Caveolin-1 and-2 in the exocytic pathway of MDCK cells
The Journal of cell biology, 1998•rupress.org
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 …
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 …
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.
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