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J. Cell Biol.,
Volume 140, Number 4, February 23, 1998 795-806

* Cell Biology Programme, European Molecular Biology Laboratory, D-69012 Heidelberg, Germany; and Abstract. We have studied the biosynthesis and transport of the endogenous caveolins in MDCK cells. We
show that in addition to homooligomers of caveolin-1,
heterooligomeric complexes of caveolin-1 and -2 are
formed in the ER. The oligomers become larger, increasingly detergent insoluble, and phosphorylated on
caveolin-2 during transport to the cell surface. In the
TGN caveolin-1/-2 heterooligomers are sorted into basolateral vesicles, whereas larger caveolin-1 homooligomers are targeted to the apical side. Caveolin-1 is
present on both the apical and basolateral plasma membrane, whereas caveolin-2 is enriched on the basolateral surface where caveolae are present. This suggests that caveolin-1 and -2 heterooligomers are involved in caveolar biogenesis in the basolateral plasma
membrane. Anti-caveolin-1 antibodies inhibit the apical delivery of influenza virus hemagglutinin without
affecting basolateral transport of vesicular stomatitis virus G protein. Thus, we suggest that caveolin-1 homooligomers play a role in apical transport.
Department of
Biological and Technical Research-Hospital San Raffaele, 20132 Milan, Italy
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