Caveolin 3
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| Location (UCSC) | Chr 3: 8.73 – 8.84 Mb | Chr 6: 112.44 – 112.45 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
Caveolin-3 is a protein that in humans is encoded by the CAV3 gene.[5][6][7] 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.
Function
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.[7]
Clinical significance
Mutations identified in this gene lead to interference with protein oligomerization or intra-cellular routing, disrupting caveolae formation and resulting in
Interactions
Caveolin 3 has been shown to
Structure
Using transmission electron microscopy and single particle analysis methods, it has been shown that nine Caveolin-3 monomers assemble to form a complex that is toroidal in shape, ~16.5 nm in diameter and ~5.5 nm in height.[13]
Cardiac physiology
Caveolin-3 is one of three isoforms of the protein
Associations with ion channels
ATP-dependent potassium channels
In cardiac myocytes, caveolin-3 negatively regulates ATP-dependent potassium channels (KATP) localized in caveolae.[18] KATP channel opening decreases significantly when interacting with caveolin-3; other isoforms of caveolin do not show this type of effect on KATP channels. The amount of KATP activation during times of biological stress influences the amount of cellular damage that will occur, thus regulation of caveolin-3 expression during these times influences the amount of cellular damage.[18]
Sodium-calcium exchanger
Caveolin-3 associates with the cardiac sodium-calcium exchanger (NCX) in caveolae of cardiac myocytes.[14][24] This association occurs predominately in areas proximate to the peripheral membrane of cardiac myocytes.[24] Interactions between caveolin-3 and cardiac NCX influence NCX-regulation of cellular signaling factors and excitation of cardiac myocytes.[14]
L-Type calcium channel
Caveolin-3 influences the opening of
Implications in disease
Alterations in caveolin-3 expression have been implicated in the altered expression and regulation of numerous signaling molecules involved in
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000182533 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000062694 – 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.
- PMID 9536092.
- S2CID 35061895.
- ^ a b c "Entrez Gene: CAV3 caveolin 3".
- PMID 24021552.
- PMID 10988290.
- PMID 11532985.
- PMID 9374534.
- PMID 23071107.
- PMID 23071107.
- ^ S2CID 19419069.
- PMID 19584897.
- PMID 15192036.
- ^ PMID 24412535.
- ^ PMID 19481058.
- ^ PMID 12966035.
- ^ PMID 14672715.
- ^ PMID 21616289.
- ^ PMID 12847114.
- ^ PMID 12138167.
- ^ PMID 19250668.
- ^ PMID 16186065.
Further reading
- Figarella-Branger D, Pouget J, Bernard R, Krahn M, Fernandez C, Lévy N, Pellissier JF (2004). "Limb-girdle muscular dystrophy in a 71-year-old woman with an R27Q mutation in the CAV3 gene". Neurology. 61 (4): 562–4. S2CID 40129179.
- Woodman SE, Sotgia F, Galbiati F, Minetti C, Lisanti MP (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, Sargiacomo M, Casanova JE, Hansen SH, Nishimoto I, Lisanti MP (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, Song K, Chu C, Kohtz DS, Nishimoto I, Lodish HF, Lisanti MP (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.
- 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, Lisanti MP, Myers MG, Ishikawa Y (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. S2CID 44686134.
- Carbone I, Bruno C, Sotgia F, Bado M, Broda P, Masetti E, Panella A, Zara F, Bricarelli FD, Cordone G, Lisanti MP, Minetti C (2000). "Mutation in the CAV3 gene causes partial caveolin-3 deficiency and hyperCKemia". Neurology. 54 (6): 1373–6. S2CID 74588429.
- Biederer CH, Ries SJ, Moser M, Florio M, Israel MA, McCormick F, Buettner R (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. PMID 10835421.
- Sotgia F, Lee JK, Das K, Bedford M, Petrucci TC, Macioce P, Sargiacomo M, Bricarelli FD, Minetti C, Sudol M, Lisanti MP (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. PMID 10988290.
- Herrmann R, Straub V, Blank M, Kutzick C, Franke N, Jacob EN, Lenard HG, Kröger S, Voit T (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, Imamura M, Yorifuji H, Nonaka I, Ozawa E, Kikuchi T (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, McNally E, Kunkel LM, Zatz M (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, Ricker K, Ramírez A, Stein V, Torbergsen T, Lee YA, Nöthen MM, Wienker TF, Malin JP, Propping P, Reis A, Mortier W, Jentsch TJ, Vorgerd M, Kubisch C (2001). "Mutations in CAV3 cause mechanical hyperirritability of skeletal muscle in rippling muscle disease". Nat. Genet. 28 (3): 218–9. S2CID 35194603.
- Matsuda C, Hayashi YK, Ogawa M, Aoki M, Murayama K, Nishino I, Nonaka I, Arahata K, Brown RH (2002). "The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle". Hum. Mol. Genet. 10 (17): 1761–6. PMID 11532985.