Biology:Caveolin 1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

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

Function

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 heterotrimeric G proteins,[3] Src tyrosine kinases (Src, Lyn) and H-Ras,[4] cholesterol,[5] TGF beta receptor 1,[6] endothelial NOS,[7] androgen receptor,[8] amyloid precursor protein,[9] gap junction protein, alpha 1,[10] nitric oxide synthase 2A,[11] epidermal growth factor receptor,[12] endothelin receptor type B,[13] PDGFRB,[14] PDGFRA,[14] PTGS2,[15] TRAF2,[16][17] estrogen receptor alpha,[18] caveolin 2,[19][20] PLD2,[21][22] Bruton's tyrosine kinase,[23] and SCP2.[24] All these interactions are through a caveolin-scaffolding domain (CSD) within caveolin-1 molecule.[4] Molecules that interact with caveolin-1 contain caveolin-binding motifs (CBM).[25]

See also

References

  1. ↑ "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. March 1999. doi:10.1006/geno.1998.5723. PMID 10087206. 
  2. ↑ "Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=857. 
  3. ↑ "Evidence for a regulated interaction between heterotrimeric G proteins and caveolin". The Journal of Biological Chemistry 270 (26): 15693–701. June 1995. doi:10.1074/jbc.270.26.15693. PMID 7797570. 
  4. ↑ 4.0 4.1 "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. November 1996. doi:10.1074/jbc.271.46.29182. PMID 8910575. 
  5. ↑ "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. January 1996. doi:10.1074/jbc.271.1.568. PMID 8550621. 
  6. ↑ "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. March 2001. doi:10.1074/jbc.M008340200. PMID 11102446. 
  7. ↑ "Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1". The Journal of Biological Chemistry 271 (44): 27237–40. November 1996. doi:10.1074/jbc.271.44.27237. PMID 8910295. 
  8. ↑ "Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation". The Journal of Biological Chemistry 276 (16): 13442–51. April 2001. doi:10.1074/jbc.M006598200. PMID 11278309. 
  9. ↑ "Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein". The Journal of Biological Chemistry 273 (17): 10485–95. April 1998. doi:10.1074/jbc.273.17.10485. PMID 9553108. 
  10. ↑ "Connexin family members target to lipid raft domains and interact with caveolin-1". Biochemistry 41 (18): 5754–64. May 2002. doi:10.1021/bi0121656. PMID 11980479. 
  11. ↑ "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. December 2000. doi:10.1073/pnas.250406797. PMID 11114180. Bibcode: 2000PNAS...9714334F. 
  12. ↑ "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. November 1997. doi:10.1074/jbc.272.48.30429. PMID 9374534. 
  13. ↑ "Regulated interaction of endothelin B receptor with caveolin-1". European Journal of Biochemistry 270 (8): 1816–27. April 2003. doi:10.1046/j.1432-1033.2003.03544.x. PMID 12694195. 
  14. ↑ 14.0 14.1 "Caveolin is an inhibitor of platelet-derived growth factor receptor signaling". Experimental Cell Research 247 (2): 380–8. March 1999. doi:10.1006/excr.1998.4379. PMID 10066366. 
  15. ↑ "Colocalization and interaction of cyclooxygenase-2 with caveolin-1 in human fibroblasts". The Journal of Biological Chemistry 276 (37): 34975–82. September 2001. doi:10.1074/jbc.M105946200. PMID 11432874. 
  16. ↑ "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. March 2001. doi:10.1074/jbc.M007116200. PMID 11112773. 
  17. ↑ "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. March 2002. doi:10.1074/jbc.C100661200. PMID 11805080. 
  18. ↑ "Ligand-independent activation of oestrogen receptor alpha by caveolin-1". The Biochemical Journal 359 (Pt 1): 203–10. October 2001. doi:10.1042/0264-6021:3590203. PMID 11563984. 
  19. ↑ "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. December 2002. doi:10.1242/jcs.00130. PMID 12414992. 
  20. ↑ "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. November 1997. doi:10.1074/jbc.272.46.29337. PMID 9361015. 
  21. ↑ "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. December 2003. doi:10.1111/j.1523-1747.2003.12614.x. PMID 14675200. 
  22. ↑ "Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains". FEBS Letters 467 (2–3): 326–32. February 2000. doi:10.1016/S0014-5793(00)01174-1. PMID 10675563. 
  23. ↑ "Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx". The Journal of Biological Chemistry 277 (11): 9351–7. March 2002. doi:10.1074/jbc.M108537200. PMID 11751885. 
  24. ↑ "Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo". Biochemistry 43 (23): 7288–306. June 2004. doi:10.1021/bi035914n. PMID 15182174. https://scholarworks.sfasu.edu/biology/44. 
  25. ↑ "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. March 1997. doi:10.1074/jbc.272.10.6525. PMID 9045678. 

Further reading



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