Caveolin 1
Caveolin-1 is a protein that in humans is encoded by the CAV1 gene.[1]
The scaffolding protein encoded by this gene is the main component of the caveolae plasma membranes found in most cell types. The protein links integrin subunits to the tyrosine kinase FYN, an initiating step in coupling integrins to the Ras-ERK pathway and promoting cell cycle progression. The gene is a tumor suppressor gene candidate and a negative regulator of the Ras-p42/44 MAP kinase cascade. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by a single transcript from this gene.[2]
Interactions
Caveolin 1 has been shown to interact with TGF beta receptor 1,[3] Endothelial NOS,[4] Androgen receptor,[5] Amyloid precursor protein,[6] Gap junction protein, alpha 1,[7] Nitric oxide synthase 2A,[8] Epidermal growth factor receptor,[9] Endothelin receptor type B,[10] PDGFRB,[11] PDGFRA,[11] PTGS2,[12] TRAF2,[13][14] Estrogen receptor alpha,[15] Caveolin 2,[16][17] PLD2,[18][19] Bruton's tyrosine kinase[20] and SCP2.[21]
See also
References
- ^ 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.
- ^ "Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=857.
- ^ Razani, B; Zhang X L, Bitzer M, von Gersdorff G, Böttinger E P, Lisanti M P (Mar. 2001). "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor". J. Biol. Chem. (United States) 276 (9): 6727–38. doi:10.1074/jbc.M008340200. ISSN 0021-9258. PMID 11102446.
- ^ García-Cardeña, G; Fan R, Stern D F, Liu J, Sessa W C (Nov. 1996). "Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1". J. Biol. Chem. (UNITED STATES) 271 (44): 27237–40. doi:10.1074/jbc.271.44.27237. ISSN 0021-9258. PMID 8910295.
- ^ Lu, M L; Schneider M C, Zheng Y, Zhang X, Richie J P (Apr. 2001). "Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation". J. Biol. Chem. (United States) 276 (16): 13442–51. doi:10.1074/jbc.M006598200. ISSN 0021-9258. PMID 11278309.
- ^ Ikezu, T; Trapp B D, Song K S, Schlegel A, Lisanti M P, Okamoto T (Apr. 1998). "Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein". J. Biol. Chem. (UNITED STATES) 273 (17): 10485–95. doi:10.1074/jbc.273.17.10485. ISSN 0021-9258. PMID 9553108.
- ^ Schubert, Anne-Lane; Schubert William, Spray David C, Lisanti Michael P (May. 2002). "Connexin family members target to lipid raft domains and interact with caveolin-1". Biochemistry (United States) 41 (18): 5754–64. doi:10.1021/bi0121656. ISSN 0006-2960. PMID 11980479.
- ^ Felley-Bosco, E; Bender F C, Courjault-Gautier F, Bron C, Quest A F (Dec. 2000). "Caveolin-1 down-regulates inducible nitric oxide synthase via the proteasome pathway in human colon carcinoma cells". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (26): 14334–9. doi:10.1073/pnas.250406797. ISSN 0027-8424. PMC 18919. PMID 11114180. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=18919.
- ^ Couet, J; Sargiacomo M, Lisanti M P (Nov. 1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities". J. Biol. Chem. (UNITED STATES) 272 (48): 30429–38. doi:10.1074/jbc.272.48.30429. ISSN 0021-9258. PMID 9374534.
- ^ Yamaguchi, Tomohiro; Murata Yasunobu, Fujiyoshi Yoshinori, Doi Tomoko (Apr. 2003). "Regulated interaction of endothelin B receptor with caveolin-1". Eur. J. Biochem. (Germany) 270 (8): 1816–27. doi:10.1046/j.1432-1033.2003.03544.x. ISSN 0014-2956. PMID 12694195.
- ^ a b Yamamoto, M; Toya Y, Jensen R A, Ishikawa Y (Mar. 1999). "Caveolin is an inhibitor of platelet-derived growth factor receptor signaling". Exp. Cell Res. (UNITED STATES) 247 (2): 380–8. doi:10.1006/excr.1998.4379. ISSN 0014-4827. PMID 10066366.
- ^ Liou, J Y; Deng W G, Gilroy D W, Shyue S K, Wu K K (Sep. 2001). "Colocalization and interaction of cyclooxygenase-2 with caveolin-1 in human fibroblasts". J. Biol. Chem. (United States) 276 (37): 34975–82. doi:10.1074/jbc.M105946200. ISSN 0021-9258. PMID 11432874.
- ^ Feng, X; Gaeta M L, Madge L A, Yang J H, Bradley J R, Pober J S (Mar. 2001). "Caveolin-1 associates with TRAF2 to form a complex that is recruited to tumor necrosis factor receptors". J. Biol. Chem. (United States) 276 (11): 8341–9. doi:10.1074/jbc.M007116200. ISSN 0021-9258. PMID 11112773.
- ^ Cao, Haiming; Courchesne William E, Mastick Cynthia Corley (Mar. 2002). "A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase". J. Biol. Chem. (United States) 277 (11): 8771–4. doi:10.1074/jbc.C100661200. ISSN 0021-9258. PMID 11805080.
- ^ Schlegel, A; Wang C, Pestell R G, Lisanti M P (Oct. 2001). "Ligand-independent activation of oestrogen receptor alpha by caveolin-1". Biochem. J. (England) 359 (Pt 1): 203–10. doi:10.1042/0264-6021:3590203. ISSN 0264-6021. PMC 1222136. PMID 11563984. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222136.
- ^ 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.
- ^ Zheng, Xiangjian; Bollinger Bollag Wendy (Dec. 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane microdomains and is downregulated upon keratinocyte differentiation". J. Invest. Dermatol. (United States) 121 (6): 1487–95. doi:10.1111/j.1523-1747.2003.12614.x. ISSN 0022-202X. PMID 14675200.
- ^ Czarny, M; Fiucci G, Lavie Y, Banno Y, Nozawa Y, Liscovitch M (Feb. 2000). "Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains". FEBS Lett. (NETHERLANDS) 467 (2–3): 326–32. doi:10.1016/S0014-5793(00)01174-1. ISSN 0014-5793. PMID 10675563.
- ^ Vargas, Leonardo; Nore Beston F, Berglof Anna, Heinonen Juhana E, Mattsson Pekka T, Smith C I Edvard, Mohamed Abdalla J (Mar. 2002). "Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx". J. Biol. Chem. (United States) 277 (11): 9351–7. doi:10.1074/jbc.M108537200. ISSN 0021-9258. PMID 11751885.
- ^ Zhou, Minglong; Parr Rebecca D, Petrescu Anca D, Payne H Ross, Atshaves Barbara P, Kier Ann B, Ball Judith M, Schroeder Friedhelm (Jun. 2004). "Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo". Biochemistry (United States) 43 (23): 7288–306. doi:10.1021/bi035914n. ISSN 0006-2960. PMID 15182174.
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.
- Razani B, Schlegel A, Liu J, Lisanti MP (2002). "Caveolin-1, a putative tumour suppressor gene". Biochem. Soc. Trans. 29 (Pt 4): 494–9. doi:10.1042/BST0290494. PMID 11498016.
- Fujimoto T, Kogo H, Nakamura N, Ozeki S (2002). "[Microdomains and caveolin]". Tanpakushitsu Kakusan Koso 47 (4 Suppl): 326–32. PMID 11915322.
- Shatz M, Liscovitch M (2004). "Caveolin-1 and cancer multidrug resistance: coordinate regulation of pro-survival proteins?". Leuk. Res. 28 (9): 907–8. doi:10.1016/j.leukres.2004.03.013. PMID 15234566.
- Frank PG, Lisanti MP (2007). "Caveolin-1 and liver regeneration: role in proliferation and lipogenesis". Cell Cycle 6 (2): 115–6. doi:10.4161/cc.6.2.3722. PMID 17314510.
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Synaptic vesicle |
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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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