The Caveolin genes: from cell biology to medicine

References

• Palade GE. Fine Structure of Blood Capillaries. J Appl Physiol 1953;24:1424–36.
   Web of Science ®Google Scholar
• Glenney JR, Jr, Soppet D. Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts. Proc Natl Acad Sci USA 1992;89: 10517–21.
   Google Scholar
• Kurzchalia T, Dupree P, Parton RG, Kellner R, Virta H, Lehnert M, et al. VIP 21, A 21-kD membrane protein is an integral component of trans-Golgi-network-derived trans-port vesicles. J Cell Biol 1992;118:1003–14.
   PubMed Web of Science ®Google Scholar
• Simons K, Toomre D. Lipid Rafts and Signal Transduction. Nat Rev Mol Cell Biol 2000;1:31–9.
   PubMed Web of Science ®Google Scholar
• Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998;14:111–36.
   PubMed Web of Science ®Google Scholar
• Galbiati F, Razani B, Lisanti MP. Emerging themes in lipid rafts and caveolae. Cell 2001;106:403–11.
   Google Scholar
• Sargiacomo M, Sudol M, Tang Z-L, Lisanti MP. Signal transducing molecules and GPI-linked proteins form a caveolin- rich insoluble complex in MDCK cells. J Cell Biol 1993;122:789–807.
   Google Scholar
• Lisanti MP, Scherer PE, Vidugiriene J, Tang Z-L, Herma-noski-Vosatka A, Tu Y-H, et al. Characterization of caveolin-rich membrane domains isolated from an endothe-lial-rich source: Implications for human disease. J Cell Biol 1994;126:111–26.
   Google Scholar
• Lisanti MP, Scherer P, Tang Z-L, Sargiacomo M. Caveolae, caveolin and caveolin-rich membrane domains: A signalling hypothesis. Trends In Cell Biology 1994;4:231–5.
   Google Scholar
• Lisanti MP, Tang Z-T, Scherer P, Sargiacomo M. Caveolae purification and GPI-linked protein sorting in polarized epithelia. Meth Enzymol 1995;250:655–68.
   Google Scholar
• Lisanti MP, Sargiacomo M, Scherer PE. Purification of caveolae-derived membrane microdomains containing lipid-anchored signaling molecules, such as GPI-anchored pro-teins, H-Ras, Src- family tyrosine kinases, eNOS, and G-protein alpha-, beta-, and gamma- subunits. Methods Mol Biol 1999;116:51–60.
   Google Scholar
• Chang WJ, Ying YS, Rothberg KG, Hooper NM, Turner AJ, Gambliel HA, et al. Purification and characterization of smooth muscle cell caveolae. J Cell Biol 1994;126:127–38.
   PubMed Web of Science ®Google Scholar
• Razani B, Engelman JA, Wang XB, Schubert W, Zhang XL, Marks CB, et al. Caveolin-1 null mice are viable but show evidence of hyperproliferative and vascular abnormalities. J Biol Chem 2001;276:38121–38.
   PubMed Web of Science ®Google Scholar
• Razani B, Combs TP, Wang XB, Frank PG, Park DS, Russell RG, et al. Caveolin-1-deficient mice are lean, resistant to diet-induced obesity, and show hypertriglyceridemia with adipocyte abnormalities. J Biol Chem 2002;277:8635–47.
   PubMed Web of Science ®Google Scholar
• Razani B, Wang XB, Engelman JA, Battista M, Lagaud G, Zhang XL, et al. Caveolin-2-deficient mice show evidence of severe pulmonary dysfunction without disruption of caveo-lae. Mol Cell Biol 2002;22:2329–44.
   PubMed Web of Science ®Google Scholar
• Drab M, Verkade P, Elger M, Kasper M, Lohn M, Lauterbach B, et al. Loss of Caveolae, Vascular Dysfunction, and Pulmonary Defects in Caveolin-1 Gene-Disrupted Mice. Science 2001;293:2449–52.
   PubMed Web of Science ®Google Scholar
• Woodman SE, Cheung MW, Tarr M, North AC, Schubert W, Lagaud G, et al. Urogenital alterations in aged male caveolin-1 knockout mice. J Urol 2004;171(2 Pt 1)950–7.
   Google Scholar
• Galbiati F, Engelman JA, Volonte D, Zhang XL, Minetti C, Li M, et al. Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and T- tubule abnormalities. J Biol Chem 2001;19:19.
   Google Scholar
• Woodman SE, Park DS, Cohen AW, Cheung MW, Chandra M, Shirani J, et al. Caveolin-3 knock-out mice develop a progressive cardiomyopathy and show hyperactivation of the p42/44 MAPK cascade. J Biol Chem 2002;277:38988–97.
   PubMed Web of Science ®Google Scholar
• Scherer PE, Okamoto T, Chun M, Nishimoto I, Lodish HF, Lisanti MP. Identification, sequence and expression of caveolin-2 defines a caveolin gene family. Proc Natl Acad Sci USA 1996;93:131–5.
   PubMed Web of Science ®Google Scholar
• Scherer PE, Lewis RY, Volonte D, Engelman JA, Galbiati F, Couet J, et al. 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 1997;272: 29337–46.
   Google Scholar
• Parolini I, Sargiacomo M, Galbiati F, Rizzo G, Grignani F, Engelman JA, et al. Expression of caveolin-1 is required for the transport of caveolin-2 to the plasma membrane. Retention of caveolin-2 at the level of the Golgi complex. J Biol Chem 1999;274:25718–25.
   Google Scholar
• Tang Z-L, Scherer PE, Okamoto T, Song K, Chu C, Kohtz DS, et al. Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle. J Biol Chem 1996;271: 2255–61.
   Google Scholar
• Way M, Parton R. M-caveolin, a muscle-specific caveolin-related protein. FEBS Lett 1995;376:108–12.
   PubMed Web of Science ®Google Scholar
• Song KS, Scherer PE, Tang Z-L, Okamoto T, Li S, Chafel M, et al. Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystro-phin-associated glycoproteins. J Biol Chem 1996; 271: 15160–5.
   Google Scholar
• Glenney JR. The sequence of human caveolin reveals identity with VIP 21, a component of transport vesicles. FEBS Lett 1992;314:45–8.
   PubMed Web of Science ®Google Scholar
• Liu P, Rudick M, Anderson RG. Multiple functions of caveolin-1. J Biol Chem 2002;277: 41295–8.
   Google Scholar
• Scherer PE, Tang Z-L, Chun MC, Sargiacomo M, Lodish HF, Lisanti MP. Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution: Identification and epitope mapping of an isoform-specific monoclonal antibody probe. J Biol Chem 1995;270:16395–401.
   Google Scholar
• Sargiacomo M, Scherer PE, Tang Z-L, Kubler E, Song KS, Sanders MC, et al. Oligomeric structure of caveolin: Impli-cations for caveolae membrane organization. Proc Natl Acad Sci USA 1995;92:9407–11.
   PubMed Web of Science ®Google Scholar
• Li S, Couet J, Lisanti MP. Src tyrosine kinases, G alpha subunits and H-Ras share a common membrane-anchored scaffolding protein, Caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. J Biol Chem 1996;271:29182–90.
   Google Scholar
• Couet J, Li S, Okamoto T, Ikezu T, Lisanti MP. Identi-fication of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J Biol Chem 1997;272:6525–33.
   Google Scholar
• Razani B, Woodman SE, Lisanti MP. Caveolae: from cell biology to animal physiology. Pharmacol Rev 2002;54:431–67.
   Google Scholar
• Schnitzer JR, Liu J, Oh P. Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases. J Biol Chem 1995;270:14399–404.
   Google Scholar
• Oh P, McIntosh DP, Schnitzer JE. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endo-thelium. J Cell Biol 1998;141:101–14.
   Google Scholar
• Henley JR, Krueger EW, Oswald BJ, McNiven MA. Dynamin-mediated internalization of caveolae. J Cell Biol 1998;141:85–99.
   PubMed Web of Science ®Google Scholar
• Murata M, Peranen J, Schreiner R, Weiland F, Kurzchalia T, Simons K. VIP21/caveolin is a cholesterol-binding protein. Proc Natl Acad Sci USA 1995;92:10339–43.
   PubMed Web of Science ®Google Scholar
• Li S, Song KS, Lisanti MP. Expression and characterization of recombinant caveolin: Purification by poly-histidine tagging and cholesterol-dependent incorporation into defined lipid membranes. J Biol Chem 1996;271:568–73.
   Google Scholar
• Smart EJ, Anderson RG. Alterations in membrane choles-terol that affect structure and function of caveolae. Methods Enzymol 2002;353:131–9.
   PubMed Web of Science ®Google Scholar
• Engelman JA, Zhang XL, Razani B, Pestell RG, Lisanti MP. p42/44 MAP kinase-dependent and -independent signaling pathways regulate caveolin-1 gene expression. Activation of Ras-MAP kinase and protein kinase A signaling cascades transcriptionally down-regulates caveolin-1 promoter activ-ity. J Biol Chem 1999;274: 32333–41.
   Google Scholar
• Bist A, Fielding PE, Fielding CJ. Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol. Proc Natl Acad Sci USA 1997;94:10693–8.
   Google Scholar
• Smart EJ, Ying Y-s, Donzell WC, Anderson RGW. A role for caveolin in transport of cholesterol from endoplasmic reticu-lum to plasma membrane. J Biol Chem 1996;271:29427–35.
   Google Scholar
• Babitt J, Trigatti B, Rigotti A, Smart EJ, Anderson RGW, Xu S, et al. Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae. J Biol Chem 1997;272:13242–9.
   PubMed Web of Science ®Google Scholar
• Fielding CJ, Fielding PE. Caveolae and intracellular traffick-ing of cholesterol. Adv Drug Deliv Rev 2001;49:251–64.
   PubMed Web of Science ®Google Scholar
• Engelman JA, Chu C, Lin A, Jo H, Ikezu T, Okamoto T, et al. Caveolin-mediated regulation of signaling along the p42/ 44 MAP kinase cascade in vivo. A role for the caveolin-scaffolding domain. FEBS Lett 1998;428:205–11.
   PubMed Web of Science ®Google Scholar
• Galbiati F, Volonte D, Engelman JA, Watanabe G, Burk R, Pestell RG, et al. Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade. EMBO J 1998;17:6633–48.
   PubMed Web of Science ®Google Scholar
• Hulit J, Bash T, Fu M, Galbiati F, Albanese C, Sage DR, et al. The cyclin D1 gene is transcriptionally repressed by caveolin-1. J Biol Chem 2000;275:21203–9.
   PubMed Web of Science ®Google Scholar
• Glenney JR, Jr. Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus. J Biol Chem 1989;264:20163–6.
   PubMed Web of Science ®Google Scholar
• Koleske AJ, Baltimore D, Lisanti MP. Reduction of caveolin and caveolae in oncogenically transformed cells. Proc Natl Acad Sci USA 1995;92:1381–5.
   PubMed Web of Science ®Google Scholar
• Lee SW, Reimer CL, Oh P, Campbell DB, Schnitzer JR. Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells. Oncogene 1998;16:1391–7.
   Google Scholar
• Engelman JA, Wykoff CC, Yasuhara S, Song KS, Okamoto T, Lisanti MP. Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-inde-pendent growth. J Biol Chem 1997;272:16374–81.
   PubMed Web of Science ®Google Scholar
• Fiucci G, Ravid D, Reich R, Liscovitch M. Caveolin-1 inhibits anchorage-independent growth, anoikis and inva-siveness in MCF-7 human breast cancer cells. Oncogene 2002;21:2365–75.
   PubMed Web of Science ®Google Scholar
• Scheel J, Srinivasan J, Honnert U, Henske A, Kurzchalia TV. Involvement of caveolin-1 in meiotic cell-cycle progression in Caenorhabditis elegans. Nat Cell Biol 1999;1: 127–9.
   Google Scholar
• Galbiati F, Volonte D, Liu J, Capozza F, Frank PG, Zhu L, et al. Caveolin-1 expression negatively regulates cell cycle progression by inducing G(0)/G(1) arrest via a p53/ p21(WAF1/Cip1)-dependent mechanism. Mol Biol Cell 2001;12:2229–44.
   PubMed Web of Science ®Google Scholar
• Williams TM, Lee H, Cheung MW, Cohen AW, Razani B, Iyengar P, et al. Combined loss of INK4a and caveolin-1 synergistically enhances cell proliferation and oncogene-induced tumorigenesis. J Biol Chem 2004;279:24745–56.
   PubMed Web of Science ®Google Scholar
• Park WY, Park JS, Cho KA, Kim DI, Ko YG, Seo JS, et al. Up-regulation of caveolin attenuates epidermal growth factor signaling in senescent cells. J Biol Chem 2000;275: 20847–52.
   PubMed Web of Science ®Google Scholar
• Lu Z, Ghosh S, Wang Z, Hunter T. Downregulation of caveolin-1 function by EGF leads to the loss of E-cadherm, increased transcriptional activity of heta-catemn, and enhanced tumor cell invasion. Cancer Cell 2003;4:499–515.
   PubMed Web of Science ®Google Scholar
• Hayashi K, Matsuda S, Machida K, Yamamoto T, Fukuda Y, Nimura Y, et al. Invasion activating caveolin-1 mutation in human scirrhous breast cancers. Cancer Res 2001; 61: 2361–4.
   PubMed Web of Science ®Google Scholar
• Han SE, Park KH, Lee G, Huh YJ, Min BM. Mutation and aberrant expression of Caveolin-1 in human oral squamous cell carcinomas and oral cancer cell lines. Int J Oncol 2004; 24:435–40.
   Google Scholar
• Aldred MA, Ginn-Pease ME, Morrison CD, Popkie AP, Gimm O, Hoang-Vu C, et al. Caveolin-1 and caveolin-2,together with three bone morphogenetic protein-related genes, may encode novel tumor suppressors down-regulated in sporadic follicular thyroid carcinogenesis. Cancer Res 2003;63:2864–71.
   PubMed Web of Science ®Google Scholar
• Engelman JA, Zhang XL, Lisanti MP. 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 1998;436: 403–10.
   Google Scholar
• Razam B, Schlegel A, Liu J, Lisanti MP. Caveolin-1, a putative tumour suppressor gene. Biochem Soc Trans 2001; 29:494–9.
   PubMed Web of Science ®Google Scholar
• Capozza F, Williams TM, Schubert W, McClain S, Bouzah-zah B, Sotgia F, et al. Absence of caveolin-1 sensitizes mouse skin to carcinogen-induced epidermal hyperplasia and tumor
   Google Scholar
• Williams TM, Cheung MW, Park DS, Razani B, Cohen AW, Muller WJ, et al. Loss of caveolin-1 gene expression accelerates the development of dysplastic mammary lesions
   Google Scholar
• Schubert W, Frank PG, Razani B, Park DS, Chow CW, Lisanti MP. Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo. J Biol Chem
   Google Scholar
• Schubert W, Frank PG, Woodman SE, Hyogo H, Cohen DE, Chow CW, et al. Microvascular hyperpermeability in caveolin-1 (-/-) knock-out mice. Treatment with a specific
   Google Scholar
• Bucci M, Gratton JP, Rudic RD, Acevedo L, Roviezzo F, Cirino G, et al. In vivo delivery of the caveolin-1 scaffolding
   Google Scholar
• Woodman SE, Ashton AW, Schubert W, Lee H, Williams TM, Medina FA, et al. Caveolin-1 knockout mice show an impaired angiogenic response to exogenous stimuli. Am J Pathol 2003;162:2059–68.
   PubMed Web of Science ®Google Scholar
• Liu J, Wang XB, Park DS, Lisanti MP. Caveolin-1 expression enhances endothelial capillary tubule formation. J Biol Chem 2002;277:10661–8.
   PubMed Web of Science ®Google Scholar
• Frank PG, Lee H, Park DS, Tandon NN, Scherer PE, Lisanti MP. Genetic ablation of caveolin-1 confers protection against atherosclerosis. Arterioscler Thromb Vasc Biol
   Google Scholar
• Hassan GS, Jasmin JF, Schubert W, Frank PG, Lisanti MP. Caveolin-1 Deficiency Stimulates Neointima Formation during Vascular Injury. Biochemistry 2004;43:8312-21. Newman GR, Campbell L, von Ruhland C, Jasani B, Gumbleton M. Caveolin and its cellular and subcellular immunolocalisation in lung alveolar epithelium: implications for alveolar epithelial type I cell function. Cell Tissue Res 1999;295: 111–20.
   Google Scholar
• Newman GR, Campbell L, von Ruhland C, Jasam B, Gumbleton M. Caveolin and its cellular and subcellular immunolocalisation in lung alveolar epithelium: implications for alveolar epithelial type I cell function. Cell Tissue Res 1999;295:111–20.
   Google Scholar
• Park DS, Cohen AW, Frank PG, Razani B, Lee H, Williams TM, et al. Caveolin-1 null (-/-) mice show dramatic reductions in life span. Biochemistry 2003;42:15124-31. Zhao YY, Liu Y, Stan RV, Fan L, Gu Y, Dalton N, et al. Defects in caveolin-1 cause dilated cardiomyopathy and pulmonary hypertension in knockout mice. Proc Natl Acad Sci USA 2002;99: 11375–80.
   Google Scholar
• Zhao YY, Liu Y, Stan RV, Fan L, Gu Y, Dalton N, et al. Defects in caveolin-1 cause dilated cardiomyopathy and pulmonary hypertension in knockout mice. Proc Natl Acad Sci USA 2002;99:11375–80.
   PubMed Web of Science ®Google Scholar
• Cohen AW, Park DS, Woodman SE, Williams TM, Chandra M, Shirani J, et al. Caveolin-1 null mice develop cardiac hypertrophy with hyperactivation of p42/44 MAP kinase in cardiac fibroblasts. Am J Physiol Cell Physiol 2003; 284: C457–74.
   PubMed Web of Science ®Google Scholar
• Park DS, Woodman SE, Schubert W, Cohen AW, Frank PG, Chandra M, et al. Caveolin-1/3 double-knockout mice are viable, but lack both muscle and non-muscle caveolae, and develop a severe cardiomyopathic phenotype. Am J Pathol 2002;160:2207–17.
   PubMed Web of Science ®Google Scholar
• Michel JB, Feron 0, Sacks D, Michel T. Reciprocal regulation of endothelial nitric-oxide synthase by Ca2+-calmodulin and caveolin. J Biol Chem 1997;272: 15583–6.
   Google Scholar
• Ju H, Zou R, Venema VJ, Venema RC. Direct Interaction of Endothelial Nitric-oxide Synthase and Caveolin-1 Inhibits Synthase Activity. J Biol Chem 1997;272:18522–5.
   PubMed Web of Science ®Google Scholar
• Garcia-Cardena G, Martasek P, Siler-Masters BS, Skidd PM, Couet JC, Li S, et al. Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: Functional significance of the NOS caveolin binding domain in vivo. J Biol Chem (Communication) 1997;272:25437–40.
   Google Scholar
• Aravamudan B, Volonte D, Ramani R, Gursoy E, Lisanti MP, London B, et al. Transgenic overexpression of caveolin-3 in the heart induces a cardiomyopathic phenotype. Hum Mol Genet 2003;12:2777–88.
   PubMed Web of Science ®Google Scholar
• Hayashi T, Arimura T, Ueda K, Shibata H, Hohda S, Takahashi M, et al. Identification and functional analysis of a caveolin-3 mutation associated with familial hypertrophic cardiomyopathy. Biochem Biophys Res Commun 2004;313: 178–84.
   PubMed Web of Science ®Google Scholar
• Minetti C, Sotogia F, Bruno C, Scartezzini P, Broda P, Bado M, et al. Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy. Nat Genet 1998; 18:365–8.
   PubMed Web of Science ®Google Scholar
• Galbiati F, Volonte D, Minetti C, Chu JB, Lisanti MP. Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C). Retention of LGMD-1C caveolin-3 mutants within the Golgi complex. J Biol Chem 1999;274:25632-41. Galbiati F, Volonte D, Minetti C, Bregman DB, Lisanti MP. Limb-girdle muscular dystrophy (LGMD-1C) mutants of caveolin-3 undergo ubiquitination and proteasomal degrada-tion. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-1C mutants and rescues wild-type caveolin-3. J Biol Chem 2000;275: 37702–11.
   Google Scholar
• Galbiati F, Volont� D, Minetti C, Bregman DB, Lisanti MP. Limb-girdle muscular dystrophy (LGMD-IC) mutants of caveolin-3 undergo ubiquitination and proteasomal degradation. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-IC mutants and rescues wild-type caveolin-3. J Biol Chem 2000;275: 37702–11.
   Google Scholar
• Lee H, Park DS, Razani B, Russell RG, Pestell RG, Lisanti MP. Caveolin-1 mutations (P132L and null) and the patho-genesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia. Am J Pathol 2002;161:1357–69.
   PubMed Web of Science ®Google Scholar
• Sunada Y, Ohi H, Hase A, Hosono T, Arata S, Higuchi S, et al. Transgenic mice expressing mutant caveolin-3 show severe myopathy associated with increased nNOS activity. Hum Mol Genet 2001;10:173–8.
   PubMed Web of Science ®Google Scholar
• Hagiwara Y, Sasaoka T, Araishi K, Imamura M, Yorifuji H, Nonaka I, et al. Caveolin-3 deficiency causes muscle degeneration in mice. Hum Mol Genet 2000;9:3047–54.
   PubMed Web of Science ®Google Scholar
• Vaghy PL, Fang J, Wu W, Vaghy LP. Increased caveolin-3 levels in mdx mouse muscles. FEBS Lett 1998;431:125–7.
   PubMed Web of Science ®Google Scholar
• Repetto S, Bado M, Broda P, Lucania G, Masetti E, Sotgia F, et al. Increased number of caveolae and caveolin-3 over-expression in Duchenne muscular dystrophy. Biochem Biophys Res Commun 1999;261:547–50.
   PubMed Web of Science ®Google Scholar
• Galbiati F, Volonte D, Chu JB, Li M, Fine SW, Fu M, et al. Transgenic overexpression of caveolin-3 in skeletal muscle fibers induces a Duchenne-like muscular dystrophy pheno-type. Proc Natl Acad Sci USA 2000;97:9689–94.
   PubMed Web of Science ®Google Scholar
• McNally EM, de Sá, Moreira E, Duggan DJ, Bönnemann CG, Lisanti MP, Lidov HGW, et al. Caveolin-3 in muscular dystrophy. Hum Mol Genet 1998;7: 871–7.
   Google Scholar
• Sotgia F, Lee JK, Das K, Bedford M, Petrucci TC, Macioce P, et al. 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 2000;275:38048–58.
   Google Scholar
• Sotgia F, Bonuccelli G, Minetti C, Woodman SE, Capozza F, Kemp RG, et al. Phosphofructokinase muscle-specific iso-form requires caveolin-3 expression for plasma membrane recruitment and caveolar targeting: implications for the pathogenesis of caveolin-related muscle diseases. Am J Pathol 2003;163:2619–34.
   PubMed Web of Science ®Google Scholar
• Smythe GM, Eby JC, Disatnik MH, Rando TA. A caveolin-3 mutant that causes limb girdle muscular dystrophy type 1 C disrupts Src localization and activity and induces apoptosis in skeletal myotubes. J Cell Sci 2003;116:4739–49.
   PubMed Web of Science ®Google Scholar
• Betz RC, Schoser BG, Kasper D, Ricker K, Ramirez A, Stein V, et al. Mutations in CAV3 cause mechanical hyperirrit-ability of skeletal muscle in rippling muscle disease. Nat Genet 2001;28:218–9.
   PubMed Web of Science ®Google Scholar
• Kubisch C, Schoser BG, von During M, Betz RC, Goebel HH, Zahn S, et al. Homozygous mutations in caveolin-3 cause a severe form of rippling muscle disease. Ann Neurol 2003;53:512–20.
   PubMed Web of Science ®Google Scholar
• Carbone I, Bruno C, Sotgia F, Bado M, Broda P, Masetti E, et al. Mutation in the CAV3 gene causes partial caveolin-3 deficiency and hyperCKemia. Neurology 2000;54:1373–6.
   PubMed Web of Science ®Google Scholar
• Woodman SE, Sotgia F, Galbiati F, Minetti C, Lisanti MP. Caveolinopathies: mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases. Neurology 2004; 62: 538–43.
   Google Scholar
• Cao G, Yang G, Timme TL, Saika T, Truong LD, Satoh T, et al. Disruption of the caveolin-1 gene impairs renal calcium reabsorption and leads to hypercalciuria and urolithiasis. Am J Pathol 2003;162:1241–8.
   PubMed Web of Science ®Google Scholar
• Scherer PE, Lisanti MP, Baldini G, Sargiacomo M, Corley-Mastick C, Lodish HF. Induction of caveolin during adipo-genesis and association of GLUT4 with caveolin-rich vesicles. J Cell Biol 1994;127: 1233–43.
   Google Scholar
• Cohen AW, Razani B, Schubert W, Williams TM, Wang XB, Iyengar P, et al. Role of caveolin-1 in the modulation of lipolysis and lipid droplet formation. Diabetes 2004;53:1261–70.
   PubMed Web of Science ®Google Scholar
• Gustavsson J, Parpal S, Stralfors P. Insulin-stimulated glucose uptake involves the transition of glucose transporters to a caveolae-rich fraction within the plasma membrane: implications for type II diabetes. Mol Med 1996;2:367–72.
   Google Scholar
• Karlsson M, Thorn H, Parpal S, Stralfors P, Gustavsson J. Insulin induces translocation of glucose transporter GLUT4 to plasma membrane caveolae in adipocytes. FASEB J 2002; 16:249–51.
   Google Scholar
• Ros-Baro A, Lopez-Iglesias C, Peiro S, Bellido D, Palacin M, Zorzano A, et al. Lipid rafts are required for GLUT4 internalization in adipose cells. Proc Natl Acad Sci USA 2001; 98:12050–5.
   PubMed Web of Science ®Google Scholar
• Shigematsu S, Watson RT, Khan AH, Pessin JE. The adipocyte plasma membrane caveolin functional/structural organization is necessary for the efficient endocytosis of GLUT4. J Biol Chem 2003;278:10683–90.
   PubMed Web of Science ®Google Scholar
• Smith RM, Harada S, Smith JA, Zhang S, Jarett L. Insulin-induced protein tyrosine phosphorylation cascade and signalling molecules are localized in a caveolin-enriched cell membrane domain. Cell Signal 1998;10:355–62.
   Google Scholar
• Yamamoto M, Toya Y, Schwencke C, Lisanti MP, Myers M, Ishikawa Y. Caveolin is an activator of insulin receptor signaling. J Biol Chem 1998;273:26962–8.
   PubMed Web of Science ®Google Scholar
• Gustavsson J, Parpal S, Karlsson M, Ramsing C, Thorn H, Borg M, et al. Localization of the insulin receptor in caveolae of adipocyte plasma membrane. FASEB J 1999;13:1961–71.
   PubMed Web of Science ®Google Scholar
• Nystrom FH, Chen H, Cong LN, Li Y, Quon M J. Caveolin-1 interacts with the insulin receptor and can differentially modulate insulin signaling in transfected Cos-7 cells and rat adipose cells. Mol Endocrinol 1999;13:2013–24.
   Google Scholar
• Kimura A, Mora S, Shigematsu S, Pessin JE, Saltiel AR. The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1. J Biol Chem 2002;277: 30153–8.
   Google Scholar
• Parpal S, Karlsson M, Thorn H, Stralfors P. Cholesterol depletion disrupts caveolae and insulin receptor signaling for metabolic control via insulin receptor substrate-1, but not for mitogen-activated protein kinase control. J Biol Chem 2001; 276:9670–8.
   PubMed Web of Science ®Google Scholar
• Cohen AW, Razani B, Wang XB, Combs TP, Williams TM, Scherer PE, et al. Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue. Am J Physiol Cell Physiol 2003;285:C222–35.
   PubMed Web of Science ®Google Scholar