Caveolin 3

From Wikipedia, the free encyclopedia

Caveolin 3

Identifiers

CAV3; VIP21; LGMD1C; MGC126100; MGC126101; MGC126129; VIP-21

External IDs

OMIM: 601253 MGI: 107570 HomoloGene: 7255

Gene ontology
Molecular Function:	• protein binding
Cellular Component:	• membrane fraction • dystrophin-associated glycoprotein complex • membrane • integral to membrane • caveolar membrane
Biological Process:	• muscle development

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001234 (mRNA)
NP_001225 (protein)

XM_973503 (mRNA)
XP_978597 (protein)

Location

Chr 3: 8.75 - 8.76 Mb

Chr 6: 112.43 - 112.44 Mb

Pubmed search

[1]

[2]

Caveolin 3, also known as CAV3, is a human gene.^[1]

This gene encodes a caveolin family member, which functions as a component of the caveolae plasma membranes found in most cell types. Caveolin proteins are proposed to be scaffolding proteins for organizing and concentrating certain caveolin-interacting molecules. Mutations identified in this gene lead to interference with protein oligomerization or intra-cellular routing, disrupting caveolae formation and resulting in Limb-Girdle muscular dystrophy type-1C (LGMD-1C), hyperCKemia or rippling muscle disease (RMD). Alternative splicing has been identified for this locus, with inclusion or exclusion of a differentially spliced intron. In addition, transcripts utilize multiple polyA sites and contain two potential translation initiation sites.^[1]

[edit] References

^ ^a ^b Entrez Gene: CAV3 caveolin 3.

[edit] Further reading

Figarella-Branger D, Pouget J, Bernard R, et al. (2004). "Limb-girdle muscular dystrophy in a 71-year-old woman with an R27Q mutation in the CAV3 gene.". Neurology 61 (4): 562–4. PMID 12939441.
Woodman SE, Sotgia F, Galbiati F, et al. (2005). "Caveolinopathies: mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases.". Neurology 62 (4): 538–43. PMID 14981167.
Li S, Okamoto T, Chun M, et al. (1995). "Evidence for a regulated interaction between heterotrimeric G proteins and caveolin.". J. Biol. Chem. 270 (26): 15693–701. PMID 7797570.
Tang Z, Scherer PE, Okamoto T, et al. (1996). "Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle.". J. Biol. Chem. 271 (4): 2255–61. PMID 8567687.
Scherer PE, Lisanti MP (1997). "Association of phosphofructokinase-M with caveolin-3 in differentiated skeletal myotubes. Dynamic regulation by extracellular glucose and intracellular metabolites.". J. Biol. Chem. 272 (33): 20698–705. PMID 9252390.
Venema VJ, Ju H, Zou R, Venema RC (1997). "Interaction of neuronal nitric-oxide synthase with caveolin-3 in skeletal muscle. Identification of a novel caveolin scaffolding/inhibitory domain.". J. Biol. Chem. 272 (45): 28187–90. PMID 9353265.
Couet J, Sargiacomo M, Lisanti MP (1997). "Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities.". J. Biol. Chem. 272 (48): 30429–38. PMID 9374534.
McNally EM, de Sá Moreira E, Duggan DJ, et al. (1998). "Caveolin-3 in muscular dystrophy.". Hum. Mol. Genet. 7 (5): 871–7. PMID 9536092.
Minetti C, Sotgia F, Bruno C, et al. (1998). "Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy.". Nat. Genet. 18 (4): 365–8. doi:10.1038/ng0498-365. PMID 9537420.
Biederer C, Ries S, Drobnik W, Schmitz G (1998). "Molecular cloning of human caveolin 3.". Biochim. Biophys. Acta 1406 (1): 5–9. PMID 9545514.
Yamamoto M, Toya Y, Schwencke C, et al. (1998). "Caveolin is an activator of insulin receptor signaling.". J. Biol. Chem. 273 (41): 26962–8. PMID 9756945.
Sotgia F, Minetti C, Lisanti MP (1999). "Localization of the human caveolin-3 gene to the D3S18/D3S4163/D3S4539 locus (3p25), in close proximity to the human oxytocin receptor gene. Identification of the caveolin-3 gene as a candidate for deletion in 3p-syndrome.". FEBS Lett. 452 (3): 177–80. PMID 10386585.
Carbone I, Bruno C, Sotgia F, et al. (2000). "Mutation in the CAV3 gene causes partial caveolin-3 deficiency and hyperCKemia.". Neurology 54 (6): 1373–6. PMID 10746614.
Biederer CH, Ries SJ, Moser M, et al. (2000). "The basic helix-loop-helix transcription factors myogenin and Id2 mediate specific induction of caveolin-3 gene expression during embryonic development.". J. Biol. Chem. 275 (34): 26245–51. doi:10.1074/jbc.M001430200. PMID 10835421.
Sotgia F, Lee JK, Das K, et al. (2001). "Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members.". J. Biol. Chem. 275 (48): 38048–58. doi:10.1074/jbc.M005321200. PMID 10988290.
Herrmann R, Straub V, Blank M, et al. (2001). "Dissociation of the dystroglycan complex in caveolin-3-deficient limb girdle muscular dystrophy.". Hum. Mol. Genet. 9 (15): 2335–40. PMID 11001938.
Hagiwara Y, Sasaoka T, Araishi K, et al. (2001). "Caveolin-3 deficiency causes muscle degeneration in mice.". Hum. Mol. Genet. 9 (20): 3047–54. PMID 11115849.
de Paula F, Vainzof M, Bernardino AL, et al. (2001). "Mutations in the caveolin-3 gene: When are they pathogenic?". Am. J. Med. Genet. 99 (4): 303–7. PMID 11251997.
Betz RC, Schoser BG, Kasper D, et al. (2001). "Mutations in CAV3 cause mechanical hyperirritability of skeletal muscle in rippling muscle disease.". Nat. Genet. 28 (3): 218–9. doi:10.1038/90050. PMID 11431690.
Matsuda C, Hayashi YK, Ogawa M, et al. (2002). "The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle.". Hum. Mol. Genet. 10 (17): 1761–6. PMID 11532985.