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Published 29 August 2005. doi:10.1083/jcb.200506103
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 5, 769-779
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Article

 Assembly and trafficking of caveolar domains in the cell : caveolae as stable, cargo-triggered, vesicular transporters



Akiko Tagawa1, Anna Mezzacasa1, Arnold Hayer1, Andrea Longatti1, Lucas Pelkmans2, and Ari Helenius1

1 Swiss Federal Institute of Technology (ETH) Zürich, ETH-Hönggerberg, 8093 Zürich, Switzerland
2 Max Planck Institute for Molecular Cell Biology and Genetics, 01307 Dresden, Germany

Correspondence to Ari Helenius: ari.helenius{at}bc.biol.ethz.ch

Using total internal reflection fluorescence microscopy (TIR-FM), fluorescence recovery after photobleaching (FRAP), and other light microscopy techniques, we analyzed the dynamics, the activation, and the assembly of caveolae labeled with fluorescently tagged caveolin-1 (Cav1). We found that when activated by simian virus 40 (SV40), a nonenveloped DNA virus that uses caveolae for cell entry, the fraction of mobile caveolae was dramatically enhanced both in the plasma membrane (PM) and in the caveosome, an intracellular organelle that functions as an intermediate station in caveolar endocytosis. Activation also resulted in increased microtubule (MT)-dependent, long-range movement of caveolar vesicles. We generated heterokaryons that contained GFP- and RFP-tagged caveolae by fusing cells expressing Cav1-GFP and -RFP, respectively, and showed that even when activated, individual caveolar domains underwent little exchange of Cav1. Only when the cells were subjected to transient cholesterol depletion, did the caveolae domain exchange Cav1. Thus, in contrast to clathrin-, or other types of coated transport vesicles, caveolae constitute stable, cholesterol-dependent membrane domains that can serve as fixed containers through vesicle traffic. Finally, we identified the Golgi complex as the site where newly assembled caveolar domains appeared first.

A. Tagawa and A. Mezzacasa contributed equally to this work.

Abbreviations used in this paper: Cav1, caveolin-1; CHX, cycloheximide; latA, latrunculin A; MOI, multiplicity of infection; MT, microtubule; MyrPalm, myristoylated-palmitoylated; PEG, polyethylene glycol; PM, plasma membrane; SFV, Semliki Forest virus; TIR-FM, total internal reflection fluorescence microscopy; VSVG, vesicular stomatitis virus G-protein.


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