Caveolin 1: Difference between revisions

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{{Infobox_gene}}
{{Infobox_gene}}
'''Caveolin-1''' is a [[protein]] that in humans is encoded by the ''CAV1'' [[gene]].<ref name="pmid10087206">{{cite journal | vauthors = Fra AM, Mastroianni N, Mancini M, Pasqualetto E, Sitia R | title = Human caveolin-1 and caveolin-2 are closely linked genes colocalized with WI-5336 in a region of 7q31 frequently deleted in tumors | journal = Genomics | volume = 56 | issue = 3 | pages = 355–6 |date=May 1999 | pmid = 10087206 | pmc =  | doi = 10.1006/geno.1998.5723 }}</ref>
'''Caveolin-1''' is a [[protein]] that in humans is encoded by the ''CAV1'' [[gene]].<ref name="pmid10087206">{{cite journal | vauthors = Fra AM, Mastroianni N, Mancini M, Pasqualetto E, Sitia R | title = Human caveolin-1 and caveolin-2 are closely linked genes colocalized with WI-5336 in a region of 7q31 frequently deleted in tumors | journal = Genomics | volume = 56 | issue = 3 | pages = 355–6 | date = March 1999 | pmid = 10087206 | pmc =  | doi = 10.1006/geno.1998.5723 }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{PBB_Summary
| section_title =  
| summary_text = 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.<ref>{{cite web | title = Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=857| accessdate = }}</ref>
}}


==Interactions==
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.<ref>{{cite web | title = Entrez Gene: CAV1 caveolin 1, caveolae protein, 22kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=857| access-date = }}</ref>
Caveolin 1 has been shown to [[Protein-protein interaction|interact]] with [[heterotrimeric G proteins]],<ref>{{cite journal|last=Li|first=Shengwen|author2=Okamoto T|author3=Chun M|author4=Sargiacomo M|author5=Casanova JE|author6=Hansen SH|author7=Nishimoto I|author8=Lisanti MP|journal=J. Biol. Chem.|year=1995|volume=270|issue=26|pages=15693–701|pmid=7797570|doi=10.1074/jbc.270.26.15693|title=Evidence for a regulated interaction between heterotrimeric G proteins and caveolin}}</ref>
Src tyrosine kinases ([[Src Kinase|Src]], [[LYN|Lyn]]) and H-Ras,<ref name="Li 29182–90">{{cite journal|last=Li|first=Shengwen|author2=Couet J|author3=Lisanti MP.|title=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.|journal=J. Biol. Chem.|date=15 Nov 1996|volume=271|issue=46|pages=29182–90.|pmid=8910575|doi=10.1074/jbc.271.46.29182}}</ref>
[[cholesterol]],<ref>{{cite journal|last=Li|first=Shengwen|author2=Song KS|author3=Lisanti MP.|title=Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes.|journal=J. Biol. Chem.|date=5 Jan 1996|volume=271|issue=1|pages=568–73.|pmid=8550621|doi=10.1074/jbc.271.1.568}}</ref>
[[TGF beta receptor 1]],<ref name=pmid11102446>{{cite journal |last=Razani |first=B |author2=Zhang X L |author3=Bitzer M |author4=von Gersdorff G |author5=Böttinger E P |author6=Lisanti M P  |date=March 2001  |title=Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor |journal=J. Biol. Chem. |volume=276 |issue=9 |pages=6727–38 |publisher= |location = United States| issn = 0021-9258| pmid = 11102446 |doi = 10.1074/jbc.M008340200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>
[[Endothelial NOS]],<ref name=pmid8910295>{{cite journal |last=García-Cardeña |first=G |author2=Fan R|author3=Stern D F|author4=Liu J|author5=Sessa W C |date=November 1996  |title=Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1 |journal=J. Biol. Chem. |volume=271 |issue=44 |pages=27237–40 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 8910295 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.271.44.27237 }}</ref>
[[Androgen receptor]],<ref name=pmid11278309>{{cite journal |last=Lu |first=M L |author2=Schneider M C|author3=Zheng Y|author4=Zhang X|author5=Richie J P |date=April 2001  |title=Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation |journal=J. Biol. Chem. |volume=276 |issue=16 |pages=13442–51 |publisher= |location = United States| issn = 0021-9258| pmid = 11278309 |doi = 10.1074/jbc.M006598200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>
[[Amyloid precursor protein]],<ref name=pmid9553108>{{cite journal |last=Ikezu |first=T |author2=Trapp B D|author3=Song K S|author4=Schlegel A|author5=Lisanti M P|author6=Okamoto T |date=April 1998  |title=Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein |journal=J. Biol. Chem. |volume=273 |issue=17 |pages=10485–95 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9553108 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.273.17.10485 }}</ref>
[[Gap junction protein, alpha 1]],<ref name=pmid11980479>{{cite journal |last=Schubert |first=Anne-Lane |author2=Schubert William |author3=Spray David C |author4=Lisanti Michael P  |date=May 2002 |title=Connexin family members target to lipid raft domains and interact with caveolin-1 |journal=Biochemistry |volume=41 |issue=18 |pages=5754–64 |publisher= |location = United States| issn = 0006-2960| pmid = 11980479 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1021/bi0121656 }}</ref>
[[Nitric oxide synthase 2A]],<ref name=pmid11114180>{{cite journal |last=Felley-Bosco |first=E |author2=Bender F C|author3=Courjault-Gautier F|author4=Bron C|author5=Quest A F |date=December 2000  |title=Caveolin-1 down-regulates inducible nitric oxide synthase via the proteasome pathway in human colon carcinoma cells |journal=[[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] |volume=97 |issue=26 |pages=14334–9 |publisher= |location = UNITED STATES| issn = 0027-8424| pmid = 11114180 |doi = 10.1073/pnas.250406797 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=18919 }}</ref> [[Epidermal growth factor receptor]],<ref name=pmid9374534>{{cite journal |last=Couet |first=J |author2=Sargiacomo M|author3=Lisanti M P |date=November 1997  |title=Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities |journal=J. Biol. Chem. |volume=272 |issue=48 |pages=30429–38 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9374534 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.272.48.30429 }}</ref> [[Endothelin receptor type B]],<ref name=pmid12694195>{{cite journal |last=Yamaguchi |first=Tomohiro |author2=Murata Yasunobu |author3=Fujiyoshi Yoshinori |author4=Doi Tomoko  |date=April 2003  |title=Regulated interaction of endothelin B receptor with caveolin-1 |journal=Eur. J. Biochem. |volume=270 |issue=8 |pages=1816–27 |publisher= |location = Germany| issn = 0014-2956| pmid = 12694195 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1046/j.1432-1033.2003.03544.x }}</ref> [[PDGFRB]],<ref name=pmid10066366>{{cite journal |last=Yamamoto |first=M |author2=Toya Y|author3=Jensen R A|author4=Ishikawa Y |date=March 1999  |title=Caveolin is an inhibitor of platelet-derived growth factor receptor signaling |journal=Exp. Cell Res. |volume=247 |issue=2 |pages=380–8 |publisher= |location = UNITED STATES| issn = 0014-4827| pmid = 10066366 |doi = 10.1006/excr.1998.4379 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[PDGFRA]],<ref name=pmid10066366/> [[PTGS2]],<ref name=pmid11432874>{{cite journal |last=Liou |first=J Y |author2=Deng W G|author3=Gilroy D W|author4=Shyue S K|author5=Wu K K |date=September 2001  |title=Colocalization and interaction of cyclooxygenase-2 with caveolin-1 in human fibroblasts |journal=J. Biol. Chem. |volume=276 |issue=37 |pages=34975–82 |publisher= |location = United States| issn = 0021-9258| pmid = 11432874 |doi = 10.1074/jbc.M105946200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[TRAF2]],<ref name=pmid11112773>{{cite journal |last=Feng |first=X |author2=Gaeta M L|author3=Madge L A|author4=Yang J H|author5=Bradley J R|author6=Pober J S |date=March 2001  |title=Caveolin-1 associates with TRAF2 to form a complex that is recruited to tumor necrosis factor receptors |journal=J. Biol. Chem. |volume=276 |issue=11 |pages=8341–9 |publisher= |location = United States| issn = 0021-9258| pmid = 11112773 |doi = 10.1074/jbc.M007116200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid11805080>{{cite journal |last=Cao |first=Haiming |author2=Courchesne William E |author3=Mastick Cynthia Corley  |date=March 2002  |title=A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase |journal=J. Biol. Chem. |volume=277 |issue=11 |pages=8771–4 |publisher= |location = United States| issn = 0021-9258| pmid = 11805080 |doi = 10.1074/jbc.C100661200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[Estrogen receptor alpha]],<ref name=pmid11563984>{{cite journal |last=Schlegel |first=A |author2=Wang C|author3=Pestell R G|author4=Lisanti M P |date=October 2001  |title=Ligand-independent activation of oestrogen receptor alpha by caveolin-1 |journal=Biochem. J. |volume=359 |issue=Pt 1 |pages=203–10 |publisher= |location = England| issn = 0264-6021| pmid = 11563984 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1042/0264-6021:3590203 |pmc=1222136 }}</ref> [[Caveolin 2]],<ref name=pmid12414992>{{cite journal |last=Breuza |first=Lionel |author2=Corby Séverine |author3=Arsanto Jean-Pierre |author4=Delgrossi Marie-Hélène |author5=Scheiffele Peter |author6=Le Bivic André  |date=December 2002  |title=The scaffolding domain of caveolin 2 is responsible for its Golgi localization in Caco-2 cells |journal=J. Cell Sci. |volume=115 |issue=Pt 23 |pages=4457–67 |publisher= |location = England| issn = 0021-9533| pmid = 12414992 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1242/jcs.00130 }}</ref><ref name=pmid9361015>{{cite journal |last=Scherer |first=P E |author2=Lewis R Y |author3=Volonte D |author4=Engelman J A |author5=Galbiati F |author6=Couet J |author7=Kohtz D S |author8=van Donselaar E |author9=Peters P |author10=Lisanti M P  |date=November 1997  |title=Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo |journal=J. Biol. Chem. |volume=272 |issue=46 |pages=29337–46 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9361015 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.272.46.29337 }}</ref> [[PLD2]],<ref name=pmid14675200>{{cite journal |last=Zheng |first=Xiangjian |author2=Bollinger Bollag Wendy |date=December 2003  |title=Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane microdomains and is downregulated upon keratinocyte differentiation |journal=J. Invest. Dermatol. |volume=121 |issue=6 |pages=1487–95 |publisher= |location = United States| issn = 0022-202X| pmid = 14675200 |doi = 10.1111/j.1523-1747.2003.12614.x | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid10675563>{{cite journal |last=Czarny |first=M |author2=Fiucci G|author3=Lavie Y|author4=Banno Y|author5=Nozawa Y|author6=Liscovitch M |date=February 2000  |title=Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains |journal=FEBS Lett. |volume=467 |issue=2–3 |pages=326–32 |publisher= |location = NETHERLANDS| issn = 0014-5793| pmid = 10675563 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1016/S0014-5793(00)01174-1 }}</ref> [[Bruton's tyrosine kinase]]<ref name=pmid11751885>{{cite journal |last=Vargas |first=Leonardo |author2=Nore Beston F |author3=Berglof Anna |author4=Heinonen Juhana E |author5=Mattsson Pekka T |author6=Smith C I Edvard |author7=Mohamed Abdalla J  |date=March 2002  |title=Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx |journal=J. Biol. Chem. |volume=277 |issue=11 |pages=9351–7 |publisher= |location = United States| issn = 0021-9258| pmid = 11751885 |doi = 10.1074/jbc.M108537200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[SCP2]].<ref name=pmid15182174>{{cite journal |last=Zhou |first=Minglong |author2=Parr Rebecca D |author3=Petrescu Anca D |author4=Payne H Ross |author5=Atshaves Barbara P |author6=Kier Ann B |author7=Ball Judith M |author8=Schroeder Friedhelm  |date=June 2004  |title=Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo |journal=Biochemistry |volume=43 |issue=23 |pages=7288–306 |publisher= |location = United States| issn = 0006-2960| pmid = 15182174 |doi = 10.1021/bi035914n | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> All these interactions are through a caveolin-scaffolding domain (CSD) within caveolin-1 molecule.<ref name="Li 29182–90"/> Molecules that interact with caveolin-1 contain caveolin-binding motifs (CBM).<ref>{{cite journal|last=Couet|first=Jacque|author2=Li S|author3=Okamoto T|author4=Ikezu T|author5=Lisanti MP.|title=Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins.|journal=J. Biol. Chem. |date=7 March 1997|volume=272|issue=10|pages=6525–33|pmid=9045678|doi=10.1074/jbc.272.10.6525}}</ref>


==See also==
== Interactions ==
 
Caveolin 1 has been shown to [[Protein-protein interaction|interact]] with [[heterotrimeric G proteins]],<ref>{{cite journal | vauthors = Li S, Okamoto T, Chun M, Sargiacomo M, Casanova JE, Hansen SH, Nishimoto I, Lisanti MP | title = Evidence for a regulated interaction between heterotrimeric G proteins and caveolin | journal = The Journal of Biological Chemistry | volume = 270 | issue = 26 | pages = 15693–701 | date = June 1995 | pmid = 7797570 | doi = 10.1074/jbc.270.26.15693 }}</ref>
Src tyrosine kinases ([[Src Kinase|Src]], [[LYN|Lyn]]) and H-Ras,<ref name="Li 29182–90">{{cite journal | vauthors = Li S, Couet J, Lisanti MP | title = 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 | journal = The Journal of Biological Chemistry | volume = 271 | issue = 46 | pages = 29182–90 | date = November 1996 | pmid = 8910575 | doi = 10.1074/jbc.271.46.29182 }}</ref>
[[cholesterol]],<ref>{{cite journal | vauthors = Li S, Song KS, Lisanti MP | title = Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes | journal = The Journal of Biological Chemistry | volume = 271 | issue = 1 | pages = 568–73 | date = January 1996 | pmid = 8550621 | doi = 10.1074/jbc.271.1.568 }}</ref>
[[TGF beta receptor 1]],<ref name=pmid11102446>{{cite journal | vauthors = Razani B, Zhang XL, Bitzer M, von Gersdorff G, Böttinger EP, Lisanti MP | title = Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor | journal = The Journal of Biological Chemistry | volume = 276 | issue = 9 | pages = 6727–38 | date = March 2001 | pmid = 11102446 | doi = 10.1074/jbc.M008340200 }}</ref>
[[endothelial NOS]],<ref name=pmid8910295>{{cite journal | vauthors = García-Cardeña G, Fan R, Stern DF, Liu J, Sessa WC | title = Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1 | journal = The Journal of Biological Chemistry | volume = 271 | issue = 44 | pages = 27237–40 | date = November 1996 | pmid = 8910295 | doi = 10.1074/jbc.271.44.27237 }}</ref>
[[androgen receptor]],<ref name=pmid11278309>{{cite journal | vauthors = Lu ML, Schneider MC, Zheng Y, Zhang X, Richie JP | title = Caveolin-1 interacts with androgen receptor. A positive modulator of androgen receptor mediated transactivation | journal = The Journal of Biological Chemistry | volume = 276 | issue = 16 | pages = 13442–51 | date = April 2001 | pmid = 11278309 | doi = 10.1074/jbc.M006598200 }}</ref>
[[amyloid precursor protein]],<ref name=pmid9553108>{{cite journal | vauthors = Ikezu T, Trapp BD, Song KS, Schlegel A, Lisanti MP, Okamoto T | title = Caveolae, plasma membrane microdomains for alpha-secretase-mediated processing of the amyloid precursor protein | journal = The Journal of Biological Chemistry | volume = 273 | issue = 17 | pages = 10485–95 | date = April 1998 | pmid = 9553108 | doi = 10.1074/jbc.273.17.10485 }}</ref>
[[gap junction protein, alpha 1]],<ref name=pmid11980479>{{cite journal | vauthors = Schubert AL, Schubert W, Spray DC, Lisanti MP | title = Connexin family members target to lipid raft domains and interact with caveolin-1 | journal = Biochemistry | volume = 41 | issue = 18 | pages = 5754–64 | date = May 2002 | pmid = 11980479 | doi = 10.1021/bi0121656 }}</ref>
[[nitric oxide synthase 2A]],<ref name=pmid11114180>{{cite journal | vauthors = Felley-Bosco E, Bender FC, Courjault-Gautier F, Bron C, Quest AF | title = Caveolin-1 down-regulates inducible nitric oxide synthase via the proteasome pathway in human colon carcinoma cells | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 26 | pages = 14334–9 | date = December 2000 | pmid = 11114180 | pmc = 18919 | doi = 10.1073/pnas.250406797 | bibcode = 2000PNAS...9714334F }}</ref> [[epidermal growth factor receptor]],<ref name=pmid9374534>{{cite journal | vauthors = Couet J, Sargiacomo M, Lisanti MP | title = Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities | journal = The Journal of Biological Chemistry | volume = 272 | issue = 48 | pages = 30429–38 | date = November 1997 | pmid = 9374534 | doi = 10.1074/jbc.272.48.30429 }}</ref> [[endothelin receptor type B]],<ref name=pmid12694195>{{cite journal | vauthors = Yamaguchi T, Murata Y, Fujiyoshi Y, Doi T | title = Regulated interaction of endothelin B receptor with caveolin-1 | journal = European Journal of Biochemistry | volume = 270 | issue = 8 | pages = 1816–27 | date = April 2003 | pmid = 12694195 | doi = 10.1046/j.1432-1033.2003.03544.x }}</ref> [[PDGFRB]],<ref name=pmid10066366>{{cite journal | vauthors = Yamamoto M, Toya Y, Jensen RA, Ishikawa Y | title = Caveolin is an inhibitor of platelet-derived growth factor receptor signaling | journal = Experimental Cell Research | volume = 247 | issue = 2 | pages = 380–8 | date = March 1999 | pmid = 10066366 | doi = 10.1006/excr.1998.4379 }}</ref> [[PDGFRA]],<ref name=pmid10066366/> [[PTGS2]],<ref name=pmid11432874>{{cite journal | vauthors = Liou JY, Deng WG, Gilroy DW, Shyue SK, Wu KK | title = Colocalization and interaction of cyclooxygenase-2 with caveolin-1 in human fibroblasts | journal = The Journal of Biological Chemistry | volume = 276 | issue = 37 | pages = 34975–82 | date = September 2001 | pmid = 11432874 | doi = 10.1074/jbc.M105946200 }}</ref> [[TRAF2]],<ref name=pmid11112773>{{cite journal | vauthors = Feng X, Gaeta ML, Madge LA, Yang JH, Bradley JR, Pober JS | title = Caveolin-1 associates with TRAF2 to form a complex that is recruited to tumor necrosis factor receptors | journal = The Journal of Biological Chemistry | volume = 276 | issue = 11 | pages = 8341–9 | date = March 2001 | pmid = 11112773 | doi = 10.1074/jbc.M007116200 }}</ref><ref name=pmid11805080>{{cite journal | vauthors = Cao H, Courchesne WE, Mastick CC | title = A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase | journal = The Journal of Biological Chemistry | volume = 277 | issue = 11 | pages = 8771–4 | date = March 2002 | pmid = 11805080 | doi = 10.1074/jbc.C100661200 }}</ref> [[estrogen receptor alpha]],<ref name=pmid11563984>{{cite journal | vauthors = Schlegel A, Wang C, Pestell RG, Lisanti MP | title = Ligand-independent activation of oestrogen receptor alpha by caveolin-1 | journal = The Biochemical Journal | volume = 359 | issue = Pt 1 | pages = 203–10 | date = October 2001 | pmid = 11563984 | pmc = 1222136 | doi = 10.1042/0264-6021:3590203 }}</ref> [[caveolin 2]],<ref name=pmid12414992>{{cite journal | vauthors = Breuza L, Corby S, Arsanto JP, Delgrossi MH, Scheiffele P, Le Bivic A | title = The scaffolding domain of caveolin 2 is responsible for its Golgi localization in Caco-2 cells | journal = Journal of Cell Science | volume = 115 | issue = Pt 23 | pages = 4457–67 | date = December 2002 | pmid = 12414992 | doi = 10.1242/jcs.00130 }}</ref><ref name=pmid9361015>{{cite journal | vauthors = Scherer PE, Lewis RY, Volonte D, Engelman JA, Galbiati F, Couet J, Kohtz DS, van Donselaar E, Peters P, Lisanti MP | title = Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo | journal = The Journal of Biological Chemistry | volume = 272 | issue = 46 | pages = 29337–46 | date = November 1997 | pmid = 9361015 | doi = 10.1074/jbc.272.46.29337 }}</ref> [[PLD2]],<ref name=pmid14675200>{{cite journal | vauthors = Zheng X, Bollinger Bollag W | title = Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane microdomains and is downregulated upon keratinocyte differentiation | journal = The Journal of Investigative Dermatology | volume = 121 | issue = 6 | pages = 1487–95 | date = December 2003 | pmid = 14675200 | doi = 10.1111/j.1523-1747.2003.12614.x }}</ref><ref name=pmid10675563>{{cite journal | vauthors = Czarny M, Fiucci G, Lavie Y, Banno Y, Nozawa Y, Liscovitch M | title = Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains | journal = FEBS Letters | volume = 467 | issue = 2-3 | pages = 326–32 | date = February 2000 | pmid = 10675563 | doi = 10.1016/S0014-5793(00)01174-1 }}</ref> [[Bruton's tyrosine kinase]]<ref name=pmid11751885>{{cite journal | vauthors = Vargas L, Nore BF, Berglof A, Heinonen JE, Mattsson PT, Smith CI, Mohamed AJ | title = Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx | journal = The Journal of Biological Chemistry | volume = 277 | issue = 11 | pages = 9351–7 | date = March 2002 | pmid = 11751885 | doi = 10.1074/jbc.M108537200 }}</ref> and [[SCP2]].<ref name=pmid15182174>{{cite journal | vauthors = Zhou M, Parr RD, Petrescu AD, Payne HR, Atshaves BP, Kier AB, Ball JM, Schroeder F | title = Sterol carrier protein-2 directly interacts with caveolin-1 in vitro and in vivo | journal = Biochemistry | volume = 43 | issue = 23 | pages = 7288–306 | date = June 2004 | pmid = 15182174 | doi = 10.1021/bi035914n }}</ref> All these interactions are through a caveolin-scaffolding domain (CSD) within caveolin-1 molecule.<ref name="Li 29182–90"/> Molecules that interact with caveolin-1 contain caveolin-binding motifs (CBM).<ref>{{cite journal | vauthors = Couet J, Li S, Okamoto T, Ikezu T, Lisanti MP | title = Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins | journal = The Journal of Biological Chemistry | volume = 272 | issue = 10 | pages = 6525–33 | date = March 1997 | pmid = 9045678 | doi = 10.1074/jbc.272.10.6525 }}</ref>
 
== See also ==
* [[Caveolin]]
* [[Caveolin]]


==References==
== References ==
{{reflist}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin |30em}}
{{PBB_Further_reading
* {{cite journal | vauthors = Engelman JA, Zhang X, Galbiati F, Volonte D, Sotgia F, Pestell RG, Minetti C, Scherer PE, Okamoto T, Lisanti MP | title = Molecular genetics of the caveolin gene family: implications for human cancers, diabetes, Alzheimer disease, and muscular dystrophy | journal = American Journal of Human Genetics | volume = 63 | issue = 6 | pages = 1578–87 | date = December 1998 | pmid = 9837809 | pmc = 1377628 | doi = 10.1086/302172 }}
| citations =
* {{cite journal | vauthors = Razani B, Schlegel A, Liu J, Lisanti MP | title = Caveolin-1, a putative tumour suppressor gene | journal = Biochemical Society Transactions | volume = 29 | issue = Pt 4 | pages = 494–9 | date = August 2001 | pmid = 11498016 | doi = 10.1042/BST0290494 }}
*{{cite journal | vauthors=Engelman JA, Zhang X, Galbiati F |title=Molecular genetics of the caveolin gene family: implications for human cancers, diabetes, Alzheimer disease, and muscular dystrophy |journal=Am. J. Hum. Genet. |volume=63 |issue= 6 |pages= 1578–87 |year= 1999 |pmid= 9837809 |doi=10.1086/302172 | pmc=1377628  |display-authors=etal}}
* {{cite journal | vauthors = Fujimoto T, Kogo H, Nakamura N, Ozeki S | title = [Microdomains and caveolin] | journal = Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme | volume = 47 | issue = 4 Suppl | pages = 326–32 | date = March 2002 | pmid = 11915322 | doi =  }}
*{{cite journal | vauthors=Razani B, Schlegel A, Liu J, Lisanti MP |title=Caveolin-1, a putative tumour suppressor gene |journal=Biochem. Soc. Trans. |volume=29 |issue= Pt 4 |pages= 494–9 |year= 2002 |pmid= 11498016 |doi=10.1042/BST0290494 }}
* {{cite journal | vauthors = Shatz M, Liscovitch M | title = Caveolin-1 and cancer multidrug resistance: coordinate regulation of pro-survival proteins? | journal = Leukemia Research | volume = 28 | issue = 9 | pages = 907–8 | date = September 2004 | pmid = 15234566 | doi = 10.1016/j.leukres.2004.03.013 }}
*{{cite journal | vauthors=Fujimoto T, Kogo H, Nakamura N, Ozeki S |title=[Microdomains and caveolin] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 4 Suppl |pages= 326–32 |year= 2002 |pmid= 11915322 |doi=  }}
* {{cite journal | vauthors = Frank PG, Lisanti MP | title = Caveolin-1 and liver regeneration: role in proliferation and lipogenesis | journal = Cell Cycle | volume = 6 | issue = 2 | pages = 115–6 | date = January 2007 | pmid = 17314510 | doi = 10.4161/cc.6.2.3722 }}
*{{cite journal | vauthors=Shatz M, Liscovitch M |title=Caveolin-1 and cancer multidrug resistance: coordinate regulation of pro-survival proteins? |journal=Leuk. Res. |volume=28 |issue= 9 |pages= 907–8 |year= 2004 |pmid= 15234566 |doi= 10.1016/j.leukres.2004.03.013 }}
*{{cite journal | vauthors=Frank PG, Lisanti MP |title=Caveolin-1 and liver regeneration: role in proliferation and lipogenesis |journal=Cell Cycle |volume=6 |issue= 2 |pages= 115–6 |year= 2007 |pmid= 17314510 |doi=10.4161/cc.6.2.3722 }}
}}
{{refend}}
{{refend}}


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{{Vesicular transport proteins}}
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[[Category:Genes]]
[[Category:Genes]]
[[Category:Human proteins]]
[[Category:Human proteins]]

Latest revision as of 06:27, 15 November 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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View/Edit Human

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. ↑ 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. ↑ "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. doi:10.1074/jbc.270.26.15693. PMID 7797570.
  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. doi:10.1074/jbc.271.46.29182. PMID 8910575.
  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. doi:10.1074/jbc.271.1.568. PMID 8550621.
  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. doi:10.1074/jbc.M008340200. PMID 11102446.
  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. doi:10.1074/jbc.271.44.27237. PMID 8910295.
  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. doi:10.1074/jbc.M006598200. PMID 11278309.
  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. doi:10.1074/jbc.273.17.10485. PMID 9553108.
  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. doi:10.1021/bi0121656. PMID 11980479.
  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. doi:10.1073/pnas.250406797. PMC 18919. PMID 11114180.
  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. doi:10.1074/jbc.272.48.30429. PMID 9374534.
  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. doi:10.1046/j.1432-1033.2003.03544.x. PMID 12694195.
  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. doi:10.1006/excr.1998.4379. PMID 10066366.
  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. doi:10.1074/jbc.M105946200. PMID 11432874.
  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. doi:10.1074/jbc.M007116200. PMID 11112773.
  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. doi:10.1074/jbc.C100661200. PMID 11805080.
  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. doi:10.1042/0264-6021:3590203. PMC 1222136. PMID 11563984.
  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. doi:10.1242/jcs.00130. PMID 12414992.
  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. doi:10.1074/jbc.272.46.29337. PMID 9361015.
  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. doi:10.1111/j.1523-1747.2003.12614.x. PMID 14675200.
  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. doi:10.1016/S0014-5793(00)01174-1. PMID 10675563.
  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. doi:10.1074/jbc.M108537200. PMID 11751885.
  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. doi:10.1021/bi035914n. PMID 15182174.
  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. doi:10.1074/jbc.272.10.6525. PMID 9045678.

Further reading

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