Caveolin 2

CAV2
Identifiers
Aliases	CAV2, CAV, caveolin 2
External IDs	OMIM: 601048 MGI: 107571 HomoloGene: 942 GeneCards: CAV2
Gene location (Human)
Chr.	Chromosome 7 (human)
End	116,508,541 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	17,289,114 bp
RNA expression pattern
	Top expressed in
	lower lobe of lung; ; right ventricle; ; vena cava; ; myocardium; ; urethra; ; synovial joint; ; parietal pleura; ; adipose tissue; ; right coronary artery; ; atrium;
	Top expressed in
	left lung; ; left lung lobe; ; white adipose tissue; ; sciatic nerve; ; right lung; ; right lung lobe; ; brown adipose tissue; ; mammary gland; ; seminal vesicula; ; interventricular septum;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	protein-macromolecule adaptor activity; protein homodimerization activity; scaffold protein binding; protein binding; protein heterodimerization activity; molecular adaptor activity; D1 dopamine receptor binding; protein kinase binding; structural molecule activity;
Cellular component	cytoplasm; Golgi apparatus; membrane; focal adhesion; extrinsic component of cytoplasmic side of plasma membrane; Golgi membrane; plasma membrane; integral component of plasma membrane; intracellular anatomical structure; transport vesicle; acrosomal membrane; perinuclear region of cytoplasm; caveola; membrane raft; cytoplasmic vesicle; nucleus; protein-containing complex; sarcolemma;
Biological process	insulin receptor signaling pathway; positive regulation of endothelial cell proliferation; caveola assembly; vesicle organization; mitochondrion organization; negative regulation of transforming growth factor beta receptor signaling pathway; positive regulation of dopamine receptor signaling pathway; endoplasmic reticulum organization; negative regulation of endothelial cell proliferation; vesicle docking; positive regulation of GTPase activity; positive regulation by host of viral process; skeletal muscle fiber development; protein complex oligomerization; receptor-mediated endocytosis of virus by host cell; vesicle fusion; positive regulation of MAPK cascade; regulation of mitotic nuclear division; negative regulation of cell population proliferation; cell differentiation;
	Sources:Amigo / QuickGO
Orthologs
	858
	12390
	ENSG00000105971
	ENSMUSG00000000058
	P51636
	Q9WVC3
	NM_001206747; NM_001206748; NM_001233; NM_198212
	NM_001277756; NM_016900
	NP_001193676; NP_001193677; NP_001224; NP_937855
	NP_001264685; NP_058596
	Wikidata
View/Edit Human	View/Edit Mouse

Caveolin-2 is a protein that in humans is encoded by the CAV2 gene.^[5]^[6]^[7]

The protein encoded by this gene is a major component of the inner surface of caveolae, small invaginations of the plasma membrane, and is involved in essential cellular functions, including signal transduction, lipid metabolism, cellular growth control and apoptosis. This protein may function as a tumor suppressor. The CAV1 and CAV2 genes are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex,^[7]^[8] which can be disrupted by Src-mediated phosphorylation of tyrosine 19 on caveolin-2.^[9] Two transcript variants encoding distinct isoforms have been identified for this gene. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by one transcript.^[7]

Interactions

Caveolin 2 has been shown to interact with Caveolin 1^[8]^[10] and RAS p21 protein activator 1.^[9]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000105971 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000000058 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Scherer PE, Okamoto T, Chun M, Nishimoto I, Lodish HF, Lisanti MP (Feb 1996). "Identification, sequence, and expression of caveolin-2 defines a caveolin gene family". Proc Natl Acad Sci U S A. 93 (1): 131–5. Bibcode:1996PNAS...93..131S. doi:10.1073/pnas.93.1.131. PMC 40192. PMID 8552590.
↑ 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.
1 2 3 "Entrez Gene: CAV2 caveolin 2".
1 2 Scherer PE, Lewis R Y, Volonte D, Engelman J A, Galbiati F, Couet J, Kohtz D S, van Donselaar E, Peters P, Lisanti M P (Nov 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.
1 2 Lee H, Park David S, Wang Xiao Bo, Scherer Philipp E, Schwartz Phillip E, Lisanti Michael P (Sep 2002). "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1". J. Biol. Chem. United States. 277 (37): 34556–67. doi:10.1074/jbc.M204367200. ISSN 0021-9258. PMID 12091389.
↑ Breuza L, Corby Séverine, Arsanto Jean-Pierre, Delgrossi Marie-Hélène, Scheiffele Peter, Le Bivic André (Dec 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. S2CID 14788127.

Engelman JA, Zhang X, Galbiati F, et al. (1999). "Molecular genetics of the caveolin gene family: implications for human cancers, diabetes, Alzheimer disease, and muscular dystrophy". Am. J. Hum. Genet. 63 (6): 1578–87. doi:10.1086/302172. PMC 1377628. PMID 9837809.
Glenney JR (1992). "The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles". FEBS Lett. 314 (1): 45–8. doi:10.1016/0014-5793(92)81458-X. PMID 1360410. S2CID 12826361.
Murata M, Peränen J, Schreiner R, et al. (1995). "VIP21/caveolin is a cholesterol-binding protein". Proc. Natl. Acad. Sci. U.S.A. 92 (22): 10339–43. Bibcode:1995PNAS...9210339M. doi:10.1073/pnas.92.22.10339. PMC 40792. PMID 7479780.
Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, et al. (1995). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID 7829101.
Scherer PE, Lewis RY, Volonte D, et al. (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. 272 (46): 29337–46. doi:10.1074/jbc.272.46.29337. PMID 9361015.
Galbiati F, Volonte D, Gil O, et al. (1998). "Expression of caveolin-1 and -2 in differentiating PC12 cells and dorsal root ganglion neurons: caveolin-2 is up-regulated in response to cell injury". Proc. Natl. Acad. Sci. U.S.A. 95 (17): 10257–62. Bibcode:1998PNAS...9510257G. doi:10.1073/pnas.95.17.10257. PMC 21495. PMID 9707634.
Engelman JA, Zhang XL, Lisanti MP (1998). "Genes encoding human caveolin-1 and -2 are co-localized to the D7S522 locus (7q31.1), a known fragile site (FRA7G) that is frequently deleted in human cancers". FEBS Lett. 436 (3): 403–10. doi:10.1016/S0014-5793(98)01134-X. PMID 9801158. S2CID 24354687.
Volonte D, Galbiati F, Li S, et al. (1999). "Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe". J. Biol. Chem. 274 (18): 12702–9. doi:10.1074/jbc.274.18.12702. PMID 10212252.
Engelman JA, Zhang XL, Lisanti MP (1999). "Sequence and detailed organization of the human caveolin-1 and -2 genes located near the D7S522 locus (7q31.1). Methylation of a CpG island in the 5' promoter region of the caveolin-1 gene in human breast cancer cell lines". FEBS Lett. 448 (2–3): 221–30. doi:10.1016/S0014-5793(99)00365-8. PMID 10218480. S2CID 37779245.
Mora R, Bonilha VL, Marmorstein A, et al. (1999). "Caveolin-2 localizes to the golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1". J. Biol. Chem. 274 (36): 25708–17. doi:10.1074/jbc.274.36.25708. PMID 10464308.
Fra AM, Pasqualetto E, Mancini M, Sitia R (2000). "Genomic organization and transcriptional analysis of the human genes coding for caveolin-1 and caveolin-2". Gene. 243 (1–2): 75–83. doi:10.1016/S0378-1119(99)00559-4. PMID 10675615.
Schwab W, Kasper M, Gavlik JM, et al. (2000). "Characterization of caveolins from human knee joint catilage: expression of caveolin-1, -2, and -3 in chondrocytes and association with integrin beta1". Histochem. Cell Biol. 113 (3): 221–5. doi:10.1007/s004180050441. PMID 10817676. S2CID 37932082.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
de Marco MC, Kremer L, Albar JP, et al. (2001). "BENE, a novel raft-associated protein of the MAL proteolipid family, interacts with caveolin-1 in human endothelial-like ECV304 cells". J. Biol. Chem. 276 (25): 23009–17. doi:10.1074/jbc.M009739200. PMID 11294831.
Andoh A, Saotome T, Sato H, et al. (2002). "Epithelial expression of caveolin-2, but not caveolin-1, is enhanced in the inflamed mucosa of patients with ulcerative colitis". Inflamm. Bowel Dis. 7 (3): 210–4. doi:10.1097/00054725-200108000-00005. PMID 11515846. S2CID 23977281.
Xu XR, Huang J, Xu ZG, et al. (2002). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089–94. Bibcode:2001PNAS...9815089X. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000105971 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000000058 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8552590-5] Scherer PE, Okamoto T, Chun M, Nishimoto I, Lodish HF, Lisanti MP (Feb 1996). "Identification, sequence, and expression of caveolin-2 defines a caveolin gene family". Proc Natl Acad Sci U S A. 93 (1): 131–5. Bibcode:1996PNAS...93..131S. doi:10.1073/pnas.93.1.131. PMC 40192. PMID 8552590.

[pmid10087206-6] 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.

[entrez-7] 1 2 3 "Entrez Gene: CAV2 caveolin 2".

[pmid9361015-8] 1 2 Scherer PE, Lewis R Y, Volonte D, Engelman J A, Galbiati F, Couet J, Kohtz D S, van Donselaar E, Peters P, Lisanti M P (Nov 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.

[pmid12091389-9] 1 2 Lee H, Park David S, Wang Xiao Bo, Scherer Philipp E, Schwartz Phillip E, Lisanti Michael P (Sep 2002). "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1". J. Biol. Chem. United States. 277 (37): 34556–67. doi:10.1074/jbc.M204367200. ISSN 0021-9258. PMID 12091389.

[pmid12414992-10] Breuza L, Corby Séverine, Arsanto Jean-Pierre, Delgrossi Marie-Hélène, Scheiffele Peter, Le Bivic André (Dec 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. S2CID 14788127.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

Interactions

References

Further reading