The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
A Critical Role of Cavin (Polymerase I and Transcript Release Factor) in Caveolae Formation and Organization
Open accessAbstract
Cavin (PTRF) has been shown to be a highly abundant protein component of caveolae, but its functional role there is unknown. Here, we confirm that cavin co-localizes with caveolin-1 in adipocytes by confocal microscopy and co-distributes with caveolin-1 in lipid raft fractions by sucrose gradient flotation. However, cavin does not directly associate with caveolin-1 as solubilization of caveolae disrupts their interaction. Cholesterol depletion with beta-cyclodextrin causes a significant down-regulation of cavin from plasma membrane lipid raft fractions. Overexpression of cavin in HEK293-Cav-1 cells and knockdown of cavin in 3T3-L1 adipocytes enhances and diminishes caveolin-1 levels, respectively, indicating an important role for cavin in maintaining the level of caveolin-1. A truncated form of cavin, eGFP-cavin-1-322, which lacks 74 amino acids from the C-terminal, reveals a microtubular network localization by confocal microscopy. Disruption of cytoskeletal elements with latrunculin B or nocodazole diminishes cavin expression without affecting the caveolin-1 amount. We propose that the presence of cavin on the inside surface of caveolae stabilizes these structures, probably through interaction with the cytoskeleton, and cavin therefore plays an important role in caveolae formation and organization.
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Caveolin, a protein component of caveolae membrane coats
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Loss of Caveolae, Vascular Dysfunction, and Pulmonary Defects in Caveolin-1 Gene-Disrupted Mice
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Caveolins, Liquid-Ordered Domains, and Signal Transduction
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THE FINE STRUCTURE OF THE GALL BLADDER EPITHELIUM OF THE MOUSE
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Cited by
Klaassen, I., Van Noorden, C. J. F., & Schlingemann, R. O. (2013) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2013.02.001 · Cited by 722
Scheller, E. L., Doucette, C. R., Learman, B. S., Cawthorn, W. P., Khandaker, S., Schell, B., Wu, B., Ding, S.-Y., Bredella, M. A., Fazeli, P. K., et al. (2015) · Nature Communications · doi:10.1038/ncomms8808 · Cited by 433
Self-citationMechanisms Shaping the Membranes of Cellular Organelles
Shibata, Y., Hu, J., Kozlov, M. M., & Rapoport, T. A. (2009) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.042308.113324 · Cited by 428
Endocytosis and signaling: Cell logistics shape the eukaryotic cell plan
Sigismund, S., Confalonieri, S., Ciliberto, A., Polo, S., Scita, G., & Di Fiore, P. P. (2012) · Physiological Reviews · doi:10.1152/physrev.00005.2011 · Cited by 338
Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
Lajoie, P., Goetz, J. G., Dennis, J. W., & Nabi, I. R. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200811059 · Cited by 344
Metadata
- Authors
- Liu, L., & Pilch, P. F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-02
- Volume
- 283
- Issue
- 7
- Pages
- 4314-4322
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1976081253
- Cited by
- 274
- References
- 57
- FWCI
- 6.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
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