Caveolin 2
Caveolin-2 is a protein that in humans is encoded by the CAV2 gene.[1][2][3]
The protein encoded by this gene is a major component of the inner surface of caveolae, small invaginations of the plasma membrane, and is involved in essential cellular functions, including signal transduction, lipid metabolism, cellular growth control and apoptosis. This protein may function as a tumor suppressor. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. Two transcript variants encoding distinct isoforms have been identified for this gene. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by one transcript.[3]
Interactions
Caveolin 2 has been shown to interact with Caveolin 1[4][5] and RAS p21 protein activator 1.[6]
References
- ^ Scherer PE, Okamoto T, Chun M, Nishimoto I, Lodish HF, Lisanti MP (Feb 1996). "Identification, sequence, and expression of caveolin-2 defines a caveolin gene family". Proc Natl Acad Sci U S A 93 (1): 131–5. doi:10.1073/pnas.93.1.131. PMC 40192. PMID 8552590. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=40192.
- ^ Fra AM, Mastroianni N, Mancini M, Pasqualetto E, Sitia R (May 1999). "Human caveolin-1 and caveolin-2 are closely linked genes colocalized with WI-5336 in a region of 7q31 frequently deleted in tumors". Genomics 56 (3): 355–6. doi:10.1006/geno.1998.5723. PMID 10087206.
- ^ a b "Entrez Gene: CAV2 caveolin 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=858.
- ^ Breuza, Lionel; Corby Séverine, Arsanto Jean-Pierre, Delgrossi Marie-Hélène, Scheiffele Peter, Le Bivic André (Dec. 2002). "The scaffolding domain of caveolin 2 is responsible for its Golgi localization in Caco-2 cells". J. Cell. Sci. (England) 115 (Pt 23): 4457–67. doi:10.1242/jcs.00130. ISSN 0021-9533. PMID 12414992.
- ^ Scherer, P E; Lewis R Y, Volonte D, Engelman J A, Galbiati F, Couet J, Kohtz D S, van Donselaar E, Peters P, Lisanti M P (Nov. 1997). "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo". J. Biol. Chem. (UNITED STATES) 272 (46): 29337–46. doi:10.1074/jbc.272.46.29337. ISSN 0021-9258. PMID 9361015.
- ^ Lee, Hyangkyu; Park David S, Wang Xiao Bo, Scherer Philipp E, Schwartz Phillip E, Lisanti Michael P (Sep. 2002). "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1". J. Biol. Chem. (United States) 277 (37): 34556–67. doi:10.1074/jbc.M204367200. ISSN 0021-9258. PMID 12091389.
Further reading
- Engelman JA, Zhang X, Galbiati F, et al. (1999). "Molecular genetics of the caveolin gene family: implications for human cancers, diabetes, Alzheimer disease, and muscular dystrophy.". Am. J. Hum. Genet. 63 (6): 1578–87. doi:10.1086/302172. PMC 1377628. PMID 9837809. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1377628.
- Glenney JR (1992). "The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles.". FEBS Lett. 314 (1): 45–8. doi:10.1016/0014-5793(92)81458-X. PMID 1360410.
- Murata M, Peränen J, Schreiner R, et al. (1995). "VIP21/caveolin is a cholesterol-binding protein.". Proc. Natl. Acad. Sci. U.S.A. 92 (22): 10339–43. doi:10.1073/pnas.92.22.10339. PMC 40792. PMID 7479780. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=40792.
- Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, et al. (1995). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening.". Genomics 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID 7829101.
- Scherer PE, Lewis RY, Volonte D, et al. (1997). "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo.". J. Biol. Chem. 272 (46): 29337–46. doi:10.1074/jbc.272.46.29337. PMID 9361015.
- Galbiati F, Volonte D, Gil O, et al. (1998). "Expression of caveolin-1 and -2 in differentiating PC12 cells and dorsal root ganglion neurons: caveolin-2 is up-regulated in response to cell injury.". Proc. Natl. Acad. Sci. U.S.A. 95 (17): 10257–62. doi:10.1073/pnas.95.17.10257. PMC 21495. PMID 9707634. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21495.
- Engelman JA, Zhang XL, Lisanti MP (1998). "Genes encoding human caveolin-1 and -2 are co-localized to the D7S522 locus (7q31.1), a known fragile site (FRA7G) that is frequently deleted in human cancers.". FEBS Lett. 436 (3): 403–10. doi:10.1016/S0014-5793(98)01134-X. PMID 9801158.
- Volonte D, Galbiati F, Li S, et al. (1999). "Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe.". J. Biol. Chem. 274 (18): 12702–9. doi:10.1074/jbc.274.18.12702. PMID 10212252.
- Engelman JA, Zhang XL, Lisanti MP (1999). "Sequence and detailed organization of the human caveolin-1 and -2 genes located near the D7S522 locus (7q31.1). Methylation of a CpG island in the 5' promoter region of the caveolin-1 gene in human breast cancer cell lines.". FEBS Lett. 448 (2-3): 221–30. doi:10.1016/S0014-5793(99)00365-8. PMID 10218480.
- Mora R, Bonilha VL, Marmorstein A, et al. (1999). "Caveolin-2 localizes to the golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1.". J. Biol. Chem. 274 (36): 25708–17. doi:10.1074/jbc.274.36.25708. PMID 10464308.
- Fra AM, Pasqualetto E, Mancini M, Sitia R (2000). "Genomic organization and transcriptional analysis of the human genes coding for caveolin-1 and caveolin-2.". Gene 243 (1-2): 75–83. doi:10.1016/S0378-1119(99)00559-4. PMID 10675615.
- Schwab W, Kasper M, Gavlik JM, et al. (2000). "Characterization of caveolins from human knee joint catilage: expression of caveolin-1, -2, and -3 in chondrocytes and association with integrin beta1.". Histochem. Cell Biol. 113 (3): 221–5. doi:10.1007/s004180050441. PMID 10817676.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310948.
- Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1083732.
- de Marco MC, Kremer L, Albar JP, et al. (2001). "BENE, a novel raft-associated protein of the MAL proteolipid family, interacts with caveolin-1 in human endothelial-like ECV304 cells.". J. Biol. Chem. 276 (25): 23009–17. doi:10.1074/jbc.M009739200. PMID 11294831.
- Andoh A, Saotome T, Sato H, et al. (2002). "Epithelial expression of caveolin-2, but not caveolin-1, is enhanced in the inflamed mucosa of patients with ulcerative colitis.". Inflamm. Bowel Dis. 7 (3): 210–4. doi:10.1097/00054725-200108000-00005. PMID 11515846.
- Xu XR, Huang J, Xu ZG, et al. (2002). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver.". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089–94. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=64988.
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SNAP25 · SNAP29
Syntaxin (STX1A, STX1B, STX2, STX3, STX4, STX5, STX6, STX7, STX8, STX10, STX11, STX12, STX16, STX17, STX18, STX19)
Munc-18: STXBP1 · STXBP2 · STXBP3 · STXBP4 · STXBP5 · STXBP6
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Other
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| COPI |
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| COPII |
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| RME/Clathrin |
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| Caveolae |
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| Other/ungrouped |
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see also vesicular transport protein disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr
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