Wikipedia

Caveolin 1

Caveolin-1 adalah protein yang disandikan oleh gen CAV1 dalam tubuh manusia.[1]

Interaksi sunting

Caveolin 1 diketahui telah berinteraksi dengan protein heterotrimerik G,[2] Src tyrosine kinases (Src, Lyn), dan H-Ras,[3] kolestrol,[4] TGF beta receptor 1,[5] endothelial NOS,[6] reseptor androgen,[7] amyloid precursor protein,[8] gap junction protein, alpha 1,[9] nitric oxide synthase 2A,[10] epidermal growth factor receptor,[11] endothelin receptor type B,[12] PDGFRB,[13] PDGFRA,[13] PTGS2,[14] TRAF2,[15][16] estrogen receptor alpha,[17] caveolin 2,[18][19] PLD2,[20][21] Bruton's tyrosine kinase[22] dan SCP2.[23] Molekul yang berinteraksi dengan caveolin-1 mengandung caveolin-binding motifs (CBM).[24]

Referensi sunting

  1. ^ Fra AM, Mastroianni N, Mancini M, Pasqualetto E, Sitia R (March 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. 
  2. ^ Li S, Okamoto T, Chun M, Sargiacomo M, Casanova JE, Hansen SH, Nishimoto I, Lisanti MP (June 1995). "Evidence for a regulated interaction between heterotrimeric G proteins and caveolin". The Journal of Biological Chemistry. 270 (26): 15693–701. doi:10.1074/jbc.270.26.15693. PMID 7797570. 
  3. ^ Li S, Couet J, Lisanti MP (November 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". The Journal of Biological Chemistry. 271 (46): 29182–90. doi:10.1074/jbc.271.46.29182. PMID 8910575. 
  4. ^ Li S, Song KS, Lisanti MP (January 1996). "Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes". The Journal of Biological Chemistry. 271 (1): 568–73. doi:10.1074/jbc.271.1.568. PMID 8550621. 
  5. ^ Razani B, Zhang XL, Bitzer M, von Gersdorff G, Böttinger EP, Lisanti MP (March 2001). "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor". The Journal of Biological Chemistry. 276 (9): 6727–38. doi:10.1074/jbc.M008340200. PMID 11102446. 
  6. ^ García-Cardeña G, Fan R, Stern DF, Liu J, Sessa WC (November 1996). "Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1". The Journal of Biological Chemistry. 271 (44): 27237–40. doi:10.1074/jbc.271.44.27237. PMID 8910295. 
  7. ^ Lu ML, Schneider MC, Zheng Y, Zhang X, Richie JP (April 2001). "Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation". The Journal of Biological Chemistry. 276 (16): 13442–51. doi:10.1074/jbc.M006598200. PMID 11278309. 
  8. ^ Ikezu T, Trapp BD, Song KS, Schlegel A, Lisanti MP, Okamoto T (April 1998). "Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein". The Journal of Biological Chemistry. 273 (17): 10485–95. doi:10.1074/jbc.273.17.10485. PMID 9553108. 
  9. ^ Schubert AL, Schubert W, Spray DC, Lisanti MP (May 2002). "Connexin family members target to lipid raft domains and interact with caveolin-1". Biochemistry. 41 (18): 5754–64. doi:10.1021/bi0121656. PMID 11980479. 
  10. ^ Felley-Bosco E, Bender FC, Courjault-Gautier F, Bron C, Quest AF (December 2000). "Caveolin-1 down-regulates inducible nitric oxide synthase via the proteasome pathway in human colon carcinoma cells". Proceedings of the National Academy of Sciences of the United States of America. 97 (26): 14334–9. Bibcode:2000PNAS...9714334F. doi:10.1073/pnas.250406797. PMC 18919  . PMID 11114180. 
  11. ^ Couet J, Sargiacomo M, Lisanti MP (November 1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities". The Journal of Biological Chemistry. 272 (48): 30429–38. doi:10.1074/jbc.272.48.30429. PMID 9374534. 
  12. ^ Yamaguchi T, Murata Y, Fujiyoshi Y, Doi T (April 2003). "Regulated interaction of endothelin B receptor with caveolin-1". European Journal of Biochemistry. 270 (8): 1816–27. doi:10.1046/j.1432-1033.2003.03544.x. PMID 12694195. 
  13. ^ a b Yamamoto M, Toya Y, Jensen RA, Ishikawa Y (March 1999). "Caveolin is an inhibitor of platelet-derived growth factor receptor signaling". Experimental Cell Research. 247 (2): 380–8. doi:10.1006/excr.1998.4379. PMID 10066366. 
  14. ^ Liou JY, Deng WG, Gilroy DW, Shyue SK, Wu KK (September 2001). "Colocalization and interaction of cyclooxygenase-2 with caveolin-1 in human fibroblasts". The Journal of Biological Chemistry. 276 (37): 34975–82. doi:10.1074/jbc.M105946200. PMID 11432874. 
  15. ^ Feng X, Gaeta ML, Madge LA, Yang JH, Bradley JR, Pober JS (March 2001). "Caveolin-1 associates with TRAF2 to form a complex that is recruited to tumor necrosis factor receptors". The Journal of Biological Chemistry. 276 (11): 8341–9. doi:10.1074/jbc.M007116200. PMID 11112773. 
  16. ^ Cao H, Courchesne WE, Mastick CC (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". The Journal of Biological Chemistry. 277 (11): 8771–4. doi:10.1074/jbc.C100661200. PMID 11805080. 
  17. ^ Schlegel A, Wang C, Pestell RG, Lisanti MP (October 2001). "Ligand-independent activation of oestrogen receptor alpha by caveolin-1". The Biochemical Journal. 359 (Pt 1): 203–10. doi:10.1042/0264-6021:3590203. PMC 1222136  . PMID 11563984. 
  18. ^ Breuza L, Corby S, Arsanto JP, Delgrossi MH, Scheiffele P, Le Bivic A (December 2002). "The scaffolding domain of caveolin 2 is responsible for its Golgi localization in Caco-2 cells". Journal of Cell Science. 115 (Pt 23): 4457–67. doi:10.1242/jcs.00130. PMID 12414992. 
  19. ^ Scherer PE, Lewis RY, Volonte D, Engelman JA, Galbiati F, Couet J, Kohtz DS, van Donselaar E, Peters P, Lisanti MP (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". The Journal of Biological Chemistry. 272 (46): 29337–46. doi:10.1074/jbc.272.46.29337. PMID 9361015. 
  20. ^ Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane microdomains and is downregulated upon keratinocyte differentiation". The Journal of Investigative Dermatology. 121 (6): 1487–95. doi:10.1111/j.1523-1747.2003.12614.x. PMID 14675200. 
  21. ^ 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 Letters. 467 (2–3): 326–32. doi:10.1016/S0014-5793(00)01174-1. PMID 10675563. 
  22. ^ Vargas L, Nore BF, Berglof A, Heinonen JE, Mattsson PT, Smith CI, Mohamed AJ (March 2002). "Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx". The Journal of Biological Chemistry. 277 (11): 9351–7. doi:10.1074/jbc.M108537200. PMID 11751885. 
  23. ^ Zhou M, Parr RD, Petrescu AD, Payne HR, Atshaves BP, Kier AB, Ball JM, Schroeder F (June 2004). "Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo". Biochemistry. 43 (23): 7288–306. doi:10.1021/bi035914n. PMID 15182174. 
  24. ^ Couet J, Li S, Okamoto T, Ikezu T, Lisanti MP (March 1997). "Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins". The Journal of Biological Chemistry. 272 (10): 6525–33. doi:10.1074/jbc.272.10.6525. PMID 9045678. 
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