression experiments show
that the Weibel-Palade body proteins P-selectin and CD63, as
well as the secretory organelle membrane proteins vesicle-associated membrane protein-2 and synaptotagmin I are diverted away from the
endogenous adrenocorticotropic hormone-containing secretory granules to
the vWF-containing pseudogranules. However, transferrin receptor,
lysosomal-associated membrane protein 1, and sialyl transferase are not
recruited. The recruitment of P-selectin is dependent on a
tyrosine-based motif within its cytoplasmic domain. Our data show that
vWF pseudogranules specifically recruit a subset of membrane proteins,
and that in a process explicitly driven by the pseudogranule content
(i.e., vWF), the active recruitment of at least one component of the
pseudogranule membrane (i.e., P-selectin) is dependent on residues of
P-selectin that are cytosolic and therefore unable to directly interact
with vWF.
Vollum Institute L-474, Oregon Health Sciences
University, Portland, Oregon; and Academic Unit of
Neurology, Division of Genomic Medicine, Medical School, University of
Sheffield, Sheffield, S10 2RX, United Kingdom
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