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Vol. 12, Issue 8, 2453-2468, August 2001
*Unité Mixte de Recherche 144 Institut Curie/ Centre National
de la Recherche Scientifique, F-75248 Paris Cedex 05, France; In HeLa cells, Shiga toxin B-subunit is transported from the plasma
membrane to the endoplasmic reticulum, via early endosomes and the
Golgi apparatus, circumventing the late endocytic pathway. We describe
here that in cells derived from human monocytes, i.e., macrophages and
dendritic cells, the B-subunit was internalized in a receptor-dependent
manner, but retrograde transport to the biosynthetic/secretory pathway
did not occur and part of the internalized protein was degraded in
lysosomes. These differences correlated with the observation that the
B-subunit associated with Triton X-100-resistant membranes in HeLa
cells, but not in monocyte-derived cells, suggesting that retrograde
targeting to the biosynthetic/secretory pathway required association
with specialized microdomains of biological membranes. In agreement
with this hypothesis we found that in HeLa cells, the B-subunit
resisted extraction by Triton X-100 until its arrival in the target
compartments of the retrograde pathway, i.e., the Golgi apparatus and
the endoplasmic reticulum. Furthermore, destabilization of Triton
X-100-resistant membranes by cholesterol extraction potently inhibited
B-subunit transport from early endosomes to the
trans-Golgi network, whereas under the same conditions,
recycling of transferrin was not affected. Our data thus provide first
evidence for a role of lipid asymmetry in membrane sorting at the
interface between early endosomes and the trans-Golgi network.
Institut National de la Santé et de la
Recherche Médicale E99-08, F-67065 Strasbourg Cedex, France; and
Hospital for Sick Children, Toronto M5G 1X8, Canada
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