Regulated internalization of caveolae

Parton, R. G., Joggerst, B. and Simons, K. (1994) Regulated internalization of caveolae. Journal of Cell Biology, 127 5: 1199-1215. doi:10.1083/jcb.127.5.1199

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Author Parton, R. G.
Joggerst, B.
Simons, K.
Title Regulated internalization of caveolae
Journal name Journal of Cell Biology   Check publisher's open access policy
ISSN 0021-9525
1540-8140
Publication date 1994-12-01
Year available 1994
Sub-type Article (original research)
DOI 10.1083/jcb.127.5.1199
Open Access Status File (Publisher version)
Volume 127
Issue 5
Start page 1199
End page 1215
Total pages 17
Place of publication New York, NY, United States
Publisher Rockefeller University Press
Language eng
Abstract Caveolae are specialized invaginations of the plasma membrane which have been proposed to play a role in diverse cellular processes such as endocytosis and signal transduction. We have developed an assay to determine the fraction of internal versus plasma membrane caveolae. The GPI-anchored protein, alkaline phosphatase, was clustered in caveolae after antibody-induced crosslinking at low temperature and then, after various treatments, the relative amount of alkaline phosphatase on the cell surface was determined. Using this assay we were able to show a time- and temperature-dependent decrease in cell-surface alkaline phosphatase activity which was dependent on antibody-induced clustering. The decrease in cell surface alkaline phosphatase activity was greatly accelerated by the phosphatase inhibitor, okadaic acid, but not by a protein kinase C activator. Internalization of clustered alkaline phosphatase in the presence or absence of okadaic acid was blocked by cytochalasin D and by the kinase inhibitor staurosporine. Electron microscopy confirmed that okadaic acid induced removal of caveolae from the cell surface. In the presence of hypertonic medium this was followed by the redistribution of groups of caveolae to the center of the cell close to the microtubule-organizing center. This process was reversible, blocked by cytochalasin D, and the centralization of the caveolar clusters was shown to be dependent on an intact microtubule network. Although the exact mechanism of internalization remains unknown, the results show that caveolae are dynamic structures which can be internalized into the cell. This process may be regulated by kinase activity and require an intact actin network.
Keyword Rous-sarcoma virus
Capillary endothelium
Okadaic acid
Plasmalemmal vesicles
Endocytic pathway
Epithelial-cells
Cholera toxin
Membrane
Receptor
Transport
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
 
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