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Vol. 9, Issue 7, 1773-1786, July 1998
Département de Pathologie et Biologie Cellulaire,
Université de Montréal, Montréal, Québec,
Canada H3C 3J7
Autocrine motility factor receptor (AMF-R) is a cell surface
receptor that is also localized to a smooth subdomain of the endoplasmic reticulum, the AMF-R tubule. By postembedding
immunoelectron microscopy, AMF-R concentrates within smooth
plasmalemmal vesicles or caveolae in both NIH-3T3 fibroblasts and HeLa
cells. By confocal microscopy, cell surface AMF-R labeled by the
addition of anti-AMF-R antibody to viable cells at 4°C exhibits
partial colocalization with caveolin, confirming the localization of
cell surface AMF-R to caveolae. Labeling of cell surface AMF-R by
either anti-AMF-R antibody or biotinylated AMF (bAMF) exhibits
extensive colocalization and after a pulse of 1-2 h at 37°C, bAMF
accumulates in densely labeled perinuclear structures as well as
fainter tubular structures that colocalize with AMF-R tubules. After a
subsequent 2- to 4-h chase, bAMF is localized predominantly to AMF-R
tubules. Cytoplasmic acidification, blocking clathrin-mediated
endocytosis, results in the essentially exclusive distribution of
internalized bAMF to AMF-R tubules. By confocal microscopy, the tubular
structures labeled by internalized bAMF show complete colocalization
with AMF-R tubules. bAMF internalized in the presence of a 10-fold excess of unlabeled AMF labels perinuclear punctate structures, which
are therefore the product of fluid phase endocytosis, but does not
label AMF-R tubules, demonstrating that bAMF targeting to AMF-R tubules
occurs via a receptor-mediated pathway. By electron microscopy, bAMF
internalized for 10 min is located to cell surface caveolae and after
30 min is present within smooth and rough endoplasmic reticulum
tubules. AMF-R is therefore internalized via a receptor-mediated clathrin-independent pathway to smooth ER. The steady state
localization of AMF-R to caveolae implicates these cell surface
invaginations in AMF-R endocytosis.
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