Caveolin-1 and -2 in the Exocytic Pathway of MDCK Cells

doi:10.1083/jcb.140.4.795

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© The Rockefeller University Press, 0021-9525/1998//795 $5.00
The Journal of Cell Biology, Volume 140, Number 4, , 1998 795-806

Article

Caveolin-1 and -2 in the Exocytic Pathway of MDCK Cells

P. Scheiffele^*, P. Verkade^*, A.M. Fra, H. Virta^*, K. Simons^*, and E. Ikonen^*

^* Cell Biology Programme, European Molecular Biology Laboratory, D-69012 Heidelberg, Germany; and Department of Biological and Technical Research-Hospital San Raffaele, 20132 Milan, Italy

Abstract. We have studied the biosynthesis and transport ofthe endogenous caveolins in MDCK cells. We show that in additionto homooligomers of caveolin-1, heterooligomeric complexesof caveolin-1 and -2 are formed in the ER. The oligomers becomelarger, increasingly detergent insoluble, and phosphorylatedon caveolin-2 during transport to the cell surface. In the TGN caveolin-1/-2 heterooligomers are sorted into basolateralvesicles, whereas larger caveolin-1 homooligomers are targetedto the apical side. Caveolin-1 is present on both the apicaland basolateral plasma membrane, whereas caveolin-2 is enrichedon the basolateral surface where caveolae are present. Thissuggests that caveolin-1 and -2 heterooligomers are involvedin caveolar biogenesis in the basolateral plasma membrane.Anti–caveolin-1 antibodies inhibit the apical deliveryof influenza virus hemagglutinin without affecting basolateraltransport of vesicular stomatitis virus G protein. Thus, wesuggest that caveolin-1 homooligomers play a role in apicaltransport.

We thank members of the Simons lab for critical support, K.Ekroos and S. Brendel for expert technical assistance, W. Huttner(Universität Heidelberg, Heidelberg, Germany) for a criticalreading of the manuscript, K. Ashman for peptide sequencing,M. Zerial for the ${lambda}$ ZAP library, J. Lanoix for rat liver cytosol,S. Bhakdi (Universität Mainz) for the generous supply ofSLO, A. Puolasmaa (MSD-Finland) for the kind gift of lovastatin,and Anton G. Rietveld (European Molecular Biology Laboratory)for the help with cholesterol determinations.

This work was financially supported by the Academy of Finland,Commission of the European Communities, Theleton, and SFB 352.

E. Ikonen's present address is Dept. of Biochemistry, NationalPublic Health Institute, Mannerheimintie 166, FIN-00300 Helsinki,Finland.

Address all correspondence to K. Simons, Cell Biology Programme, European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach10 2209, D-69012 Heidelberg, Germany. Tel.: (49) 622-138-7334.Fax: (49) 622-138-7512.

1. Abbreviations used in this paper: 2D, two-dimensional; HA,influenza virus hemagglutinin; SLO, streptolysin-O; VSV-G,vesicular stomatitis virus glycoprotein.

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