메뉴 건너뛰기




Volumn 8, Issue 3, 2007, Pages 185-194

The multiple faces of caveolae

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLIN 1; CAVEOLIN 2; CAVEOLIN 3; DYNAMIN; DYSFERLIN; FIBRONECTIN; GLYCOSYLPHOSPHATIDYLINOSITOL; MEMBRANE PROTEIN; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; SMALL INTERFERING RNA; SNARE PROTEIN;

EID: 33847181297     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2122     Document Type: Review
Times cited : (1224)

References (141)
  • 1
    • 0000855817 scopus 로고
    • Fine structure of blood capillaries
    • Palade, G.E. Fine structure of blood capillaries. J. Appl. Phys. 24, 1424 (1953).
    • (1953) J. Appl. Phys , vol.24 , pp. 1424
    • Palade, G.E.1
  • 2
    • 77049234363 scopus 로고
    • The fine structures of the gall bladder epithelium of the mouse
    • Yamada, E. The fine structures of the gall bladder epithelium of the mouse. J. Biophys. Biochem. Cytol. 1, 445-458 (1955).
    • (1955) J. Biophys. Biochem. Cytol , vol.1 , pp. 445-458
    • Yamada, E.1
  • 3
    • 29144534595 scopus 로고    scopus 로고
    • Structure of caveolae
    • Stan, R.V. Structure of caveolae. Biochim. Biophys. Acta 1746, 334-348 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 334-348
    • Stan, R.V.1
  • 4
    • 3342972122 scopus 로고    scopus 로고
    • Stan, R.V., Tkachenko, E. & Niesman, I.R. PV1 is a key structural component for the formation of the stomatal and fenestral diaphragms. Mol. Biol. Cell 15, 3615-3630 (2004).
    • Stan, R.V., Tkachenko, E. & Niesman, I.R. PV1 is a key structural component for the formation of the stomatal and fenestral diaphragms. Mol. Biol. Cell 15, 3615-3630 (2004).
  • 5
    • 0029204576 scopus 로고
    • Caveolae, transmembrane signalling and cellular transformation
    • Lisanti, M.P. et al. Caveolae, transmembrane signalling and cellular transformation. Mol. Membr. Biol. 12, 121-124 (1995).
    • (1995) Mol. Membr. Biol , vol.12 , pp. 121-124
    • Lisanti, M.P.1
  • 7
    • 13644266312 scopus 로고    scopus 로고
    • Caveolin-1 in oncogenic transformation, cancer, and metastasis
    • Williams, T.M. & Lisanti, M.P. Caveolin-1 in oncogenic transformation, cancer, and metastasis. Am. J. Physiol. Cell Physiol. 288, C494-C506 (2005).
    • (2005) Am. J. Physiol. Cell Physiol , vol.288
    • Williams, T.M.1    Lisanti, M.P.2
  • 8
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans, L., Kartenbeck, J. & Helenius, A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nature Cell Biol. 3, 473-483 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 9
    • 0034604515 scopus 로고    scopus 로고
    • Involvement of cellular caveolae in bacterial entry into mast cells
    • Shin, J.S., Gao, Z. & Abraham, S.N. Involvement of cellular caveolae in bacterial entry into mast cells. Science 289, 785-788 (2000).
    • (2000) Science , vol.289 , pp. 785-788
    • Shin, J.S.1    Gao, Z.2    Abraham, S.N.3
  • 10
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin
    • Fra, A.M., Williamson, E., Simons, K. & Parton, R.G. De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin. Proc. Natl Acad. Sci. USA 92, 8655-8659 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8655-8659
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 11
    • 0035964954 scopus 로고    scopus 로고
    • Loss of caveolae, vascular dysfunction, and pulmonary defects in Caveolin-1 gene-disrupted mice
    • Drab, M. et al. Loss of caveolae, vascular dysfunction, and pulmonary defects in Caveolin-1 gene-disrupted mice. Science 293, 2449-2452 (2001).
    • (2001) Science , vol.293 , pp. 2449-2452
    • Drab, M.1
  • 12
    • 0035877753 scopus 로고    scopus 로고
    • Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities
    • Galbiati, F. 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. 276, 21425-21433 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 21425-21433
    • Galbiati, F.1
  • 13
    • 0030060941 scopus 로고    scopus 로고
    • Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle
    • Tang, Z. et al. Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle. J. Biol. Chem. 271, 2255-2261 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 2255-2261
    • Tang, Z.1
  • 14
    • 0030561979 scopus 로고
    • M-caveolin, a muscle-specific caveolin-related protein
    • Way, M. & Parton, R.G. M-caveolin, a muscle-specific caveolin-related protein. FEBS Lett. 376, 108-112 (1995).
    • (1995) FEBS Lett , vol.376 , pp. 108-112
    • Way, M.1    Parton, R.G.2
  • 15
    • 0036123019 scopus 로고    scopus 로고
    • Caveolin-2-deficient mice show evidence of severe pulmonary dysfunction without disruption of caveolae
    • Razani, B. et al. Caveolin-2-deficient mice show evidence of severe pulmonary dysfunction without disruption of caveolae. Mol. Cell. Biol. 22, 2329-2344 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 2329-2344
    • Razani, B.1
  • 16
    • 0038313015 scopus 로고    scopus 로고
    • The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation
    • Sowa, G., Pypaert, M., Fulton, D. & Sessa, W.C. The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation. Proc. Natl Acad. Sci. USA 100, 6511-6516 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6511-6516
    • Sowa, G.1    Pypaert, M.2    Fulton, D.3    Sessa, W.C.4
  • 17
    • 0037434839 scopus 로고    scopus 로고
    • Involvement of caveolin-2 in caveolar biogenesis in MDCK cells
    • Lahtinen, U., Honsho, M., Parton, R.G., Simons, K. & Verkade, P. Involvement of caveolin-2 in caveolar biogenesis in MDCK cells. FEBS Lett. 538, 85-88 (2003).
    • (2003) FEBS Lett , vol.538 , pp. 85-88
    • Lahtinen, U.1    Honsho, M.2    Parton, R.G.3    Simons, K.4    Verkade, P.5
  • 18
    • 0028885614 scopus 로고
    • VIP21/caveolin is a cholesterol-binding protein
    • Murata, M. et al. VIP21/caveolin is a cholesterol-binding protein. Proc. Natl Acad. Sci. USA 92, 10339-10343 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10339-10343
    • Murata, M.1
  • 19
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae
    • Dietzen, D.J., Hastings, W.R. & Lublin, D.M. Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae. J. Biol. Chem. 270, 6838-6842 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 20
    • 0026559095 scopus 로고
    • Caveolin, a protein component of caveolae membrane coats
    • Rothberg, K.G. et al. Caveolin, a protein component of caveolae membrane coats. Cell 68, 673-682 (1992).
    • (1992) Cell , vol.68 , pp. 673-682
    • Rothberg, K.G.1
  • 21
    • 21844454457 scopus 로고    scopus 로고
    • Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae
    • Pelkmans, L. & Zerial, M. Kinase-regulated quantal assemblies and kiss-and-run recycling of caveolae. Nature 436, 128-133 (2005).
    • (2005) Nature , vol.436 , pp. 128-133
    • Pelkmans, L.1    Zerial, M.2
  • 22
    • 2442653807 scopus 로고    scopus 로고
    • Ortegren, U. et al. Lipids and glycosphingolipids in caveolae and surrounding plasma membrane of primary rat adipocytes. Eur. J. Biochem. 271, 2028-2036 (2004). Quantification of lipid levels within caveolae shows that glycosphingolipids and cholesterol are concentrated more within caveolae compared with the surrounding plasma membrane. Higher packing of total lipids is observed in caveolae compared with the surrounding plasma membrane.
    • Ortegren, U. et al. Lipids and glycosphingolipids in caveolae and surrounding plasma membrane of primary rat adipocytes. Eur. J. Biochem. 271, 2028-2036 (2004). Quantification of lipid levels within caveolae shows that glycosphingolipids and cholesterol are concentrated more within caveolae compared with the surrounding plasma membrane. Higher packing of total lipids is observed in caveolae compared with the surrounding plasma membrane.
  • 23
    • 12344260000 scopus 로고    scopus 로고
    • Polarized sorting in epithelial cells: Raft clustering and the biogenesis of the apical membrane
    • Schuck, S. & Simons, K. Polarized sorting in epithelial cells: raft clustering and the biogenesis of the apical membrane. J. Cell Sci. 117, 5955-5964 (2004).
    • (2004) J. Cell Sci , vol.117 , pp. 5955-5964
    • Schuck, S.1    Simons, K.2
  • 24
    • 1842482773 scopus 로고    scopus 로고
    • Simons, K. & Vaz, W.L. Model systems, lipid rafts, and cell membranes. Annu. Rev. Biophys. Biomol. Struct. 33, 269-295 (2004). An extensive review of the data supporting lipid-based microdomain formation in model systems and in cell membranes.
    • Simons, K. & Vaz, W.L. Model systems, lipid rafts, and cell membranes. Annu. Rev. Biophys. Biomol. Struct. 33, 269-295 (2004). An extensive review of the data supporting lipid-based microdomain formation in model systems and in cell membranes.
  • 25
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: Contentious only from simplistic standpoints
    • Hancock, J.F. Lipid rafts: contentious only from simplistic standpoints. Nature Rev. Mol. Cell Biol. 7, 456-462 (2006).
    • (2006) Nature Rev. Mol. Cell Biol , vol.7 , pp. 456-462
    • Hancock, J.F.1
  • 26
    • 0032498628 scopus 로고    scopus 로고
    • Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells
    • Lipardi, C. et al. Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells. J. Cell Biol. 140, 617-626 (1998).
    • (1998) J. Cell Biol , vol.140 , pp. 617-626
    • Lipardi, C.1
  • 27
    • 33645216741 scopus 로고    scopus 로고
    • Parton, R.G., Hanzal-Bayer, M. & Hancock, J.F. Biogenesis of caveolae: a structural model for caveolin-induced domain formation. J. Cell Sci. 119, 787-796 (2006). Summary of current data on caveola biogenesis and a proposed model for the formation of caveolae through caveolin-lipid interactions.
    • Parton, R.G., Hanzal-Bayer, M. & Hancock, J.F. Biogenesis of caveolae: a structural model for caveolin-induced domain formation. J. Cell Sci. 119, 787-796 (2006). Summary of current data on caveola biogenesis and a proposed model for the formation of caveolae through caveolin-lipid interactions.
  • 28
    • 0028998554 scopus 로고
    • VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro
    • Monier, S. et al. VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro. Mol. Biol. Cell 6, 911-927 (1995).
    • (1995) Mol. Biol. Cell , vol.6 , pp. 911-927
    • Monier, S.1
  • 29
    • 0030591426 scopus 로고    scopus 로고
    • Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol
    • Monier, S., Dietzen, D.J., Hastings, W.R., Lublin, D.M. & Kurzchalia, T.V. Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol. FEBS Lett. 388, 143-149 (1996).
    • (1996) FEBS Lett , vol.388 , pp. 143-149
    • Monier, S.1    Dietzen, D.J.2    Hastings, W.R.3    Lublin, D.M.4    Kurzchalia, T.V.5
  • 30
    • 16344368798 scopus 로고    scopus 로고
    • Cholesterol and fatty acids regulate dynamic caveolin trafficking through the Golgi complex and between the cell surface and lipid bodies
    • Pol, A. et al. Cholesterol and fatty acids regulate dynamic caveolin trafficking through the Golgi complex and between the cell surface and lipid bodies. Mol. Biol. Cell 16, 2091-2105 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2091-2105
    • Pol, A.1
  • 31
    • 33745635738 scopus 로고    scopus 로고
    • Distinct mechanisms of clathrin-independent cndocytosis have unique sphingolipid requirements
    • Cheng, Z.J. et al. Distinct mechanisms of clathrin-independent cndocytosis have unique sphingolipid requirements. Mol. Biol. Cell 17, 3197-3210 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3197-3210
    • Cheng, Z.J.1
  • 32
    • 24144431634 scopus 로고    scopus 로고
    • Tagawa, A. et al. Assembly and trafficking of caveolar domains in the cell: caveolae as stable, cargo-triggered, vesicular transporters. J. Cell Biol. 170, 769-779 (2005). Real-time microscopy and cell-fusion experiments show that caveolae are remarkably stable with evidence for formation of 'caveolae' in the Golgi complex that then fuse directly with the plasma membrane.
    • Tagawa, A. et al. Assembly and trafficking of caveolar domains in the cell: caveolae as stable, cargo-triggered, vesicular transporters. J. Cell Biol. 170, 769-779 (2005). Real-time microscopy and cell-fusion experiments show that caveolae are remarkably stable with evidence for formation of 'caveolae' in the Golgi complex that then fuse directly with the plasma membrane.
  • 33
    • 0027294580 scopus 로고
    • Domain-induced budding of fluid membranes
    • Lipowsky, R. Domain-induced budding of fluid membranes. Biophys. J. 64, 1133-1138 (1993).
    • (1993) Biophys. J , vol.64 , pp. 1133-1138
    • Lipowsky, R.1
  • 34
    • 33749078313 scopus 로고    scopus 로고
    • A new paradigm for membrane-organizing and -shaping scaffolds
    • Bauer, M. & Pelkmans, L. A new paradigm for membrane-organizing and -shaping scaffolds. FEBS Lett. 580, 5559-5564 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 5559-5564
    • Bauer, M.1    Pelkmans, L.2
  • 35
    • 33645713636 scopus 로고    scopus 로고
    • Choudhury, A., Marks, D.L., Proctor, K.M., Gould, G.W. & Pagano, R.E. Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface. Nature Cell Biol. 8, 317-328 (2006). Identifies syntaxin-6 as a regulator of CAV1, GPI-anchored proteins, and GM1 transport from Golgi to the plasma membrane and provides insights into the coupling of exocytosis and endocytosis of lipid-raft components.
    • Choudhury, A., Marks, D.L., Proctor, K.M., Gould, G.W. & Pagano, R.E. Regulation of caveolar endocytosis by syntaxin 6-dependent delivery of membrane components to the cell surface. Nature Cell Biol. 8, 317-328 (2006). Identifies syntaxin-6 as a regulator of CAV1, GPI-anchored proteins, and GM1 transport from Golgi to the plasma membrane and provides insights into the coupling of exocytosis and endocytosis of lipid-raft components.
  • 36
    • 27644505702 scopus 로고    scopus 로고
    • Caveolin-1 is not essential for biosynthetic apical membrane transport
    • Manninen, A. et al. Caveolin-1 is not essential for biosynthetic apical membrane transport. Mol. Cell. Biol. 25, 10087-10096 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 10087-10096
    • Manninen, A.1
  • 37
    • 29644441031 scopus 로고    scopus 로고
    • Aberrant dysferlin trafficking in cells lacking caveolin or expressing dystrophy mutants of caveolin-3
    • Hernandez-Deviez, D.J. et al. Aberrant dysferlin trafficking in cells lacking caveolin or expressing dystrophy mutants of caveolin-3. Hum. Mol. Genet. 15, 129-142 (2006).
    • (2006) Hum. Mol. Genet , vol.15 , pp. 129-142
    • Hernandez-Deviez, D.J.1
  • 38
    • 0037592388 scopus 로고    scopus 로고
    • Caveolin interacts with the angiotensin II type 1 receptor during exocytic transport but not at the plasma membrane
    • Wyse, B.D. et al. Caveolin interacts with the angiotensin II type 1 receptor during exocytic transport but not at the plasma membrane. J. Biol. Chem. 278, 23738-23746 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 23738-23746
    • Wyse, B.D.1
  • 39
    • 0037663884 scopus 로고    scopus 로고
    • Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue
    • Cohen, A.W. et al. Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue. Am. J. Physiol. Cell Physiol. 285, C222-C235 (2003).
    • (2003) Am. J. Physiol. Cell Physiol , vol.285
    • Cohen, A.W.1
  • 41
    • 13944263659 scopus 로고    scopus 로고
    • TRPC1 forms the stretch-activated cation channel in vertebrate cells
    • Maroto, R. et al. TRPC1 forms the stretch-activated cation channel in vertebrate cells. Nature Cell Biol. 7, 179-185 (2005).
    • (2005) Nature Cell Biol , vol.7 , pp. 179-185
    • Maroto, R.1
  • 42
    • 0032559560 scopus 로고    scopus 로고
    • Caveolin-1 and -2 in the exocytic pathway of MDCK cells
    • Scheiffele, P. et al. Caveolin-1 and -2 in the exocytic pathway of MDCK cells. J. Cell Biol. 140, 795-806 (1998).
    • (1998) J. Cell Biol , vol.140 , pp. 795-806
    • Scheiffele, P.1
  • 43
    • 0034695916 scopus 로고    scopus 로고
    • Induction of caveolae in the apical plasma membrane of Madin-Darby canine kidney cells
    • Verkade, P., Harder, T., Lafont, F. & Simons, K. Induction of caveolae in the apical plasma membrane of Madin-Darby canine kidney cells. J. Cell Biol. 148, 727-739 (2000).
    • (2000) J. Cell Biol , vol.148 , pp. 727-739
    • Verkade, P.1    Harder, T.2    Lafont, F.3    Simons, K.4
  • 44
    • 4544375506 scopus 로고    scopus 로고
    • Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic
    • Pelkmans, L., Burli, T., Zerial, M. & Helenius, A. Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic. Cell 118, 767-780 (2004).
    • (2004) Cell , vol.118 , pp. 767-780
    • Pelkmans, L.1    Burli, T.2    Zerial, M.3    Helenius, A.4
  • 45
    • 0036151510 scopus 로고    scopus 로고
    • Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking
    • Thomsen, P., Roepstorff, K., Stahlhut, M. & van Deurs, B. Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking. Mol. Biol. Cell 13, 238-250 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 238-250
    • Thomsen, P.1    Roepstorff, K.2    Stahlhut, M.3    van Deurs, B.4
  • 46
    • 13444310587 scopus 로고    scopus 로고
    • Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles
    • Kirkham, M. et al. Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles. J. Cell Biol. 168, 465-476 (2005).
    • (2005) J. Cell Biol , vol.168 , pp. 465-476
    • Kirkham, M.1
  • 47
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans, L., Puntener, D. & Helenius, A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296, 535-539 (2002).
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 48
    • 3042850162 scopus 로고    scopus 로고
    • Selective stimulation of caveolar endocytosis by glycosphingolipids and cholesterol
    • Sharma, D.K. et al. Selective stimulation of caveolar endocytosis by glycosphingolipids and cholesterol. Mol. Biol. Cell 15, 3114-3122 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3114-3122
    • Sharma, D.K.1
  • 49
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh, P., McIntosh, D.P. & Schnitzer, J.E. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol. 141, 101-114 (1998).
    • (1998) J. Cell Biol , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 51
    • 16244399830 scopus 로고    scopus 로고
    • Caveolin-1 interacts directly with dynamin-2
    • Yao, Q. et al. Caveolin-1 interacts directly with dynamin-2. J. Mol. Biol. 348, 491-501 (2005).
    • (2005) J. Mol. Biol , vol.348 , pp. 491-501
    • Yao, Q.1
  • 52
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin- and caveolin-1-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae
    • Damm, E.M. et al. Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae. J. Cell Biol. 168, 477-488 (2005).
    • (2005) J. Cell Biol , vol.168 , pp. 477-488
    • Damm, E.M.1
  • 53
    • 24944523300 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: New insights into caveolae and non-caveolar lipid raft carriers
    • Kirkham, M. & Parton, R.G. Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers. Biochim. Biophys. Acta 1745, 273-286 (2005).
    • (2005) Biochim. Biophys. Acta , vol.1745 , pp. 273-286
    • Kirkham, M.1    Parton, R.G.2
  • 54
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • Nabi, I.R. & Le, P.U. Caveolae/raft-dependent endocytosis. J. Cell Biol. 161, 673-677 (2003).
    • (2003) J. Cell Biol , vol.161 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 55
    • 21844440569 scopus 로고    scopus 로고
    • Pelkmans, L. et al. Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature 436, 78-86 (2005). A high-throughput screen of kinases involved in endocytosis provides fascinating insights into the complex interplay between endocytosis and other cellular processes, such as cell adhesion and cell division.
    • Pelkmans, L. et al. Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature 436, 78-86 (2005). A high-throughput screen of kinases involved in endocytosis provides fascinating insights into the complex interplay between endocytosis and other cellular processes, such as cell adhesion and cell division.
  • 56
    • 24944555198 scopus 로고    scopus 로고
    • Sharma, D.K. et al. The glycosphingolipid, lactosylceramide, regulates β1-integrin clustering and endocytosis. Cancer Res. 65, 8233-8241 (2005). Evidence for glycosphingolipid-stimulated β1-integrin internalization through a caveolae-mediated pathway.
    • Sharma, D.K. et al. The glycosphingolipid, lactosylceramide, regulates β1-integrin clustering and endocytosis. Cancer Res. 65, 8233-8241 (2005). Evidence for glycosphingolipid-stimulated β1-integrin internalization through a caveolae-mediated pathway.
  • 57
    • 12844269776 scopus 로고    scopus 로고
    • Fibronectin matrix turnover occurs through a caveolin-1-dependent process
    • Sottile, J. & Chandler, J. Fibronectin matrix turnover occurs through a caveolin-1-dependent process. Mol. Biol. Cell 16, 757-768 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 757-768
    • Sottile, J.1    Chandler, J.2
  • 58
    • 26944437142 scopus 로고    scopus 로고
    • del Pozo, M.A. et al. Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization. Nature Cell Biol. 7, 901-908 (2005). Demonstrates striking internalization of lipid-raft components upon cell detachment from the substratum through a phospho-CAV1-dependent pathway.
    • del Pozo, M.A. et al. Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization. Nature Cell Biol. 7, 901-908 (2005). Demonstrates striking internalization of lipid-raft components upon cell detachment from the substratum through a phospho-CAV1-dependent pathway.
  • 59
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton, R.G. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 42, 155-166 (1994).
    • (1994) J. Histochem. Cytochem , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 60
    • 0037446837 scopus 로고    scopus 로고
    • GM1-containing lipid rafts are depleted within clathrin-coated pits
    • Nichols, B.J. GM1-containing lipid rafts are depleted within clathrin-coated pits. Curr. Biol. 13, 686-690 (2003).
    • (2003) Curr. Biol , vol.13 , pp. 686-690
    • Nichols, B.J.1
  • 61
    • 0036307071 scopus 로고    scopus 로고
    • Modulation of Brucella-induced macropinocytosis by lipid rafts mediates intracellular replication
    • Watarai, M., Makino, S., Fujii, Y., Okamoto, K. & Shirahata, T. Modulation of Brucella-induced macropinocytosis by lipid rafts mediates intracellular replication. Cell Microbiol. 4, 341-355 (2002).
    • (2002) Cell Microbiol , vol.4 , pp. 341-355
    • Watarai, M.1    Makino, S.2    Fujii, Y.3    Okamoto, K.4    Shirahata, T.5
  • 62
    • 0034605039 scopus 로고    scopus 로고
    • Endothelial cell-surface gp60 activates vesicle formation and trafficking via G(i)-coupled Src kinase signaling pathway
    • Minshall, R.D. et al. Endothelial cell-surface gp60 activates vesicle formation and trafficking via G(i)-coupled Src kinase signaling pathway. J. Cell Biol. 150, 1057-1070 (2000).
    • (2000) J. Cell Biol , vol.150 , pp. 1057-1070
    • Minshall, R.D.1
  • 63
    • 0035965995 scopus 로고    scopus 로고
    • Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo
    • Schubert, W. et al. Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo. J. Biol. Chem. 276, 48619-48622 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 48619-48622
    • Schubert, W.1
  • 64
    • 33644839698 scopus 로고    scopus 로고
    • Miyawaki-Shimizu, K. et al. siRNA-induced caveolin-1 knockdown in mice increases lung vascular permeability via the junctional pathway. Am. J. Physiol. Lung Cell. Mol. Physiol. 290, L405-L413 (2006). siRNA-mediated downregulation of CAV1 in vivo causes a loss of endothelial caveolae and an increase in vascular hyperpermeability to albumin. Ultrastructural studies showed dilation of interendothelial junctions.
    • Miyawaki-Shimizu, K. et al. siRNA-induced caveolin-1 knockdown in mice increases lung vascular permeability via the junctional pathway. Am. J. Physiol. Lung Cell. Mol. Physiol. 290, L405-L413 (2006). siRNA-mediated downregulation of CAV1 in vivo causes a loss of endothelial caveolae and an increase in vascular hyperpermeability to albumin. Ultrastructural studies showed dilation of interendothelial junctions.
  • 65
    • 33748426207 scopus 로고    scopus 로고
    • Rosengren, B.I. et al. Transvascular protein transport in mice lacking endothelial caveolae. Am. J. Physiol. Heart Circ. Physiol. 291, H1371-H1377 (2006). Evidence for a passive porous pathway for transport of albumin across the endothelium in vivo in both Cav1-knockout and wild-type mice, arguing against caveolae as a quantitatively important transport route.
    • Rosengren, B.I. et al. Transvascular protein transport in mice lacking endothelial caveolae. Am. J. Physiol. Heart Circ. Physiol. 291, H1371-H1377 (2006). Evidence for a passive porous pathway for transport of albumin across the endothelium in vivo in both Cav1-knockout and wild-type mice, arguing against caveolae as a quantitatively important transport route.
  • 66
    • 0037131313 scopus 로고    scopus 로고
    • Microvascular hyperpermeability in caveolin-1 (-/-) knock-out mice. Treatment with a specific nitric-oxide synthase inhibitor, L-NAME, restores normal microvascular permeability in Cav-1 null mice
    • Schubert, W. et al. Microvascular hyperpermeability in caveolin-1 (-/-) knock-out mice. Treatment with a specific nitric-oxide synthase inhibitor, L-NAME, restores normal microvascular permeability in Cav-1 null mice. J. Biol. Chem. 277, 40091-40098 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 40091-40098
    • Schubert, W.1
  • 67
    • 14544306526 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis of ubiquitinated cargos
    • Sigismund, S. et al. Clathrin-independent endocytosis of ubiquitinated cargos. Proc. Natl Acad. Sci. USA 102, 2760-2765 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 2760-2765
    • Sigismund, S.1
  • 68
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-β receptor signalling and turnover
    • Di Guglielmo, G.M., Le Roy, C., Goodfellow, A.F. & Wrana, J.L. Distinct endocytic pathways regulate TGF-β receptor signalling and turnover. Nature Cell Biol. 5, 410-421 (2003).
    • (2003) Nature Cell Biol , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4
  • 69
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson, H.A., Chen, Y. & Norkin, L.C. Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol. Biol. Cell 7, 1825-1834 (1996).
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 70
    • 0030745673 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules mediate association of SV40 with caveolae
    • Stang, E., Kartenbeck, J. & Parton, R.G. Major histocompatibility complex class I molecules mediate association of SV40 with caveolae. Mol. Biol. Cell 8, 47-57 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 47-57
    • Stang, E.1    Kartenbeck, J.2    Parton, R.G.3
  • 71
    • 0345829922 scopus 로고    scopus 로고
    • Escherichia coli K1 internalization via caveolae requires caveolin-1 and protein kinase Cα interaction in human brain microvascular endothelial cells
    • Sukumaran, S.K., Quon, M.J. & Prasadarao, N.V. Escherichia coli K1 internalization via caveolae requires caveolin-1 and protein kinase Cα interaction in human brain microvascular endothelial cells. J. Biol. Chem. 277, 50716-50724 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 50716-50724
    • Sukumaran, S.K.1    Quon, M.J.2    Prasadarao, N.V.3
  • 72
    • 14244264008 scopus 로고    scopus 로고
    • Pseudomonas invasion of type I pneumocytes is dependent on the expression and phosphorylation of caveolin-2
    • Zaas, D.W., Duncan, M.J., Li, G., Wright, J.R. & Abraham, S.N. Pseudomonas invasion of type I pneumocytes is dependent on the expression and phosphorylation of caveolin-2. J. Biol. Chem. 280, 4864-4872 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 4864-4872
    • Zaas, D.W.1    Duncan, M.J.2    Li, G.3    Wright, J.R.4    Abraham, S.N.5
  • 73
    • 25444514225 scopus 로고    scopus 로고
    • Requirement for intercellular adhesion molecule 1 and caveolae in invasion of human oral epithelial cells by Porphyromonas gingivalis
    • Tamai, R., Asai, Y. & Ogawa, T. Requirement for intercellular adhesion molecule 1 and caveolae in invasion of human oral epithelial cells by Porphyromonas gingivalis. Infect. Immun. 73, 6290-6298 (2005).
    • (2005) Infect. Immun , vol.73 , pp. 6290-6298
    • Tamai, R.1    Asai, Y.2    Ogawa, T.3
  • 74
    • 0042978789 scopus 로고    scopus 로고
    • Host cell caveolae act as an entry-port for group A streptococci
    • Rohde, M., Muller, E., Chhatwal, G.S. & Talay, S.R. Host cell caveolae act as an entry-port for group A streptococci. Cell. Microbiol. 5, 323-342 (2003).
    • (2003) Cell. Microbiol , vol.5 , pp. 323-342
    • Rohde, M.1    Muller, E.2    Chhatwal, G.S.3    Talay, S.R.4
  • 75
    • 33645162400 scopus 로고    scopus 로고
    • Lymphocyte transcellular migration occurs through recruitment of endothelial ICAM-1 to caveola- and F-actin-rich domains
    • Millan, J. et al. Lymphocyte transcellular migration occurs through recruitment of endothelial ICAM-1 to caveola- and F-actin-rich domains. Nature Cell Biol. 8, 113-123 (2006).
    • (2006) Nature Cell Biol , vol.8 , pp. 113-123
    • Millan, J.1
  • 76
    • 0038067968 scopus 로고    scopus 로고
    • A novel endocytic pathway induced by clustering endothelial ICAM-1 or PECAM-1
    • Muro, S. et al. A novel endocytic pathway induced by clustering endothelial ICAM-1 or PECAM-1. J. Cell Sci. 116, 1599-1609 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 1599-1609
    • Muro, S.1
  • 77
    • 27744450311 scopus 로고    scopus 로고
    • Impaired phagocytosis in caveolin-1 deficient macrophages
    • Li, J. et al. Impaired phagocytosis in caveolin-1 deficient macrophages. Cell Cycle 4, 1599-1607 (2005).
    • (2005) Cell Cycle , vol.4 , pp. 1599-1607
    • Li, J.1
  • 78
    • 13544252448 scopus 로고    scopus 로고
    • Beardsley, A. et al. Loss of caveolin-1 polarity impedes endothelial cell polarization and directional movement. J. Biol. Chem. 280, 3541-3547 (2005). Provides evidence for a functional role for CAV1 in endothelial-cell motility. In actively migrating cells, caveolae are localized at the rear of the cell and excluded from the leading edge.
    • Beardsley, A. et al. Loss of caveolin-1 polarity impedes endothelial cell polarization and directional movement. J. Biol. Chem. 280, 3541-3547 (2005). Provides evidence for a functional role for CAV1 in endothelial-cell motility. In actively migrating cells, caveolae are localized at the rear of the cell and excluded from the leading edge.
  • 79
    • 0037705362 scopus 로고    scopus 로고
    • Immunopurification and characterization of rat adipocyte caveolae suggest their dissociation from insulin signaling
    • Souto, R.P. et al. Immunopurification and characterization of rat adipocyte caveolae suggest their dissociation from insulin signaling. J. Biol. Chem. 278, 18321-18329 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 18321-18329
    • Souto, R.P.1
  • 80
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, Gα subunits, and H-Ras share a common membrane-anchored scaffolding protein, caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • Li, S., Couet, J. & Lisanti, M.P. Src tyrosine kinases, Gα 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. 271, 29182-29190 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 81
    • 0033529643 scopus 로고    scopus 로고
    • A role for the caveolin scaffolding domain in mediating the membrane attachment of caveolin-1. The caveolin scaffolding domain is both necessary and sufficient for membrane binding in vitro
    • Schlegel, A., Schwab, R.B., Scherer, P.E. & Lisanti, M.P. A role for the caveolin scaffolding domain in mediating the membrane attachment of caveolin-1. The caveolin scaffolding domain is both necessary and sufficient for membrane binding in vitro. J. Biol. Chem. 274, 22660-22667 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 22660-22667
    • Schlegel, A.1    Schwab, R.B.2    Scherer, P.E.3    Lisanti, M.P.4
  • 82
    • 9644281567 scopus 로고    scopus 로고
    • Caveolin scaffolding region and cholesterol-rich domains in membranes
    • Epand, R.M., Sayer, B.G. & Epand, R.F. Caveolin scaffolding region and cholesterol-rich domains in membranes. J. Mol. Biol. 345, 339-350 (2005).
    • (2005) J. Mol. Biol , vol.345 , pp. 339-350
    • Epand, R.M.1    Sayer, B.G.2    Epand, R.F.3
  • 83
    • 0034702838 scopus 로고    scopus 로고
    • Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS
    • Arbuzova, A. et al. Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS. Biochemistry 39, 10330-10339 (2000).
    • (2000) Biochemistry , vol.39 , pp. 10330-10339
    • Arbuzova, A.1
  • 84
    • 4644261120 scopus 로고    scopus 로고
    • Small interfering RNA-mediated downregulation of caveolin-1 differentially modulates signaling pathways in endothelial cells
    • Gonzalez, E., Nagiel, A., Lin, A.J., Golan, D.E. & Michel, T. Small interfering RNA-mediated downregulation of caveolin-1 differentially modulates signaling pathways in endothelial cells. J. Biol. Chem. 279, 40659-40669 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 40659-40669
    • Gonzalez, E.1    Nagiel, A.2    Lin, A.J.3    Golan, D.E.4    Michel, T.5
  • 85
    • 14144250454 scopus 로고    scopus 로고
    • Dissecting the molecular control of endothelial NO synthase by caveolin-1 using cell-permeable peptides
    • Bernatchez, P.N. et al. Dissecting the molecular control of endothelial NO synthase by caveolin-1 using cell-permeable peptides. Proc. Natl Acad. Sci. USA 102, 761-766 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 761-766
    • Bernatchez, P.N.1
  • 86
    • 0032483575 scopus 로고    scopus 로고
    • A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth
    • Wary, K.K., Mariotti, A., Zurzolo, C. & Giancotti, F.G. A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth. Cell 94, 625-634 (1998).
    • (1998) Cell , vol.94 , pp. 625-634
    • Wary, K.K.1    Mariotti, A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 87
    • 19944428563 scopus 로고    scopus 로고
    • Bauer, P.M. et al. Endothelial-specific expression of caveolin-1 impairs microvascular permeability and angiogenesis. Proc. Natl Acad. Sci. USA 102, 204-209 (2005). Transgenic overexpression of CAV1 impairs eNOS activation and decreases VEGF-stimulated vascular permeability. CAV1 overexpression reduced VEGF-mediated angiogenesis after experimentally induced tissue ischaemia.
    • Bauer, P.M. et al. Endothelial-specific expression of caveolin-1 impairs microvascular permeability and angiogenesis. Proc. Natl Acad. Sci. USA 102, 204-209 (2005). Transgenic overexpression of CAV1 impairs eNOS activation and decreases VEGF-stimulated vascular permeability. CAV1 overexpression reduced VEGF-mediated angiogenesis after experimentally induced tissue ischaemia.
  • 88
    • 0034529950 scopus 로고    scopus 로고
    • In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
    • Bucci, M. et al. In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation. Nature Med. 6, 1362-1367 (2000).
    • (2000) Nature Med , vol.6 , pp. 1362-1367
    • Bucci, M.1
  • 89
    • 0039397709 scopus 로고    scopus 로고
    • Dissecting the interaction between nitric oxide synthase (NOS) and caveolin. Functional significance of the NOS caveolin binding domain in vivo
    • Garcia-Cardena, G. 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. 272, 25437-25440 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 25437-25440
    • Garcia-Cardena, G.1
  • 90
    • 33744958085 scopus 로고    scopus 로고
    • Key role of Src kinase in S100B-induced activation of the receptor for advanced glycation end products in vascular smooth muscle cells
    • Reddy, M.A. et al. Key role of Src kinase in S100B-induced activation of the receptor for advanced glycation end products in vascular smooth muscle cells. J. Biol. Chem. 281, 13685-13693 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 13685-13693
    • Reddy, M.A.1
  • 91
    • 33745209452 scopus 로고    scopus 로고
    • Focal adhesions in (myo)fibroblasts scaffold adenylyl cyclase with phosphorylated caveolin
    • Swaney, J.S. et al. Focal adhesions in (myo)fibroblasts scaffold adenylyl cyclase with phosphorylated caveolin. J. Biol. Chem. 281, 17173-17179 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 17173-17179
    • Swaney, J.S.1
  • 93
    • 15744367070 scopus 로고    scopus 로고
    • + channels in vascular endothelial cells
    • + channels in vascular endothelial cells. J. Biol. Chem. 280, 11656-11664 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 11656-11664
    • Wang, X.L.1
  • 95
    • 33646168160 scopus 로고    scopus 로고
    • Lipid droplets: A unified view of a dynamic organelle
    • Martin, S. & Parton, R.G. Lipid droplets: a unified view of a dynamic organelle. Nature Rev. Mol. Cell Biol. 7, 373-378 (2006).
    • (2006) Nature Rev. Mol. Cell Biol , vol.7 , pp. 373-378
    • Martin, S.1    Parton, R.G.2
  • 96
    • 0034903123 scopus 로고    scopus 로고
    • The biogenesis and functions of lipid bodies in animals, plants and microorganisms
    • Murphy, D.J. The biogenesis and functions of lipid bodies in animals, plants and microorganisms. Prog. Lipid Res. 40, 325-438 (2001).
    • (2001) Prog. Lipid Res , vol.40 , pp. 325-438
    • Murphy, D.J.1
  • 97
    • 15944365201 scopus 로고    scopus 로고
    • Caveolin, cholesterol, and lipid bodies
    • Martin, S. & Parton, R.G. Caveolin, cholesterol, and lipid bodies. Semin. Cell Dev. Biol. 16, 163-174 (2005).
    • (2005) Semin. Cell Dev. Biol , vol.16 , pp. 163-174
    • Martin, S.1    Parton, R.G.2
  • 98
    • 8744267532 scopus 로고    scopus 로고
    • Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes
    • Brasaemle, D.L., Dolios, G., Shapiro, L. & Wang, R. Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes. J. Biol. Chem. 279, 46835-46842 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 46835-46842
    • Brasaemle, D.L.1    Dolios, G.2    Shapiro, L.3    Wang, R.4
  • 99
    • 0346099345 scopus 로고    scopus 로고
    • Dynamic and regulated association of caveolin with lipid bodies: Modulation of lipid body motility and function by a dominant negative mutant
    • Pol, A. et al. Dynamic and regulated association of caveolin with lipid bodies: modulation of lipid body motility and function by a dominant negative mutant. Mol. Biol. Cell 15, 99-110 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 99-110
    • Pol, A.1
  • 100
    • 33644675358 scopus 로고    scopus 로고
    • Role of caveolin-1 and cholesterol in transmembrane fatty acid movement
    • Meshulam, T., Simard, J.R., Wharton, J., Hamilton, J.A. & Pilch, P.F. Role of caveolin-1 and cholesterol in transmembrane fatty acid movement. Biochemistry 45, 2882-2893 (2006).
    • (2006) Biochemistry , vol.45 , pp. 2882-2893
    • Meshulam, T.1    Simard, J.R.2    Wharton, J.3    Hamilton, J.A.4    Pilch, P.F.5
  • 101
    • 1842689994 scopus 로고    scopus 로고
    • Expression of caveolin-1 enhances cholesterol efflux in hepatic cells
    • Fu, Y. et al. Expression of caveolin-1 enhances cholesterol efflux in hepatic cells. J. Biol. Chem. 279, 14140-14146 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 14140-14146
    • Fu, Y.1
  • 102
    • 0035963902 scopus 로고    scopus 로고
    • Caveolae and intracellular trafficking of cholesterol
    • Fielding, C.J. & Fielding, P.E. Caveolae and intracellular trafficking of cholesterol. Adv. Drug Deliv. Rev. 49, 251-264 (2001).
    • (2001) Adv. Drug Deliv. Rev , vol.49 , pp. 251-264
    • Fielding, C.J.1    Fielding, P.E.2
  • 103
    • 33746855808 scopus 로고    scopus 로고
    • Caveolin-1 and the regulation of cellular cholesterol homeostasis
    • Frank, P.G. et al. Caveolin-1 and the regulation of cellular cholesterol homeostasis. Am. J. Physiol. Heart Circ. Physiol. 291, H677-H686 (2006).
    • (2006) Am. J. Physiol. Heart Circ. Physiol , vol.291
    • Frank, P.G.1
  • 104
    • 0035809933 scopus 로고    scopus 로고
    • A caveolin dominant negative mutant associates with lipid bodies and induces intracellular cholesterol imbalance
    • Pol, A. et al. A caveolin dominant negative mutant associates with lipid bodies and induces intracellular cholesterol imbalance. J. Cell Biol. 152, 1057-1070 (2001).
    • (2001) J. Cell Biol , vol.152 , pp. 1057-1070
    • Pol, A.1
  • 105
    • 33748773325 scopus 로고    scopus 로고
    • Caveolin-1 is essential for liver regeneration
    • Fernandez, M.A. et al. Caveolin-1 is essential for liver regeneration. Science 313, 1628-1632 (2006).
    • (2006) Science , vol.313 , pp. 1628-1632
    • Fernandez, M.A.1
  • 106
    • 0037040994 scopus 로고    scopus 로고
    • Caveolin-1-deficient mice are lean, resistant to diet-induced obesity, and show hypertriglyceridemia with adipocyte abnormalities
    • Razani, B. et al. Caveolin-1-deficient mice are lean, resistant to diet-induced obesity, and show hypertriglyceridemia with adipocyte abnormalities. J. Biol. Chem. 277, 8635-8647 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 8635-8647
    • Razani, B.1
  • 107
    • 33745844829 scopus 로고    scopus 로고
    • Cholesterol-induced caveolin targeting to lipid droplets in adipocytes: A role for caveolar endocytosis
    • Le Lay, S. et al. Cholesterol-induced caveolin targeting to lipid droplets in adipocytes: a role for caveolar endocytosis. Traffic 7, 549-561 (2006).
    • (2006) Traffic , vol.7 , pp. 549-561
    • Le Lay, S.1
  • 108
    • 0029156582 scopus 로고
    • From entangled membranes to eclectic morphologies: Cubic membranes as subcellular space organizers
    • Landh, T. From entangled membranes to eclectic morphologies: cubic membranes as subcellular space organizers. FEBS Lett. 369, 13-17 (1995).
    • (1995) FEBS Lett , vol.369 , pp. 13-17
    • Landh, T.1
  • 109
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel, V. & Sheetz, M. Local force and geometry sensing regulate cell functions. Nature Rev. Mol. Cell Biol. 7, 265-275 (2006).
    • (2006) Nature Rev. Mol. Cell Biol , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 110
    • 0141676760 scopus 로고    scopus 로고
    • Rizzo, V., Morton, C., DePaola, N., Schnitzer, J.E. & Davies, P.F. Recruitment of endothelial caveolae into mechanotransduction pathways by flow conditioning in vitro. Am. J. Physiol. Heart Circ. Physiol. 285, H1720-H1729 (2003). In cultured endothelial cells, chronic exposure to shear stress causes increased surface localization of CAV1 and caveolae; this effect is linked to increased mechanosensitivity and activation of specific signalling pathways.
    • Rizzo, V., Morton, C., DePaola, N., Schnitzer, J.E. & Davies, P.F. Recruitment of endothelial caveolae into mechanotransduction pathways by flow conditioning in vitro. Am. J. Physiol. Heart Circ. Physiol. 285, H1720-H1729 (2003). In cultured endothelial cells, chronic exposure to shear stress causes increased surface localization of CAV1 and caveolae; this effect is linked to increased mechanosensitivity and activation of specific signalling pathways.
  • 111
    • 0041357203 scopus 로고    scopus 로고
    • Chronic shear induces caveolae formation and alters ERK and Akt responses in endothelial cells
    • Boyd, N.L. et al. Chronic shear induces caveolae formation and alters ERK and Akt responses in endothelial cells. Am. J. Physiol. Heart Circ. Physiol. 285, H1113-H1122 (2003).
    • (2003) Am. J. Physiol. Heart Circ. Physiol , vol.285
    • Boyd, N.L.1
  • 112
    • 12344250442 scopus 로고    scopus 로고
    • Radel, C. & Rizzo, V. Integrin mechanotransduction stimulates caveolin-1 phosphorylation and recruitment of Csk to mediate actin reorganization. Am. J. Physiol. Heart Circ. Physiol. 288, H936-H945 (2005). Cultured bovine aortic endothelial cells subjected to shear stress show rapid Tyr14 phosphorylation of CAV1, which is dependent on β1-integrin activation, supporting a role for caveolae in mechanosensing.
    • Radel, C. & Rizzo, V. Integrin mechanotransduction stimulates caveolin-1 phosphorylation and recruitment of Csk to mediate actin reorganization. Am. J. Physiol. Heart Circ. Physiol. 288, H936-H945 (2005). Cultured bovine aortic endothelial cells subjected to shear stress show rapid Tyr14 phosphorylation of CAV1, which is dependent on β1-integrin activation, supporting a role for caveolae in mechanosensing.
  • 113
    • 33646422239 scopus 로고    scopus 로고
    • Yu, J. et al. Direct evidence for the role of caveolin-1 and caveolae in mechanotransduction and remodeling of blood vessels. J. Clin. Invest. 116, 1284-1291 (2006). Endothelial expression of CAV1 in Cav1-null mice shows that CAV1 is required for eNOS activation in response to endothelial flow; these data provide further support for a mechanosensing role of caveolae.
    • Yu, J. et al. Direct evidence for the role of caveolin-1 and caveolae in mechanotransduction and remodeling of blood vessels. J. Clin. Invest. 116, 1284-1291 (2006). Endothelial expression of CAV1 in Cav1-null mice shows that CAV1 is required for eNOS activation in response to endothelial flow; these data provide further support for a mechanosensing role of caveolae.
  • 114
    • 0032520153 scopus 로고    scopus 로고
    • Direct evidence for the importance of endothelium-derived nitric oxide in vascular remodeling
    • Rudic, R.D. et al. Direct evidence for the importance of endothelium-derived nitric oxide in vascular remodeling. J. Clin. Invest. 101, 731-736 (1998).
    • (1998) J. Clin. Invest , vol.101 , pp. 731-736
    • Rudic, R.D.1
  • 115
    • 16444371939 scopus 로고    scopus 로고
    • Sedding, D.G. et al. Caveolin-1 facilitates mechanosensitive protein kinase B (Akt) signaling in vitro and in vivo. Circ. Res. 96, 635-642 (2005). Smooth-muscle cells subjected to cyclic stretch show rapid redistribution of CAV1 to focal contacts. CAV1 is required for stretch-triggered cell-cycle progression.
    • Sedding, D.G. et al. Caveolin-1 facilitates mechanosensitive protein kinase B (Akt) signaling in vitro and in vivo. Circ. Res. 96, 635-642 (2005). Smooth-muscle cells subjected to cyclic stretch show rapid redistribution of CAV1 to focal contacts. CAV1 is required for stretch-triggered cell-cycle progression.
  • 117
    • 4143125479 scopus 로고    scopus 로고
    • Neutral sphingomyelinase inhibitor scyphostatin prevents and ceramide mimics mechanotransduction in vascular endothelium
    • Czarny, M. & Schnitzer, J.E. Neutral sphingomyelinase inhibitor scyphostatin prevents and ceramide mimics mechanotransduction in vascular endothelium. Am. J. Physiol. Heart. Circ Physiol. 287, H1344-H1352 (2004).
    • (2004) Am. J. Physiol. Heart. Circ Physiol , vol.287
    • Czarny, M.1    Schnitzer, J.E.2
  • 118
    • 17344376055 scopus 로고    scopus 로고
    • Mechanotransduction: All signals point to cytoskeleton, matrix, and integrins
    • Alenghat, F.J. & Ingber, D.E. Mechanotransduction: all signals point to cytoskeleton, matrix, and integrins. Sci. STKE 2002, PE6 (2002).
    • (2002) Sci. STKE , vol.2002
    • Alenghat, F.J.1    Ingber, D.E.2
  • 119
    • 2342469391 scopus 로고    scopus 로고
    • Regulation of sodium channel function by bilayer elasticity: The importance of hydrophobic coupling. Effects of micelle-forming amphiphiles and cholesterol
    • Lundbaek, J.A. et al. Regulation of sodium channel function by bilayer elasticity: the importance of hydrophobic coupling. Effects of micelle-forming amphiphiles and cholesterol. J. Gen. Physiol. 123, 599-621 (2004).
    • (2004) J. Gen. Physiol , vol.123 , pp. 599-621
    • Lundbaek, J.A.1
  • 120
    • 0037339478 scopus 로고    scopus 로고
    • Cholesterol-induced protein sorting: An analysis of energetic feasibility
    • Lundbaek, J.A., Andersen, O.S., Werge, T. & Nielsen, C. Cholesterol-induced protein sorting: an analysis of energetic feasibility. Biophys. J. 84, 2080-2089 (2003).
    • (2003) Biophys. J , vol.84 , pp. 2080-2089
    • Lundbaek, J.A.1    Andersen, O.S.2    Werge, T.3    Nielsen, C.4
  • 122
    • 0028953271 scopus 로고
    • Reduction of caveolin and caveolae in oncogenically transformed cells
    • Koleske, A.J., Baltimore, D. & Lisanti, M.P. Reduction of caveolin and caveolae in oncogenically transformed cells. Proc. Natl Acad. Sci. USA 92, 1381-1385 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1381-1385
    • Koleske, A.J.1    Baltimore, D.2    Lisanti, M.P.3
  • 123
    • 0032546319 scopus 로고    scopus 로고
    • Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells
    • Lee, S.W., Reimer, C.L., Oh, P., Campbell, D.B. & Schnitzer, J.E. Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells. Oncogene 16, 1391-1397 (1998).
    • (1998) Oncogene , vol.16 , pp. 1391-1397
    • Lee, S.W.1    Reimer, C.L.2    Oh, P.3    Campbell, D.B.4    Schnitzer, J.E.5
  • 124
    • 0035866759 scopus 로고    scopus 로고
    • Invasion activating caveolin-1 mutation in human scirrhous breast cancers
    • Hayashi, K. et al. Invasion activating caveolin-1 mutation in human scirrhous breast cancers. Cancer Res. 61, 2361-2364 (2001).
    • (2001) Cancer Res , vol.61 , pp. 2361-2364
    • Hayashi, K.1
  • 125
    • 0037342807 scopus 로고    scopus 로고
    • Loss of caveolin-1 gene expression accelerates the development of dysplastic mammary lesions in tumor-prone transgenic mice
    • Williams, T.M. et al. Loss of caveolin-1 gene expression accelerates the development of dysplastic mammary lesions in tumor-prone transgenic mice. Mol. Biol. Cell 14, 1027-1042 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1027-1042
    • Williams, T.M.1
  • 126
    • 0038751964 scopus 로고    scopus 로고
    • Absence of caveolin-1 sensitizes mouse skin to carcinogen-induced epidermal hyperplasia and tumor formation
    • Capozza, F. et al. Absence of caveolin-1 sensitizes mouse skin to carcinogen-induced epidermal hyperplasia and tumor formation. Am. J. Pathol. 162, 2029-2039 (2003).
    • (2003) Am. J. Pathol , vol.162 , pp. 2029-2039
    • Capozza, F.1
  • 127
    • 33744776333 scopus 로고    scopus 로고
    • Caveolin-1 mutations in human breast cancer: Functional association with estrogen receptor α-positive status
    • Li, T. et al. Caveolin-1 mutations in human breast cancer: functional association with estrogen receptor α-positive status. Am. J. Pathol. 168, 1998-2013 (2006).
    • (2006) Am. J. Pathol , vol.168 , pp. 1998-2013
    • Li, T.1
  • 128
    • 3042569629 scopus 로고    scopus 로고
    • Different roles for caveolin-1 in the development of non-small cell lung cancer versus small cell lung cancer
    • Sunaga, N. et al. Different roles for caveolin-1 in the development of non-small cell lung cancer versus small cell lung cancer. Cancer Res. 64, 4277-4285 (2004).
    • (2004) Cancer Res , vol.64 , pp. 4277-4285
    • Sunaga, N.1
  • 129
    • 0032831879 scopus 로고    scopus 로고
    • Caveolin-1, a metastasis-related gene that promotes cell survival in prostate cancer
    • Thompson, T.C., Timme, T.L., Li, L. & Goltsov, A. Caveolin-1, a metastasis-related gene that promotes cell survival in prostate cancer. Apoptosis 4, 233-237 (1999).
    • (1999) Apoptosis , vol.4 , pp. 233-237
    • Thompson, T.C.1    Timme, T.L.2    Li, L.3    Goltsov, A.4
  • 130
    • 14744275841 scopus 로고    scopus 로고
    • Combined c-Myc and caveolin-1 expression in human prostate carcinoma predicts prostate carcinoma progression
    • Yang, G., Timme, T.L., Frolov, A., Wheeler, T.M. & Thompson, T.C. Combined c-Myc and caveolin-1 expression in human prostate carcinoma predicts prostate carcinoma progression. Cancer 103, 1186-1194 (2005).
    • (2005) Cancer , vol.103 , pp. 1186-1194
    • Yang, G.1    Timme, T.L.2    Frolov, A.3    Wheeler, T.M.4    Thompson, T.C.5
  • 131
    • 0035956556 scopus 로고    scopus 로고
    • A sporadic case of rippling muscle disease caused by a de novo caveolin-3 mutation
    • Vorgerd, M. et al. A sporadic case of rippling muscle disease caused by a de novo caveolin-3 mutation. Neurology 57, 2273-2277 (2001).
    • (2001) Neurology , vol.57 , pp. 2273-2277
    • Vorgerd, M.1
  • 132
    • 0345582159 scopus 로고    scopus 로고
    • Caveolin-3 in muscular dystrophy
    • McNally, E.M. et al. Caveolin-3 in muscular dystrophy. Hum. Mol. Genet. 7, 871-877 (1998).
    • (1998) Hum. Mol. Genet , vol.7 , pp. 871-877
    • McNally, E.M.1
  • 133
    • 1342267006 scopus 로고    scopus 로고
    • Caveolinopathies: Mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases
    • Woodman, S.E., Sotgia, F., Galbiati, F., Minetti, C. & Lisanti, M.P. Caveolinopathies: mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases. Neurology 62, 538-543 (2004).
    • (2004) Neurology , vol.62 , pp. 538-543
    • Woodman, S.E.1    Sotgia, F.2    Galbiati, F.3    Minetti, C.4    Lisanti, M.P.5
  • 134
    • 0031920515 scopus 로고    scopus 로고
    • Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy
    • Minetti, C. et al. Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy. Nature Genet. 18, 365-368 (1998).
    • (1998) Nature Genet , vol.18 , pp. 365-368
    • Minetti, C.1
  • 135
    • 0033520482 scopus 로고    scopus 로고
    • 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
    • Galbiati, F., Volonte, D., Minetti, C., Chu, J.B. & Lisanti, M.P. 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. 274, 25632-25641 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 25632-25641
    • Galbiati, F.1    Volonte, D.2    Minetti, C.3    Chu, J.B.4    Lisanti, M.P.5
  • 136
    • 0035880516 scopus 로고    scopus 로고
    • The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle
    • Matsuda, C. et al. The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle. Hum. Mol. Genet. 10, 1761-1766 (2001).
    • (2001) Hum. Mol. Genet , vol.10 , pp. 1761-1766
    • Matsuda, C.1
  • 137
    • 0037195870 scopus 로고    scopus 로고
    • Characterization of a distinct plasma membrane macrodomain in differentiated adipocytes
    • Parton, R.G., Molero, J.C., Floetenmeyer, M., Green, K.M. & James, D.E. Characterization of a distinct plasma membrane macrodomain in differentiated adipocytes. J. Biol. Chem. 277, 46769-46778 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 46769-46778
    • Parton, R.G.1    Molero, J.C.2    Floetenmeyer, M.3    Green, K.M.4    James, D.E.5
  • 138
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L.J., De Hoog, C.L. & Mann, M. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl Acad. Sci. USA 100, 5813-5818 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 139
    • 24144480448 scopus 로고    scopus 로고
    • Zebrafish as a model for caveolinassociated muscle disease; caveolin-3 is required for myofibril organization and muscle cell patterning
    • Nixon, S.J. et al. Zebrafish as a model for caveolinassociated muscle disease; caveolin-3 is required for myofibril organization and muscle cell patterning. Hum. Mol. Genet. 14, 1727-1743 (2005).
    • (2005) Hum. Mol. Genet , vol.14 , pp. 1727-1743
    • Nixon, S.J.1
  • 140
    • 1342268582 scopus 로고    scopus 로고
    • Overexpression of P104L mutant caveolin-3 in mice develops hypertrophic cardiomyopathy with enhanced contractility in association with increased endothelial nitric oxide synthase activity
    • Ohsawa, Y. et al. Overexpression of P104L mutant caveolin-3 in mice develops hypertrophic cardiomyopathy with enhanced contractility in association with increased endothelial nitric oxide synthase activity. Hum. Mol. Genet. 13, 151-157 (2004).
    • (2004) Hum. Mol. Genet , vol.13 , pp. 151-157
    • Ohsawa, Y.1
  • 141
    • 0037470170 scopus 로고    scopus 로고
    • Glycosphingolipids internalized via caveolar-related endocytosis rapidly merge with the clathrin pathway in early endosomes and form microdomains for recycling
    • Sharma, D.K. et al. Glycosphingolipids internalized via caveolar-related endocytosis rapidly merge with the clathrin pathway in early endosomes and form microdomains for recycling. J. Biol. Chem. 278, 7564-7572 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 7564-7572
    • Sharma, D.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.