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Oligomeric structure of caveolin: implications for caveolae membrane organization.
Open accessAbstract
A 22-kDa protein, caveolin, is localized to the cytoplasmic surface of plasma membrane specializations called caveolae. We have proposed that caveolin may function as a scaffolding protein to organize and concentrate signaling molecules within caveolae. Here, we show that caveolin interacts with itself to form homooligomers. Electron microscopic visualization of these purified caveolin homooligomers demonstrates that they appear as individual spherical particles. By using recombinant expression of caveolin as a glutathione S-transferase fusion protein, we have defined a region of caveolin's cytoplasmic N-terminal domain that mediates these caveolin-caveolin interactions. We suggest that caveolin homooligomers may function to concentrate caveolin-interacting molecules within caveolae. In this regard, it may be useful to think of caveolin homooligomers as "fishing lures" with multiple "hooks" or attachment sites for caveolin-interacting molecules.
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Cited by
Doherty, G. J., & McMahon, H. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081307.110540 · Cited by 3,075
Identification, sequence, and expression of caveolin-2 defines a caveolin gene family.
Scherer, P. E., Okamoto, T., Chun, M., Nishimoto, I., Lodish, H. F., & Lisanti, M. P. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.131 · Cited by 561
Self-citationCaveolae-deficient Endothelial Cells Show Defects in the Uptake and Transport of Albumin in Vivo
Schubert, W., Frank, P. G., Razani, B., Park, D. S., Chow, C.-W., & Lisanti, M. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100613200 · Cited by 337
Self-citationPol, A., Luetterforst, R., Lindsay, M., Heino, S., Ikonen, E., & Parton, R. G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.5.1057 · Cited by 326
Ritz, D., Vuk, M., Kirchner, P., Bug, M., Schütz, S., Hayer, A., Bremer, S., Lusk, C., Baloh, R. H., Lee, H., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2301 · Cited by 224
Metadata
- Authors
- Sargiacomo, M., Scherer, P. E., Tang, Z., Kübler, E., Song, K. S., Sanders, M. C., & Lisanti, M. P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1995-09-26
- Volume
- 92
- Issue
- 20
- Pages
- 9407-9411
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1995150314
- Cited by
- 548
- References
- 0
- FWCI
- 8.78
- Type
- journal article
- Language
- en
- Open access
- green
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- Sargiacomo, M., Scherer, P. E., Tang, Z., Kübler, E., Song, K. S., Sanders, M. C., & Lisanti, M. P. (1995). Oligomeric structure of caveolin: implications for caveolae membrane organization. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.92.20.9407
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