Caveolin 1

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Aliases CAV1, BSCL3, CGL3, LCCNS, MSTP085, PPH3, VIP21, Caveolin 1
External IDs MGI: 102709 HomoloGene: 1330 GeneCards: CAV1
RNA expression pattern
PBB GE CAV1 203065 s at tn.png

PBB GE CAV1 212097 at tn.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 7: 116.52 – 116.56 Mb Chr 6: 17.31 – 17.34 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Caveolin-1 is a protein that in humans is encoded by the CAV1 gene.[3]

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.[4]


Caveolin 1 has been shown to interact with heterotrimeric G proteins,[5] Src tyrosine kinases (Src, Lyn) and H-Ras,[6] cholesterol,[7] TGF beta receptor 1,[8] Endothelial NOS,[9] Androgen receptor,[10] Amyloid precursor protein,[11] Gap junction protein, alpha 1,[12] Nitric oxide synthase 2A,[13] Epidermal growth factor receptor,[14] Endothelin receptor type B,[15] PDGFRB,[16] PDGFRA,[16] PTGS2,[17] TRAF2,[18][19] Estrogen receptor alpha,[20] Caveolin 2,[21][22] PLD2,[23][24] Bruton's tyrosine kinase[25] and SCP2.[26] All these interactions are through a caveolin-scaffolding domain (CSD) within caveolin-1 molecule.[6] Molecules that interact with caveolin-1 contain caveolin-binding motifs (CBM).[27]

See also[edit]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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. 
  4. ^ "Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa". 
  5. ^ Li, Shengwen; Okamoto T; Chun M; Sargiacomo M; Casanova JE; Hansen SH; Nishimoto I; Lisanti MP (1995). "Evidence for a regulated interaction between heterotrimeric G proteins and caveolin". J. Biol. Chem. 270 (26): 15693–701. doi:10.1074/jbc.270.26.15693. PMID 7797570. 
  6. ^ a b Li, Shengwen; Couet J; Lisanti MP. (15 Nov 1996). "Src tyrosine kinases, Galpha subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases.". J. Biol. Chem. 271 (46): 29182–90. doi:10.1074/jbc.271.46.29182. PMID 8910575. 
  7. ^ Li, Shengwen; Song KS; Lisanti MP. (5 Jan 1996). "Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes.". J. Biol. Chem. 271 (1): 568–73. doi:10.1074/jbc.271.1.568. PMID 8550621. 
  8. ^ Razani, B; Zhang X L; Bitzer M; von Gersdorff G; Böttinger E P; Lisanti M P (March 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. 
  9. ^ García-Cardeña, G; Fan R; Stern D F; Liu J; Sessa W C (November 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. 
  10. ^ Lu, M L; Schneider M C; Zheng Y; Zhang X; Richie J P (April 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. 
  11. ^ Ikezu, T; Trapp B D; Song K S; Schlegel A; Lisanti M P; Okamoto T (April 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. 
  12. ^ 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. 
  13. ^ Felley-Bosco, E; Bender F C; Courjault-Gautier F; Bron C; Quest A F (December 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 18919Freely accessible. PMID 11114180. 
  14. ^ Couet, J; Sargiacomo M; Lisanti M P (November 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. 
  15. ^ Yamaguchi, Tomohiro; Murata Yasunobu; Fujiyoshi Yoshinori; Doi Tomoko (April 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. 
  16. ^ a b Yamamoto, M; Toya Y; Jensen R A; Ishikawa Y (March 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. 
  17. ^ Liou, J Y; Deng W G; Gilroy D W; Shyue S K; Wu K K (September 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. 
  18. ^ Feng, X; Gaeta M L; Madge L A; Yang J H; Bradley J R; Pober J S (March 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. 
  19. ^ Cao, Haiming; Courchesne William E; Mastick Cynthia Corley (March 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. 
  20. ^ Schlegel, A; Wang C; Pestell R G; Lisanti M P (October 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 1222136Freely accessible. PMID 11563984. 
  21. ^ Breuza, Lionel; Corby Séverine; Arsanto Jean-Pierre; Delgrossi Marie-Hélène; Scheiffele Peter; Le Bivic André (December 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. 
  22. ^ 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 (November 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. 
  23. ^ Zheng, Xiangjian; Bollinger Bollag Wendy (December 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. 
  24. ^ Czarny, M; Fiucci G; Lavie Y; Banno Y; Nozawa Y; Liscovitch M (February 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. 
  25. ^ Vargas, Leonardo; Nore Beston F; Berglof Anna; Heinonen Juhana E; Mattsson Pekka T; Smith C I Edvard; Mohamed Abdalla J (March 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. 
  26. ^ Zhou, Minglong; Parr Rebecca D; Petrescu Anca D; Payne H Ross; Atshaves Barbara P; Kier Ann B; Ball Judith M; Schroeder Friedhelm (June 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. 
  27. ^ Couet, Jacque; Li S; Okamoto T; Ikezu T; Lisanti MP. (7 March 1997). "Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins.". J. Biol. Chem. 272 (10): 6525–33. doi:10.1074/jbc.272.10.6525. PMID 9045678. 

Further reading[edit]