Location via proxy:   [ UP ]  
[Report a bug]   [Manage cookies]                
Saltar ao contido

Caveolina 1

Na Galipedia, a Wikipedia en galego.
caveolina 1
Estruturas dispoñibles
PDBBuscar ortólogos: PDBe, RCSB
Identificadores
Nomenclatura
SímbolosCAV1 (HGNC: 1527) BSCL3, CGL3, LCCNS, MSTP085, PPH3, VIP21, Caveolin 1
Identificadores
externos
LocusCr. 7 q31.2
Padrón de expresión de ARNm
Máis información
Ortólogos
Especies
Humano Rato
Entrez
857 12389
Ensembl
Véxase HS Véxase MM
UniProt
Q03135 P49817
RefSeq
(ARNm)
NM_001753 NM_001243064
RefSeq
(proteína) NCBI
NP_001166366 NP_001229993
Localización (UCSC)
Cr. 7:
116.53 – 116.56 Mb 		Cr. 6:
17.31 – 17.34 Mb
PubMed (Busca)
857


12389

A caveolina 1 é unha proteína que nos humanos está codificada no xene CAV1 do cromosoma 7.[1]

Función

[editar | editar a fonte]

A proteína de armazón codificada neste xene é o principal compoñente das caveolas da membrana plasmática que se encontran na maioría dos tipos celulares. A proteína enlaza subunidades de integrinas á tirosina quinase FYN, un paso inicial no acoplamento de integrina á vía Ras-ERK e na promoción da progresión do ciclo celular. O xene é un supresor de tumores candidato e un regulador negativo da fervenza da Ras-p42/44 MAP quinase. Os xenes CAV1 e CAV2 están localizados un a carón do outro no cromosoma 7 e expresan proteínas colocalizadas que forman un complexo heterooligomérico estable. Utilizando codóns de iniciación alternativos no mesmo marco de lectura, as dúas isoformas que existen da caveolina 1 (alfa e beta) son codificadas por un só transcrito deste xene.[2]

Interaccións

[editar | editar a fonte]

A caveolina 1 presenta interaccións coas proteínas G heterotriméricas,[3] tirosina quinases Src (Src, Lyn) e H-Ras,[4] o colesterol,[5] o receptor de TGF 1,[6] a óxido nítrico sintase endotelial (eNOS),[7] o receptor de andróxenos,[8] a proteína precursora amiloide,[9] a proteína das unións comunicantes, alfa 1,[10] a óxido nítrico sintase 2A,[11] o receptor do factor de crecemento epidérmico,[12] o receptor de endotelina de tipo B,[13] a PDGFRB,[14] a PDGFRA,[14] a PTGS2,[15] o TRAF2,[16][17] o receptor de estróxenos alfa,[18] a caveolina 2,[19][20] a PLD2,[21][22] a tirosina quinase de Bruton[23] e a SCP2.[24] Todas estas interaccións son por medio dun dominio de armazón de caveolina (CSD) que hai na molécula de caveolina 1.[4] As moléculas que interaccionan coa caveolina 1 conteñen motivos de unión á caveolina (CBM).[25]

Notas

[editar | editar a fonte]
  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. PMID 10087206. doi:10.1006/geno.1998.5723. 
  2. ↑ "Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa". 
  3. ↑ 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. PMID 7797570. doi:10.1074/jbc.270.26.15693. 
  4. ↑ 4,0 4,1 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. PMC 6687395. PMID 8910575. doi:10.1074/jbc.271.46.29182. 
  5. ↑ 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. PMID 8550621. doi:10.1074/jbc.271.1.568. 
  6. ↑ 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. PMID 11102446. doi:10.1074/jbc.M008340200. 
  7. ↑ 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. PMID 8910295. doi:10.1074/jbc.271.44.27237. 
  8. ↑ 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. PMID 11278309. doi:10.1074/jbc.M006598200. 
  9. ↑ 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. PMID 9553108. doi:10.1074/jbc.273.17.10485. 
  10. ↑ 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. PMID 11980479. doi:10.1021/bi0121656. 
  11. ↑ 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. PMC 18919. PMID 11114180. doi:10.1073/pnas.250406797. 
  12. ↑ 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. PMID 9374534. doi:10.1074/jbc.272.48.30429. 
  13. ↑ 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. PMID 12694195. doi:10.1046/j.1432-1033.2003.03544.x. 
  14. ↑ 14,0 14,1 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. PMID 10066366. doi:10.1006/excr.1998.4379. 
  15. ↑ 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. PMID 11432874. doi:10.1074/jbc.M105946200. 
  16. ↑ 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. PMID 11112773. doi:10.1074/jbc.M007116200. 
  17. ↑ 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. PMID 11805080. doi:10.1074/jbc.C100661200. 
  18. ↑ 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. PMC 1222136. PMID 11563984. doi:10.1042/0264-6021:3590203. 
  19. ↑ 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. PMID 12414992. doi:10.1242/jcs.00130. 
  20. ↑ 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. PMID 9361015. doi:10.1074/jbc.272.46.29337. 
  21. ↑ 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. PMID 14675200. doi:10.1111/j.1523-1747.2003.12614.x. 
  22. ↑ 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. PMID 10675563. doi:10.1016/S0014-5793(00)01174-1. 
  23. ↑ 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. PMID 11751885. doi:10.1074/jbc.M108537200. 
  24. ↑ 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. PMID 15182174. doi:10.1021/bi035914n. 
  25. ↑ 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. PMID 9045678. doi:10.1074/jbc.272.10.6525. 

Véxase tamén

[editar | editar a fonte]

Outros artigos

[editar | editar a fonte]

Bibliografía

[editar | editar a fonte]
Traído desde «https://gl.wikipedia.org/w/index.php?title=Caveolina_1&oldid=5950601»