Caveolin 2

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Caveolin 2
Identifiers
Symbols CAV2 ; CAV
External IDs OMIM601048 MGI107571 HomoloGene942 GeneCards: CAV2 Gene
RNA expression pattern
PBB GE CAV2 203323 at tn.png
PBB GE CAV2 203324 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 858 12390
Ensembl ENSG00000105971 ENSMUSG00000000058
UniProt P51636 Q9WVC3
RefSeq (mRNA) NM_001206747 NM_001277756
RefSeq (protein) NP_001193676 NP_001264685
Location (UCSC) Chr 7:
115.93 – 116.15 Mb
Chr 6:
17.28 – 17.29 Mb
PubMed search [1] [2]

Caveolin-2 is a protein that in humans is encoded by the CAV2 gene.123

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. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. 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.3

Interactions

Caveolin 2 has been shown to interact with Caveolin 145 and RAS p21 protein activator 1.6

References

  1. ^ 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. doi:10.1073/pnas.93.1.131. PMC 40192. PMID 8552590. 
  2. ^ 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. 
  3. ^ a b "Entrez Gene: CAV2 caveolin 2". 
  4. ^ Breuza, Lionel; 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. 
  5. ^ Scherer, P E; 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. 
  6. ^ Lee, Hyangkyu; 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. 

Further reading










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