메뉴 건너뛰기




Volumn 14, Issue 2, 2013, Pages 98-112

Caveolae as plasma membrane sensors, protectors and organizers

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLIN 1; CAVIN; COAT PROTEIN; FILAMIN A; GREEN FLUORESCENT PROTEIN; INTEGRIN; SERINE; UNCLASSIFIED DRUG;

EID: 84872959202     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3512     Document Type: Article
Times cited : (708)

References (210)
  • 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
    • 70349195987 scopus 로고    scopus 로고
    • Human PTRF mutations cause secondary deficiency of caveolins resulting in muscular dystrophy with generalized lipodystrophy
    • Hayashi, Y. K. et al. Human PTRF mutations cause secondary deficiency of caveolins resulting in muscular dystrophy with generalized lipodystrophy. J. Clin. Invest. 11 9, 2623-2633 (2009).
    • (2009) J. Clin. Invest. , vol.11 , pp. 92623-92633
    • Hayashi, Y.K.1
  • 4
    • 77950431859 scopus 로고    scopus 로고
    • Fatal cardiac arrhythmia and long-QT syndrome in a new form of congenital generalized lipodystrophy with muscle rippling (CGL4) due to PTRF-CAVIN mutations
    • Rajab, A. et al. Fatal cardiac arrhythmia and long-QT syndrome in a new form of congenital generalized lipodystrophy with muscle rippling (CGL4) due to PTRF-CAVIN mutations. PLoS Genet. 6, e1000874 (2010).
    • (2010) PLoS Genet. , vol.6
    • Rajab, A.1
  • 6
    • 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
  • 7
    • 43149102677 scopus 로고    scopus 로고
    • High-resolution 3D quantitative analysis of caveolar ultrastructure and caveola-cytoskeleton interactions
    • Richter, T. et al. High-resolution 3D quantitative analysis of caveolar ultrastructure and caveola-cytoskeleton interactions. Traffic 9, 893-909 (2008).
    • (2008) Traffic , vol.9 , pp. 893-909
    • Richter, T.1
  • 8
    • 77950343947 scopus 로고    scopus 로고
    • The shape of caveolae is omegalike after glutaraldehyde fixation and cup-like after cryofixation
    • Schlormann, W. et al. The shape of caveolae is omegalike after glutaraldehyde fixation and cup-like after cryofixation. Histochem. Cell Biol. 133, 223-228 (2010).
    • (2010) Histochem. Cell Biol. , vol.133 , pp. 223-228
    • Schlormann, W.1
  • 9
    • 34447529246 scopus 로고    scopus 로고
    • Caveolin-1 is required for lateral line neuromast and notochord development
    • Nixon, S. J. et al. Caveolin-1 is required for lateral line neuromast and notochord development. J. Cell Sci. 120, 2151-2161 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 2151-2161
    • Nixon, S.J.1
  • 10
    • 0022364832 scopus 로고
    • Endothelial plasmalemmal vesicles have a characteristic striped bipolar surface structure
    • Peters, K. R., Carley, W. W. & Palade, G. E. Endothelial plasmalemmal vesicles have a characteristic striped bipolar surface structure. J. Cell Biol. 101, 2233-2238 (1985).
    • (1985) J. Cell Biol. , vol.101 , pp. 2233-2238
    • Peters, K.R.1    Carley, W.W.2    Palade, G.E.3
  • 11
    • 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
  • 12
    • 78651322726 scopus 로고    scopus 로고
    • Is caveolin involved in normal proximal tubule function? Presence in model PT systems but absence in situ
    • Zhuang, Z., Marshansky, V., Breton, S. & Brown, D. Is caveolin involved in normal proximal tubule function? Presence in model PT systems but absence in situ. Am. J. Physiol. Renal Physiol. 300, F199-F206 (2011).
    • (2011) Am. J. Physiol. Renal Physiol. , vol.300
    • Zhuang, Z.1    Marshansky, V.2    Breton, S.3    Brown, D.4
  • 13
    • 0141764814 scopus 로고    scopus 로고
    • Cell surface orifices of caveolae and localization of caveolin to the necks of caveolae in adipocytes
    • Thorn, H. et al. Cell surface orifices of caveolae and localization of caveolin to the necks of caveolae in adipocytes. Mol. Biol. Cell 14, 3967-3976 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3967-3976
    • Thorn, H.1
  • 15
    • 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
  • 16
    • 0041969715 scopus 로고    scopus 로고
    • Differential caveolin-1 polarization in endothelial cells during migration in two and three dimensions
    • Parat, M. O., Anand-Apte, B. & Fox, P. L. Differential caveolin-1 polarization in endothelial cells during migration in two and three dimensions. Mol. Biol. Cell 14, 3156-3168 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3156-3168
    • Parat, M.O.1    Anand-Apte, B.2    Fox, P.L.3
  • 17
    • 0026640940 scopus 로고
    • VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
    • Kurzchalia, T. V. et al. VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles. J. Cell Biol. 11 8, 1003-1014 (1992).
    • (1992) J. Cell Biol. , vol.11 , pp. 81003-81014
    • Kurzchalia, T.V.1
  • 18
    • 0030034772 scopus 로고    scopus 로고
    • Identification, sequence, and expression of caveolin-2 defines a caveolin gene family
    • Scherer, P. E. et al. Identification, sequence, and expression of caveolin-2 defines a caveolin gene family. Proc. Natl Acad. Sci. USA 93, 131-135 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 131-135
    • Scherer, P.E.1
  • 19
    • 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
  • 20
    • 57149137051 scopus 로고    scopus 로고
    • Freeze-fracture replica immunolabelling reveals caveolin-1 in the human cardiomyocyte plasma membrane
    • Robenek, H., Weissen-Plenz, G. & Severs, N. J. Freeze-fracture replica immunolabelling reveals caveolin-1 in the human cardiomyocyte plasma membrane. J. Cell. Mol. Med. 12, 2519-2521 (2008).
    • (2008) J. Cell. Mol. Med. , vol.12 , pp. 2519-2521
    • Robenek, H.1    Weissen-Plenz, G.2    Severs, N.J.3
  • 21
    • 33748747144 scopus 로고    scopus 로고
    • Microtubules and actin microfilaments regulate lipid raft/caveolae localization of adenylyl cyclase signaling components
    • Head, B. P. et al. Microtubules and actin microfilaments regulate lipid raft/caveolae localization of adenylyl cyclase signaling components. J. Biol. Chem. 281, 26391-26399 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 26391-26399
    • Head, B.P.1
  • 22
    • 34247620232 scopus 로고    scopus 로고
    • Mechanisms of cardiac protection from ischemia/reperfusion injury: A role for caveolae and caveolin-1
    • Patel, H. H. et al. Mechanisms of cardiac protection from ischemia/reperfusion injury: a role for caveolae and caveolin-1. FASEB J. 21, 1565-1574 (2007).
    • (2007) FASEB J. , vol.21 , pp. 1565-1574
    • Patel, H.H.1
  • 23
    • 80053088287 scopus 로고    scopus 로고
    • Caveolin-1 orchestrates TCR synaptic polarity, signal specificity, and function in CD8 T cells
    • Tomassian, T. et al. Caveolin-1 orchestrates TCR synaptic polarity, signal specificity, and function in CD8 T cells. J. Immunol. 187, 2993-3002 (2011).
    • (2011) J. Immunol. , vol.187 , pp. 2993-3002
    • Tomassian, T.1
  • 24
    • 84859980069 scopus 로고    scopus 로고
    • Caveolin-1 orchestrates the balance between glucose and lipid-dependent energy metabolism: Implications for liver regeneration
    • Fernandez-Rojo, M. A. et al. Caveolin-1 orchestrates the balance between glucose and lipid-dependent energy metabolism: implications for liver regeneration. Hepatology 55, 1574-1584 (2012).
    • (2012) Hepatology , vol.55 , pp. 1574-1584
    • Fernandez-Rojo, M.A.1
  • 25
    • 80053024695 scopus 로고    scopus 로고
    • Neuron-targeted caveolin-1 protein enhances signaling and promotes arborization of primary neurons
    • Head, B. P. et al. Neuron-targeted caveolin-1 protein enhances signaling and promotes arborization of primary neurons. J. Biol. Chem. 286, 33310-33321 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 33310-33321
    • Head, B.P.1
  • 26
    • 78650832142 scopus 로고    scopus 로고
    • Loss of caveolin-1 accelerates neurodegeneration and aging
    • Head, B. P. et al. Loss of caveolin-1 accelerates neurodegeneration and aging. PLoS ONE 5, e15697 (2010).
    • (2010) PLoS ONE , vol.5
    • Head, B.P.1
  • 27
    • 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
  • 28
    • 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
  • 29
    • 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
  • 30
    • 84865206830 scopus 로고    scopus 로고
    • Constitutive formation of caveolae in a bacterium
    • Walser, P. J. et al. Constitutive formation of caveolae in a bacterium. Cell 150, 752-763 (2012).
    • (2012) Cell , vol.150 , pp. 752-763
    • Walser, P.J.1
  • 31
    • 77950860471 scopus 로고    scopus 로고
    • Exploring the caves: Cavins, caveolins and caveolae
    • Hansen, C. G. & Nichols, B. J. Exploring the caves: cavins, caveolins and caveolae. Trends Cell Biol. 20, 177-186 (2010).
    • (2010) Trends Cell Biol. , vol.20 , pp. 177-186
    • Hansen, C.G.1    Nichols, B.J.2
  • 32
    • 67649583182 scopus 로고    scopus 로고
    • MURC/cavin-4 and cavin family members form tissue-specific caveolar complexes
    • Bastiani, M. et al. MURC/cavin-4 and cavin family members form tissue-specific caveolar complexes. J. Cell Biol. 185, 1259-1273 (2009).
    • (2009) J. Cell Biol. , vol.185 , pp. 1259-1273
    • Bastiani, M.1
  • 33
    • 0032525134 scopus 로고    scopus 로고
    • Cloning and functional characterization of PTRF, a novel protein which induces dissociation of paused ternary transcription complexes
    • Jansa, P., Mason, S. W., Hoffmann-Rohrer, U. & Grummt, I. Cloning and functional characterization of PTRF, a novel protein which induces dissociation of paused ternary transcription complexes. EMBO J. 17, 2855-2864 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2855-2864
    • Jansa, P.1    Mason, S.W.2    Hoffmann-Rohrer, U.3    Grummt, I.4
  • 34
    • 0027661333 scopus 로고
    • Serum deprivation response gene is induced by serum starvation but not by contact inhibition
    • Gustincich, S. & Schneider, C. Serum deprivation response gene is induced by serum starvation but not by contact inhibition. Cell Growth Differ. 4, 753-760 (1993).
    • (1993) Cell Growth Differ. , vol.4 , pp. 753-760
    • Gustincich, S.1    Schneider, C.2
  • 35
    • 0030614872 scopus 로고    scopus 로고
    • A protein kinase Cδ-binding protein SRBC whose expression is induced by serum starvation
    • Izumi, Y. et al. A protein kinase Cδ-binding protein SRBC whose expression is induced by serum starvation. J. Biol. Chem. 272, 7381-7389 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 7381-7389
    • Izumi, Y.1
  • 36
    • 43249119946 scopus 로고    scopus 로고
    • MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK pathway, induces cardiac dysfunction and conduction disturbance
    • Ogata, T. et al. MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK pathway, induces cardiac dysfunction and conduction disturbance. Mol. Cell. Biol. 28, 3424-3436 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3424-3436
    • Ogata, T.1
  • 37
    • 55949135301 scopus 로고    scopus 로고
    • MURC, a muscle-restricted coiled-coil protein, is involved in the regulation of skeletal myogenesis
    • Tagawa, M. et al. MURC, a muscle-restricted coiled-coil protein, is involved in the regulation of skeletal myogenesis. Am. J. Physiol. Cell Physiol. 295, C490-C498 (2008).
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Tagawa, M.1
  • 38
    • 37649011760 scopus 로고    scopus 로고
    • PTRF-cavin, a conserved cytoplasmic protein required for caveola formation and function
    • Hill, M. M. et al. PTRF-cavin, a conserved cytoplasmic protein required for caveola formation and function. Cell 132, 113-124 (2008).
    • (2008) Cell , vol.132 , pp. 113-124
    • Hill, M.M.1
  • 39
    • 53049091996 scopus 로고    scopus 로고
    • Deletion of cavin/PTRF causes global loss of caveolae, dyslipidemia, and glucose intolerance
    • Liu, L. et al. Deletion of cavin/PTRF causes global loss of caveolae, dyslipidemia, and glucose intolerance. Cell Metab. 8, 310-317 (2008).
    • (2008) Cell Metab. , vol.8 , pp. 310-317
    • Liu, L.1
  • 40
    • 67650072744 scopus 로고    scopus 로고
    • SDPR induces membrane curvature and functions in the formation of caveolae
    • Hansen, C. G., Bright, N. A., Howard, G. & Nichols, B. J. SDPR induces membrane curvature and functions in the formation of caveolae. Nature Cell Biol. 11, 807-814 (2009).
    • (2009) Nature Cell Biol. , vol.11 , pp. 807-814
    • Hansen, C.G.1    Bright, N.A.2    Howard, G.3    Nichols, B.J.4
  • 41
    • 67349244346 scopus 로고    scopus 로고
    • SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae function
    • McMahon, K. A. et al. SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae function. EMBO J. 28, 1001-1015 (2009).
    • (2009) EMBO J. , vol.28 , pp. 1001-1015
    • McMahon, K.A.1
  • 42
    • 77949557277 scopus 로고    scopus 로고
    • Biogenesis of caveolae: Stepwise assembly of large caveolin and cavin complexes
    • Hayer, A., Stoeber, M., Bissig, C. & Helenius, A. Biogenesis of caveolae: stepwise assembly of large caveolin and cavin complexes. Traffic 11, 361-382 (2010).
    • (2010) Traffic , vol.11 , pp. 361-382
    • Hayer, A.1    Stoeber, M.2    Bissig, C.3    Helenius, A.4
  • 43
    • 0033118814 scopus 로고    scopus 로고
    • The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein
    • Gustincich, S. et al. The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein. Genomics 57, 120-129 (1999).
    • (1999) Genomics , vol.57 , pp. 120-129
    • Gustincich, S.1
  • 44
    • 79961113678 scopus 로고    scopus 로고
    • High-resolution mapping reveals topologically distinct cellular pools of phosphatidylserine
    • Fairn, G. D. et al. High-resolution mapping reveals topologically distinct cellular pools of phosphatidylserine. J. Cell Biol. 194, 257-275 (2011).
    • (2011) J. Cell Biol. , vol.194 , pp. 257-275
    • Fairn, G.D.1
  • 45
    • 0037435608 scopus 로고    scopus 로고
    • Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains
    • Wanaski, S. P., Ng, B. K. & Glaser, M. Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains. Biochemistry 42, 42-56 (2003).
    • (2003) Biochemistry , vol.42 , pp. 42-56
    • Wanaski, S.P.1    Ng, B.K.2    Glaser, M.3
  • 46
    • 79551677684 scopus 로고    scopus 로고
    • Cells respond to mechanical stress by rapid disassembly of caveolae
    • Sinha, B. et al. Cells respond to mechanical stress by rapid disassembly of caveolae. Cell 144, 402-413 (2011).
    • (2011) Cell , vol.144 , pp. 402-413
    • Sinha, B.1
  • 47
    • 84859508881 scopus 로고    scopus 로고
    • Cholesterol depletion in adipocytes causes caveolae collapse concomitant with proteosomal degradation of cavin-2 in a switch-like fashion
    • Breen, M. R., Camps, M., Carvalho-Simoes, F., Zorzano, A. & Pilch, P. F. Cholesterol depletion in adipocytes causes caveolae collapse concomitant with proteosomal degradation of cavin-2 in a switch-like fashion. PLoS ONE 7, e34516 (2012).
    • (2012) PLoS ONE , vol.7
    • Breen, M.R.1    Camps, M.2    Carvalho-Simoes, F.3    Zorzano, A.4    Pilch, P.F.5
  • 48
    • 79151477797 scopus 로고    scopus 로고
    • EHD proteins: Key conductors of endocytic transport
    • Naslavsky, N. & Caplan, S. EHD proteins: key conductors of endocytic transport. Trends Cell Biol. 21, 122-131 (2011).
    • (2011) Trends Cell Biol. , vol.21 , pp. 122-131
    • Naslavsky, N.1    Caplan, S.2
  • 49
    • 35349007899 scopus 로고    scopus 로고
    • Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling
    • Daumke, O. et al. Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling. Nature 449, 923-927 (2007).
    • (2007) Nature , vol.449 , pp. 923-927
    • Daumke, O.1
  • 50
    • 84859396266 scopus 로고    scopus 로고
    • EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization
    • Moren, B. et al. EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization. Mol. Biol. Cell 23, 1316-1329 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1316-1329
    • Moren, B.1
  • 51
    • 84861183378 scopus 로고    scopus 로고
    • Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin
    • Stoeber, M. et al. Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin. EMBO J. 31, 2350-2364 (2012).
    • (2012) EMBO J. , vol.31 , pp. 2350-2364
    • Stoeber, M.1
  • 52
    • 67249137553 scopus 로고    scopus 로고
    • A distinct pool of phosphatidylinositol 4, 5-bisphosphate in caveolae revealed by a nanoscale labeling technique
    • Fujita, A., Cheng, J., Tauchi-Sato, K., Takenawa, T. & Fujimoto, T. A distinct pool of phosphatidylinositol 4, 5-bisphosphate in caveolae revealed by a nanoscale labeling technique. Proc. Natl Acad. Sci. USA 106, 9256-9261 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 9256-9261
    • Fujita, A.1    Cheng, J.2    Tauchi-Sato, K.3    Takenawa, T.4    Fujimoto, T.5
  • 54
    • 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
  • 55
    • 79961145704 scopus 로고    scopus 로고
    • Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis
    • Hansen, C. G., Howard, G. & Nichols, B. J. Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis. J. Cell Sci. 124, 2777-2785 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 2777-2785
    • Hansen, C.G.1    Howard, G.2    Nichols, B.J.3
  • 56
    • 79958105143 scopus 로고    scopus 로고
    • Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting
    • Senju, Y., Itoh, Y., Takano, K., Hamada, S. & Suetsugu, S. Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting. J. Cell Sci. 124, 2032-2040 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 2032-2040
    • Senju, Y.1    Itoh, Y.2    Takano, K.3    Hamada, S.4    Suetsugu, S.5
  • 57
    • 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
  • 58
    • 26944437142 scopus 로고    scopus 로고
    • Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization
    • del Pozo, M. A. et al. Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization. Nature Cell Biol. 7, 901-908 (2005).
    • (2005) Nature Cell Biol. , vol.7 , pp. 901-908
    • Del Pozo, M.A.1
  • 59
    • 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
  • 60
    • 84862773017 scopus 로고    scopus 로고
    • Caveolar domain organization and trafficking is regulated by Abl kinases and mDia1
    • Echarri, A. et al. Caveolar domain organization and trafficking is regulated by Abl kinases and mDia1. J. Cell Sci. 125, 309-3113 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 309-3113
    • Echarri, A.1
  • 62
    • 0031030664 scopus 로고    scopus 로고
    • Caveolin-3 associates with developing T-tubules during muscle differentiation
    • Parton, R. G., Way, M., Zorzi, N. & Stang, E. Caveolin-3 associates with developing T-tubules during muscle differentiation. J. Cell Biol. 136, 137-154 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 137-154
    • Parton, R.G.1    Way, M.2    Zorzi, N.3    Stang, E.4
  • 63
    • 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
  • 64
    • 84862989117 scopus 로고    scopus 로고
    • GM1 structure determines SV40-induced membrane invagination and infection
    • Ewers, H. et al. GM1 structure determines SV40-induced membrane invagination and infection. Nature Cell Biol. 12, 11-18 (2010).
    • (2010) Nature Cell Biol. , vol.12 , pp. 11-18
    • Ewers, H.1
  • 65
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin-and caveolin1-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae
    • Damm, E. M. et al. Clathrin-and caveolin1-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
  • 66
    • 33947146207 scopus 로고    scopus 로고
    • Live dynamic imaging of caveolae pumping targeted antibody rapidly and specifically across endothelium in the lung
    • Oh, P. et al. Live dynamic imaging of caveolae pumping targeted antibody rapidly and specifically across endothelium in the lung. Nature Biotech. 25, 327-337 (2007).
    • (2007) Nature Biotech. , vol.25 , pp. 327-337
    • Oh, P.1
  • 68
    • 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 11 8, 767-780 (2004).
    • (2004) Cell , vol.11 , pp. 8767-8780
    • Pelkmans, L.1    Burli, T.2    Zerial, M.3    Helenius, A.4
  • 69
    • 78049508213 scopus 로고    scopus 로고
    • Caveolin-1 is ubiquitinated and targeted to intralumenal vesicles in endolysosomes for degradation
    • Hayer, A. et al. Caveolin-1 is ubiquitinated and targeted to intralumenal vesicles in endolysosomes for degradation. J. Cell Biol. 191, 615-629 (2010).
    • (2010) J. Cell Biol. , vol.191 , pp. 615-629
    • Hayer, A.1
  • 71
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • Parton, R. G., Joggerst, B. & Simons, K. Regulated internalization of caveolae. J. Cell Biol. 127, 1199-1215 (1994).
    • (1994) J. Cell Biol. , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 72
    • 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
  • 73
    • 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
  • 74
    • 79961132983 scopus 로고    scopus 로고
    • Phosphorylated filamin A regulates actin-linked caveolae dynamics
    • Muriel, O. et al. Phosphorylated filamin A regulates actin-linked caveolae dynamics. J. Cell Sci. 124, 2763-2776 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 2763-2776
    • Muriel, O.1
  • 76
    • 80052451417 scopus 로고    scopus 로고
    • Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations
    • Ritz, D. et al. Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations. Nature Cell Biol. 13, 1116-1123 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 1116-1123
    • Ritz, D.1
  • 77
    • 84855206731 scopus 로고    scopus 로고
    • Recent advances in p97/VCP/Cdc48 cellular functions
    • Yamanaka, K., Sasagawa, Y. & Ogura, T. Recent advances in p97/VCP/Cdc48 cellular functions. Biochim. Biophys. Acta 1823, 130-137 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1823 , pp. 130-137
    • Yamanaka, K.1    Sasagawa, Y.2    Ogura, T.3
  • 78
    • 0033973279 scopus 로고    scopus 로고
    • Identification of filamin as a novel ligand for caveolin-1: Evidence for the organization of caveolin-1-associated membrane domains by the actin cytoskeleton
    • Stahlhut, M. & van Deurs, B. Identification of filamin as a novel ligand for caveolin-1: evidence for the organization of caveolin-1-associated membrane domains by the actin cytoskeleton. Mol. Biol. Cell 11, 325-337 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 325-337
    • Stahlhut, M.1    Van Deurs, B.2
  • 79
    • 77957883339 scopus 로고    scopus 로고
    • Integrin-linked kinase controls microtubule dynamics required for plasma membrane targeting of caveolae
    • Wickstrom, S. A. et al. Integrin-linked kinase controls microtubule dynamics required for plasma membrane targeting of caveolae. Dev. Cell 19, 574-588 (2010).
    • (2010) Dev. Cell , vol.19 , pp. 574-588
    • Wickstrom, S.A.1
  • 80
    • 77949522346 scopus 로고    scopus 로고
    • Gangliosides and β1-integrin are required for caveolae and membrane domains
    • Singh, R. D. et al. Gangliosides and β1-integrin are required for caveolae and membrane domains. Traffic 11, 348-360 (2010).
    • (2010) Traffic , vol.11 , pp. 348-360
    • Singh, R.D.1
  • 81
    • 73949156281 scopus 로고    scopus 로고
    • Filamin A regulates caveolae internalization and trafficking in endothelial cells
    • Sverdlov, M., Shinin, V., Place, A. T., Castellon, M. & Minshall, R. D. Filamin A regulates caveolae internalization and trafficking in endothelial cells. Mol. Biol. Cell 20, 4531-4540 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4531-4540
    • Sverdlov, M.1    Shinin, V.2    Place, A.T.3    Castellon, M.4    Minshall, R.D.5
  • 82
    • 77956934524 scopus 로고    scopus 로고
    • 2+ release
    • 2+ release. J. Cell Sci. 123, 3061-3070 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 3061-3070
    • Sharma, P.1
  • 83
    • 0029294497 scopus 로고
    • Biomechanics of skeletal muscle capillaries: Hemodynamic resistance, endothelial distensibility, and pseudopod formation
    • Lee, J. & Schmid-Schonbein, G. W. Biomechanics of skeletal muscle capillaries: hemodynamic resistance, endothelial distensibility, and pseudopod formation. Ann. Biomed. Eng. 23, 226-246 (1995).
    • (1995) Ann. Biomed. Eng. , vol.23 , pp. 226-246
    • Lee, J.1    Schmid-Schonbein, G.W.2
  • 84
    • 0016754249 scopus 로고
    • The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths
    • Dulhunty, A. F. & Franzini-Armstrong, C. The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths. J. Physiol. 250, 513-539 (1975).
    • (1975) J. Physiol. , vol.250 , pp. 513-539
    • Dulhunty, A.F.1    Franzini-Armstrong, C.2
  • 85
    • 77949528042 scopus 로고    scopus 로고
    • Cl, swell channel activation during swelling in the rat ventricular myocyte
    • Cl, swell channel activation during swelling in the rat ventricular myocyte. PLoS ONE 4, e8312 (2009).
    • (2009) PLoS ONE , vol.4
    • Kozera, L.1    White, E.2    Calaghan, S.3
  • 86
    • 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
  • 87
    • 0032500605 scopus 로고    scopus 로고
    • Rapid mechanotransduction in situ at the luminal cell surface of vascular endothelium and its caveolae
    • Rizzo, V., Sung, A., Oh, P. & Schnitzer, J. E. Rapid mechanotransduction in situ at the luminal cell surface of vascular endothelium and its caveolae. J. Biol. Chem. 273, 26323-26329 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 26323-26329
    • Rizzo, V.1    Sung, A.2    Oh, P.3    Schnitzer, J.E.4
  • 88
    • 16444371939 scopus 로고    scopus 로고
    • Caveolin-1 facilitates mechanosensitive protein kinase B (Akt) signaling in vitro and in vivo
    • 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).
    • (2005) Circ. Res. , vol.96 , pp. 635-642
    • Sedding, D.G.1
  • 89
    • 33646422239 scopus 로고    scopus 로고
    • Direct evidence for the role of caveolin-1 and caveolae in mechanotransduction and remodeling of blood vessels
    • Yu, J. et al. Direct evidence for the role of caveolin-1 and caveolae in mechanotransduction and remodeling of blood vessels. J. Clin. Invest. 11 6, 1284-1291 (2006).
    • (2006) J. Clin. Invest. , vol.11 , pp. 61284-61291
    • Yu, J.1
  • 90
    • 34250646601 scopus 로고    scopus 로고
    • Caveolin-1 phosphorylation is required for stretch-induced EGFR and Akt activation in mesangial cells
    • Zhang, B. et al. Caveolin-1 phosphorylation is required for stretch-induced EGFR and Akt activation in mesangial cells. Cell. Signal. 19, 1690-1700 (2007).
    • (2007) Cell. Signal. , vol.19 , pp. 1690-1700
    • Zhang, B.1
  • 91
    • 84869115072 scopus 로고    scopus 로고
    • Phosphocaveolin-1 is a mechanotransducer that induces caveola biogenesis via Egr1 transcriptional regulation
    • Joshi, B. et al. Phosphocaveolin-1 is a mechanotransducer that induces caveola biogenesis via Egr1 transcriptional regulation. J. Cell Biol. 199, 425-435 (2012).
    • (2012) J. Cell Biol. , vol.199 , pp. 425-435
    • Joshi, B.1
  • 92
    • 12344250442 scopus 로고    scopus 로고
    • Integrin mechanotransduction stimulates caveolin-1 phosphorylation and recruitment of Csk to mediate actin reorganization
    • 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).
    • (2005) Am. J. Physiol. Heart Circ. Physiol. , vol.288
    • Radel, C.1    Rizzo, V.2
  • 93
    • 34249063885 scopus 로고    scopus 로고
    • Caveolin-1 regulates cell polarization and directional migration through Src kinase and Rho GTPases
    • Grande-Garcia, A. et al. Caveolin-1 regulates cell polarization and directional migration through Src kinase and Rho GTPases. J. Cell Biol. 177, 683-694 (2007).
    • (2007) J. Cell Biol. , vol.177 , pp. 683-694
    • Grande-Garcia, A.1
  • 94
    • 79959947008 scopus 로고    scopus 로고
    • Biomechanical remodeling of the microenvironment by stromal caveolin-1 favors tumor invasion and metastasis
    • Goetz, J. G. et al. Biomechanical remodeling of the microenvironment by stromal caveolin-1 favors tumor invasion and metastasis. Cell 146, 148-163 (2011).
    • (2011) Cell , vol.146 , pp. 148-163
    • Goetz, J.G.1
  • 95
    • 79551484695 scopus 로고    scopus 로고
    • P190 RhoGTPase-activating protein links the β1 integrincaveolin-1 mechanosignaling complex to rhoa and actin remodeling
    • Yang, B., Radel, C., Hughes, D., Kelemen, S. & Rizzo, V. p190 RhoGTPase-activating protein links the β1 integrin/caveolin-1 mechanosignaling complex to RhoA and actin remodeling. Arterioscler. Thromb. Vasc. Biol. 31, 376-383 (2011).
    • (2011) Arterioscler. Thromb. Vasc. Biol. , vol.31 , pp. 376-383
    • Yang, B.1    Radel, C.2    Hughes, D.3    Kelemen, S.4    Rizzo, V.5
  • 96
    • 77956834144 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake by inducing Vav2-RhoA-mediated cytoskeletal rearrangements
    • Boettcher, J. P. et al. Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake by inducing Vav2-RhoA-mediated cytoskeletal rearrangements. PLoS Biol. 8, e1000457 (2010).
    • (2010) PLoS Biol. , vol.8
    • Boettcher, J.P.1
  • 97
    • 79960128557 scopus 로고    scopus 로고
    • Regulation of cellular senescence by the essential caveolar component PTRF/cavin-1
    • Bai, L. et al. Regulation of cellular senescence by the essential caveolar component PTRF/cavin-1. Cell Res. 21, 1088-1101 (2011).
    • (2011) Cell Res. , vol.21 , pp. 1088-1101
    • Bai, L.1
  • 98
    • 0034177159 scopus 로고    scopus 로고
    • PTRF (polymerase i and transcript-release factor) is tissue-specific and interacts with the BFCOL1 (binding factor of a type-I collagen promoter) zinc-finger transcription factor which binds to the two mouse type-I collagen gene promoters
    • Hasegawa, T. et al. PTRF (polymerase I and transcript-release factor) is tissue-specific and interacts with the BFCOL1 (binding factor of a type-I collagen promoter) zinc-finger transcription factor which binds to the two mouse type-I collagen gene promoters. Biochem. J. 347 (Pt. 1), 55-59 (2000).
    • (2000) Biochem. J. , vol.347 , Issue.PART 1 , pp. 55-59
    • Hasegawa, T.1
  • 99
    • 38349182440 scopus 로고    scopus 로고
    • Differential dependence of stretch and shear stress signaling on caveolin-1 in the vascular wall
    • Albinsson, S., Nordstrom, I., Sward, K. & Hellstrand, P. Differential dependence of stretch and shear stress signaling on caveolin-1 in the vascular wall. Am. J. Physiol. Cell Physiol. 294, C271-C279 (2008).
    • (2008) Am. J. Physiol. Cell Physiol. , vol.294
    • Albinsson, S.1    Nordstrom, I.2    Sward, K.3    Hellstrand, P.4
  • 101
    • 67650133653 scopus 로고    scopus 로고
    • Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin
    • Cai, C. et al. Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin. J. Biol. Chem. 284, 15894-15902 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 15894-15902
    • Cai, C.1
  • 102
    • 79953836217 scopus 로고    scopus 로고
    • Polymerase transcriptase release factor (PTRF) anchors MG53 protein to cell injury site for initiation of membrane repair
    • Zhu, H. et al. Polymerase transcriptase release factor (PTRF) anchors MG53 protein to cell injury site for initiation of membrane repair. J. Biol. Chem. 286, 12820-12824 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 12820-12824
    • Zhu, H.1
  • 103
    • 33750578365 scopus 로고    scopus 로고
    • Muscular atrophy of caveolin 3-deficient mice is rescued by myostatin inhibition
    • Ohsawa, Y. et al. Muscular atrophy of caveolin 3-deficient mice is rescued by myostatin inhibition. J. Clin. Invest. 11 6, 2924-2934 (2006).
    • (2006) J. Clin. Invest. , vol.11 , pp. 62924-62934
    • Ohsawa, Y.1
  • 104
    • 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
  • 105
    • 70249093948 scopus 로고    scopus 로고
    • The absence of caveolin-1 increases proliferation and anchorage-independent growth by a Rac-dependent, Erk-independent mechanism
    • Cerezo, A. et al. The absence of caveolin-1 increases proliferation and anchorage-independent growth by a Rac-dependent, Erk-independent mechanism. Mol. Cell. Biol. 29, 5046-5059 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5046-5059
    • Cerezo, A.1
  • 106
    • 78650058704 scopus 로고    scopus 로고
    • Integrin α1β1 promotes caveolin-1 dephosphorylation by activating T cell protein-tyrosine phosphatase
    • Borza, C. M. et al. Integrin α1β1 promotes caveolin-1 dephosphorylation by activating T cell protein-tyrosine phosphatase. J. Biol. Chem. 285, 40114-40124 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 40114-40124
    • Borza, C.M.1
  • 107
    • 0032483575 scopus 로고    scopus 로고
    • A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent 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 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
  • 108
    • 79959345857 scopus 로고    scopus 로고
    • Integrin activation and internalization on soft ECM as a mechanism of induction of stem cell differentiation by ECM elasticity
    • Du, J. et al. Integrin activation and internalization on soft ECM as a mechanism of induction of stem cell differentiation by ECM elasticity. Proc. Natl Acad. Sci. USA 108, 9466-9471 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 9466-9471
    • Du, J.1
  • 109
    • 41549127550 scopus 로고    scopus 로고
    • Concerted regulation of focal adhesion dynamics by galectin-3 and tyrosine-phosphorylated caveolin-1
    • Goetz, J. G. et al. Concerted regulation of focal adhesion dynamics by galectin-3 and tyrosine-phosphorylated caveolin-1. J. Cell Biol. 180, 1261-1275 (2008).
    • (2008) J. Cell Biol. , vol.180 , pp. 1261-1275
    • Goetz, J.G.1
  • 110
    • 24944547482 scopus 로고    scopus 로고
    • Tensional homeostasis and the malignant phenotype
    • Paszek, M. J. et al. Tensional homeostasis and the malignant phenotype. Cancer Cell 8, 241-254 (2005).
    • (2005) Cancer Cell , vol.8 , pp. 241-254
    • Paszek, M.J.1
  • 111
    • 80051587832 scopus 로고    scopus 로고
    • ROCK and JAK1 signaling cooperate to control actomyosin contractility in tumor cells and stroma
    • Sanz-Moreno, V. et al. ROCK and JAK1 signaling cooperate to control actomyosin contractility in tumor cells and stroma. Cancer Cell 20, 229-245 (2011).
    • (2011) Cancer Cell , vol.20 , pp. 229-245
    • Sanz-Moreno, V.1
  • 112
    • 70450222098 scopus 로고    scopus 로고
    • Matrix crosslinking forces tumor progression by enhancing integrin signaling
    • Levental, K. R. et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell 139, 891-906 (2009).
    • (2009) Cell , vol.139 , pp. 891-906
    • Levental, K.R.1
  • 113
    • 36749013537 scopus 로고    scopus 로고
    • Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells
    • Gaggioli, C. et al. Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells. Nature Cell Biol. 9, 1392-1400 (2007).
    • (2007) Nature Cell Biol. , vol.9 , pp. 1392-1400
    • Gaggioli, C.1
  • 114
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins
    • Couet, J., Li, S., Okamoto, T., Ikezu, T. & Lisanti, M. P. Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J. Biol. Chem. 272, 6525-6533 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 115
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane
    • Okamoto, T., Schlegel, A., Scherer, P. E. & Lisanti, M. P. Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane. J. Biol. Chem. 273, 5419-5422 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 116
    • 84864025624 scopus 로고    scopus 로고
    • Structure-based reassessment of the caveolin signaling model: Do caveolae regulate signaling through caveolin-protein interactions? Dev
    • Collins, B. M., Davis, M. J., Hancock, J. F. & Parton, R. G. Structure-based reassessment of the caveolin signaling model: do caveolae regulate signaling through caveolin-protein interactions? Dev. Cell 23, 11-20 (2012).
    • (2012) Cell , vol.23 , pp. 11-20
    • Collins, B.M.1    Davis, M.J.2    Hancock, J.F.3    Parton, R.G.4
  • 117
    • 84866443110 scopus 로고    scopus 로고
    • Evaluating caveolin interactions: Do proteins interact with the caveolin scaffolding domain through a widespread aromatic residue-rich motif?
    • Byrne, D. P., Dart, C. & Rigden, D. J. Evaluating caveolin interactions: do proteins interact with the caveolin scaffolding domain through a widespread aromatic residue-rich motif? PLoS ONE 7, e44879 (2012).
    • (2012) PLoS ONE , vol.7
    • Byrne, D.P.1    Dart, C.2    Rigden, D.J.3
  • 118
    • 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
  • 119
    • 0035923728 scopus 로고    scopus 로고
    • Distinction between signaling mechanisms in lipid rafts versus caveolae
    • Sowa, G., Pypaert, M. & Sessa, W. C. Distinction between signaling mechanisms in lipid rafts versus caveolae. Proc. Natl Acad. Sci. USA 98, 14072-14077 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14072-14077
    • Sowa, G.1    Pypaert, M.2    Sessa, W.C.3
  • 120
    • 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
  • 121
    • 80053218128 scopus 로고    scopus 로고
    • Cooperative role of caveolin-1 and C-terminal Src kinase binding protein in C-terminal Src kinase-mediated negative regulation of c-Src
    • Place, A. T. et al. Cooperative role of caveolin-1 and C-terminal Src kinase binding protein in C-terminal Src kinase-mediated negative regulation of c-Src. Mol. Pharmacol. 80, 665-672 (2011).
    • (2011) Mol. Pharmacol. , vol.80 , pp. 665-672
    • Place, A.T.1
  • 122
    • 84555186826 scopus 로고    scopus 로고
    • Caveolin-1 opens endothelial cell junctions by targeting catenins
    • Kronstein, R. et al. Caveolin-1 opens endothelial cell junctions by targeting catenins. Cardiovasc. Res. 93, 130-140 (2012).
    • (2012) Cardiovasc. Res. , vol.93 , pp. 130-140
    • Kronstein, R.1
  • 123
    • 77950360654 scopus 로고    scopus 로고
    • Plasma membrane subdomain compartmentalization contributes to distinct mechanisms of ceramide action on insulin signaling
    • Blouin, C. M. et al. Plasma membrane subdomain compartmentalization contributes to distinct mechanisms of ceramide action on insulin signaling. Diabetes 59, 600-610 (2010).
    • (2010) Diabetes , vol.59 , pp. 600-610
    • Blouin, C.M.1
  • 124
    • 77956864994 scopus 로고    scopus 로고
    • Caveolin-1-ablated mice survive in cold by nonshivering thermogenesis despite desensitized adrenergic responsiveness
    • Mattsson, C. L., Csikasz, R. I., Shabalina, I. G., Nedergaard, J. & Cannon, B. Caveolin-1-ablated mice survive in cold by nonshivering thermogenesis despite desensitized adrenergic responsiveness. Am. J. Physiol. Endocrinol. Metab. 299, e374-e383 (2010).
    • (2010) Am. J. Physiol. Endocrinol. Metab. , vol.299
    • Mattsson, C.L.1    Csikasz, R.I.2    Shabalina, I.G.3    Nedergaard, J.4    Cannon, B.5
  • 125
    • 67651183872 scopus 로고    scopus 로고
    • Caveolin-1 loss of function accelerates glucose transporter 4 and insulin receptor degradation in 3T3-L1 adipocytes
    • Gonzalez-Munoz, E. et al. Caveolin-1 loss of function accelerates glucose transporter 4 and insulin receptor degradation in 3T3-L1 adipocytes. Endocrinology 150, 3493-3502 (2009).
    • (2009) Endocrinology , vol.150 , pp. 3493-3502
    • Gonzalez-Munoz, E.1
  • 126
    • 44449121951 scopus 로고    scopus 로고
    • Caveolin regulates endocytosis of the muscle repair protein, dysferlin
    • Hernandez-Deviez, D. J. et al. Caveolin regulates endocytosis of the muscle repair protein, dysferlin. J. Biol. Chem. 283, 6476-6488 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 6476-6488
    • Hernandez-Deviez, D.J.1
  • 127
    • 77950585581 scopus 로고    scopus 로고
    • Caveolin-1-dependent occludin endocytosis is required for TNF-induced tight junction regulation in vivo
    • Marchiando, A. M. et al. Caveolin-1-dependent occludin endocytosis is required for TNF-induced tight junction regulation in vivo. J. Cell Biol. 189, 111-126 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 111-126
    • Marchiando, A.M.1
  • 128
    • 70350230143 scopus 로고    scopus 로고
    • Caveolae mediate growth factor-induced disassembly of adherens junctions to support tumor cell dissociation
    • Orlichenko, L. et al. Caveolae mediate growth factor-induced disassembly of adherens junctions to support tumor cell dissociation. Mol. Biol. Cell 20, 4140-4152 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4140-4152
    • Orlichenko, L.1
  • 129
    • 0742305342 scopus 로고    scopus 로고
    • Clustering induces a lateral redistribution of α2 β1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization
    • Upla, P. et al. Clustering induces a lateral redistribution of α2 β1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization. Mol. Biol. Cell 15, 625-636 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 625-636
    • Upla, P.1
  • 130
    • 49649095969 scopus 로고    scopus 로고
    • Caveolin-1-dependent β1 integrin endocytosis is a critical regulator of fibronectin turnover
    • Shi, F. & Sottile, J. Caveolin-1-dependent β1 integrin endocytosis is a critical regulator of fibronectin turnover. J. Cell Sci. 121, 2360-2371 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 2360-2371
    • Shi, F.1    Sottile, J.2
  • 131
    • 84858295593 scopus 로고    scopus 로고
    • Distinct recycling of active and inactive β1 integrins
    • Arjonen, A., Alanko, J., Veltel, S. & Ivaska, J. Distinct recycling of active and inactive β1 integrins. Traffic 13, 610-625 (2012).
    • (2012) Traffic , vol.13 , pp. 610-625
    • Arjonen, A.1    Alanko, J.2    Veltel, S.3    Ivaska, J.4
  • 132
    • 51449087302 scopus 로고    scopus 로고
    • Integrin trafficking regulated by Rab21 is necessary for cytokinesis
    • Pellinen, T. et al. Integrin trafficking regulated by Rab21 is necessary for cytokinesis. Dev. Cell 15, 371-385 (2008).
    • (2008) Dev. Cell , vol.15 , pp. 371-385
    • Pellinen, T.1
  • 133
    • 84866905864 scopus 로고    scopus 로고
    • Cell surface expression of human ether -A-go-go-related gene (hERG) channels is regulated by caveolin-3 protein via the ubiquitin ligase Nedd4-2
    • Guo, J. et al. Cell surface expression of human ether-a-go-go-related gene (hERG) channels is regulated by caveolin-3 protein via the ubiquitin ligase Nedd4-2. J. Biol. Chem. 287, 33132-33141 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 33132-33141
    • Guo, J.1
  • 134
    • 67649816872 scopus 로고    scopus 로고
    • The activity of the epithelial sodium channels is regulated by caveolin-1 via a Nedd4-2-dependent mechanism
    • Lee, I. H. et al. The activity of the epithelial sodium channels is regulated by caveolin-1 via a Nedd4-2-dependent mechanism. J. Biol. Chem. 284, 12663-12669 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 12663-12669
    • Lee, I.H.1
  • 135
    • 77749254828 scopus 로고    scopus 로고
    • Caveolin gene transfer improves glucose metabolism in diabetic mice
    • Otsu, K. et al. Caveolin gene transfer improves glucose metabolism in diabetic mice. Am. J. Physiol. Cell Physiol. 298, C450-C456 (2010).
    • (2010) Am. J. Physiol. Cell Physiol. , vol.298
    • Otsu, K.1
  • 136
    • 48049121310 scopus 로고    scopus 로고
    • TRPC1 binds to caveolin-3 and is regulated by Src kinase-role in Duchenne muscular dystrophy
    • Gervasio, O. L., Whitehead, N. P., Yeung, E. W., Phillips, W. D. & Allen, D. G. TRPC1 binds to caveolin-3 and is regulated by Src kinase-role in Duchenne muscular dystrophy. J. Cell Sci. 121, 2246-2255 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 2246-2255
    • Gervasio, O.L.1    Whitehead, N.P.2    Yeung, E.W.3    Phillips, W.D.4    Allen, D.G.5
  • 137
    • 41649104490 scopus 로고    scopus 로고
    • Caveolin-1 and-2 interact with connexin43 and regulate gap junctional intercellular communication in keratinocytes
    • Langlois, S., Cowan, K. N., Shao, Q., Cowan, B. J. & Laird, D. W. Caveolin-1 and-2 interact with connexin43 and regulate gap junctional intercellular communication in keratinocytes. Mol. Biol. Cell 19, 912-928 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 912-928
    • Langlois, S.1    Cowan, K.N.2    Shao, Q.3    Cowan, B.J.4    Laird, D.W.5
  • 138
    • 73949101745 scopus 로고    scopus 로고
    • Activation of TRPC1 by STIM1 in ER-PM microdomains involves release of the channel from its scaffold caveolin-1
    • Pani, B. et al. Activation of TRPC1 by STIM1 in ER-PM microdomains involves release of the channel from its scaffold caveolin-1. Proc. Natl Acad. Sci. USA 106, 20087-20092 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 20087-20092
    • Pani, B.1
  • 140
    • 79955418663 scopus 로고    scopus 로고
    • Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: Sumoylation affects G-protein-coupled receptor desensitization
    • Fuhs, S. R. & Insel, P. A. Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: sumoylation affects G-protein-coupled receptor desensitization. J. Biol. Chem. 286, 14830-14841 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 14830-14841
    • Fuhs, S.R.1    Insel, P.A.2
  • 141
    • 77953162073 scopus 로고    scopus 로고
    • Focal-adhesion targeting links caveolin-1 to a Rac1-degradation pathway
    • Nethe, M. et al. Focal-adhesion targeting links caveolin-1 to a Rac1-degradation pathway. J. Cell Sci. 123, 1948-1958 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 1948-1958
    • Nethe, M.1
  • 142
    • 75649143337 scopus 로고    scopus 로고
    • Caveolin-3 promotes nicotinic acetylcholine receptor clustering and regulates neuromuscular junction activity
    • Hezel, M., de Groat, W. C. & Galbiati, F. Caveolin-3 promotes nicotinic acetylcholine receptor clustering and regulates neuromuscular junction activity. Mol. Biol. Cell 21, 302-310 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 302-310
    • Hezel, M.1    De Groat, W.C.2    Galbiati, F.3
  • 143
    • 0032574603 scopus 로고    scopus 로고
    • 2+ waves preferentially originate at specific loci in caveolin-rich cell edges
    • 2+ waves preferentially originate at specific loci in caveolin-rich cell edges. Proc. Natl Acad. Sci. USA 95, 5009-5014 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5009-5014
    • Isshiki, M.1
  • 144
    • 84857210803 scopus 로고    scopus 로고
    • 2+ waves at caveolae in vascular endothelial cells
    • 2+ waves at caveolae in vascular endothelial cells. J. Cell Sci. 124, 3477-3483 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 3477-3483
    • Yamamoto, K.1
  • 145
    • 77954829892 scopus 로고    scopus 로고
    • Caveolin 3 is associated with the calcium release complex and is modified via in vivo triadin modification
    • Vassilopoulos, S. et al. Caveolin 3 is associated with the calcium release complex and is modified via in vivo triadin modification. Biochemistry 49, 6130-6135 (2010).
    • (2010) Biochemistry , vol.49 , pp. 6130-6135
    • Vassilopoulos, S.1
  • 146
    • 79953018318 scopus 로고    scopus 로고
    • Caveolin-1 assembles type 1 inositol 1, 4, 5-trisphosphate receptors and canonical transient receptor potential 3 channels into a functional signaling complex in arterial smooth muscle cells
    • Adebiyi, A., Narayanan, D. & Jaggar, J. H. Caveolin-1 assembles type 1 inositol 1, 4, 5-trisphosphate receptors and canonical transient receptor potential 3 channels into a functional signaling complex in arterial smooth muscle cells. J. Biol. Chem. 286, 4341-4348 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 4341-4348
    • Adebiyi, A.1    Narayanan, D.2    Jaggar, J.H.3
  • 147
    • 78649738478 scopus 로고    scopus 로고
    • Caveolin limits membrane microdomain mobility and integrin-mediated uptake of fibronectin-binding pathogens
    • Hoffmann, C. et al. Caveolin limits membrane microdomain mobility and integrin-mediated uptake of fibronectin-binding pathogens. J. Cell Sci. 123, 4280-4291 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 4280-4291
    • Hoffmann, C.1
  • 149
    • 0033145517 scopus 로고    scopus 로고
    • Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains
    • Roy, S. et al. Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains. Nature Cell Biol. 1, 98-105 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 98-105
    • Roy, S.1
  • 150
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D. & Simons, K. Lipid rafts as a membrane-organizing principle. Science 327, 46-50 (2010).
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 151
    • 0037124116 scopus 로고    scopus 로고
    • Inhibition of lipid raft-dependent signaling by a dystrophy-associated mutant of caveolin-3
    • Carozzi, A. J. et al. Inhibition of lipid raft-dependent signaling by a dystrophy-associated mutant of caveolin-3. J. Biol. Chem. 277, 17944-17949 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 17944-17949
    • Carozzi, A.J.1
  • 152
    • 47649113551 scopus 로고    scopus 로고
    • Evolutionary analysis and molecular dissection of caveola biogenesis
    • Kirkham, M. et al. Evolutionary analysis and molecular dissection of caveola biogenesis. J. Cell Sci. 121, 2075-2086 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 2075-2086
    • Kirkham, M.1
  • 153
    • 2442653807 scopus 로고    scopus 로고
    • Lipids and glycosphingolipids in caveolae and surrounding plasma membrane of primary rat adipocytes
    • Ortegren, U. et al. Lipids and glycosphingolipids in caveolae and surrounding plasma membrane of primary rat adipocytes. Eur. J. Biochem. 271, 2028-2036 (2004).
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2028-2036
    • Ortegren, U.1
  • 154
    • 24944555198 scopus 로고    scopus 로고
    • The glycosphingolipid, lactosylceramide, regulates β1-integrin clustering and endocytosis
    • Sharma, D. K. et al. The glycosphingolipid, lactosylceramide, regulates β1-integrin clustering and endocytosis. Cancer Res. 65, 8233-8241 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 8233-8241
    • Sharma, D.K.1
  • 155
    • 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
  • 156
    • 70849114215 scopus 로고    scopus 로고
    • GM3 synthase overexpression results in reduced cell motility and in caveolin-1 upregulation in human ovarian carcinoma cells
    • Prinetti, A. et al. GM3 synthase overexpression results in reduced cell motility and in caveolin-1 upregulation in human ovarian carcinoma cells. Glycobiology 20, 62-77 (2010).
    • (2010) Glycobiology , vol.20 , pp. 62-77
    • Prinetti, A.1
  • 157
    • 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
  • 159
    • 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
  • 160
    • 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
  • 161
    • 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
  • 162
    • 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
  • 163
    • 79955471276 scopus 로고    scopus 로고
    • Caveolin-1 deficiency causes cholesterol-dependent mitochondrial dysfunction and apoptotic susceptibility
    • Bosch, M. et al. Caveolin-1 deficiency causes cholesterol-dependent mitochondrial dysfunction and apoptotic susceptibility. Curr. Biol. 21, 681-686 (2011).
    • (2011) Curr. Biol. , vol.21 , pp. 681-686
    • Bosch, M.1
  • 164
    • 84863416895 scopus 로고    scopus 로고
    • Altered mitochondrial function and metabolic inflexibility associated with loss of caveolin-1
    • Asterholm, I. W., Mundy, D. I., Weng, J., Anderson, R. G. & Scherer, P. E. Altered mitochondrial function and metabolic inflexibility associated with loss of caveolin-1. Cell. Metab. 15, 171-185 (2012).
    • (2012) Cell. Metab. , vol.15 , pp. 171-185
    • Asterholm, I.W.1    Mundy, D.I.2    Weng, J.3    Anderson, R.G.4    Scherer, P.E.5
  • 165
    • 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
  • 166
    • 77951032613 scopus 로고    scopus 로고
    • Caveolins sequester fatty acids on the cytoplasmic leaflet of the plasma membrane, augment triglyceride formation and protect cells from lipotoxicity
    • Simard, J. R. et al. Caveolins sequester fatty acids on the cytoplasmic leaflet of the plasma membrane, augment triglyceride formation and protect cells from lipotoxicity. J. Lipid Res. 51, 914-922 (2009).
    • (2009) J. Lipid Res. , vol.51 , pp. 914-922
    • Simard, J.R.1
  • 167
    • 1842426851 scopus 로고    scopus 로고
    • Long-chain fatty acid uptake into adipocytes depends on lipid raft function
    • Pohl, J. et al. Long-chain fatty acid uptake into adipocytes depends on lipid raft function. Biochemistry 43, 4179-4187 (2004).
    • (2004) Biochemistry , vol.43 , pp. 4179-4187
    • Pohl, J.1
  • 168
    • 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
  • 169
    • 33746855808 scopus 로고    scopus 로고
    • Caveolin-1 and regulation of cellular cholesterol homeostasis
    • Frank, P. G. et al. Caveolin-1 and 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
  • 170
    • 2342510295 scopus 로고    scopus 로고
    • Role of caveolin-1 in the modulation of lipolysis and lipid droplet formation
    • Cohen, A. W. et al. Role of caveolin-1 in the modulation of lipolysis and lipid droplet formation. Diabetes 53, 1261-1270 (2004).
    • (2004) Diabetes , vol.53 , pp. 1261-1270
    • Cohen, A.W.1
  • 171
    • 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
  • 172
    • 84858199982 scopus 로고    scopus 로고
    • Adiponectin and cardiovascular disease: Mechanisms and new therapeutic approaches
    • Siasos, G. et al. Adiponectin and cardiovascular disease: mechanisms and new therapeutic approaches. Curr. Med. Chem. 19, 1193-1209 (2012).
    • (2012) Curr. Med. Chem. , vol.19 , pp. 1193-1209
    • Siasos, G.1
  • 173
    • 79960680874 scopus 로고    scopus 로고
    • Fat caves: Caveolae, lipid trafficking and lipid metabolism in adipocytes
    • Pilch, P. F. & Liu, L. Fat caves: caveolae, lipid trafficking and lipid metabolism in adipocytes. Trends Endocrinol. Metab. 22, 318-324 (2011).
    • (2011) Trends Endocrinol. Metab. , vol.22 , pp. 318-324
    • Pilch, P.F.1    Liu, L.2
  • 174
    • 84866864613 scopus 로고    scopus 로고
    • Caveolin-1 deficiency leads to increased susceptibility to cell death and fibrosis in white adipose tissue: Characterization of a lipodystrophic model
    • Martin, S. et al. Caveolin-1 deficiency leads to increased susceptibility to cell death and fibrosis in white adipose tissue: characterization of a lipodystrophic model. PLoS ONE 7, e46242 (2012).
    • (2012) PLoS ONE , vol.7
    • Martin, S.1
  • 175
    • 62849107819 scopus 로고    scopus 로고
    • Metabolic dysregulation and adipose tissue fibrosis: Role of collagen VI
    • Khan, T. et al. Metabolic dysregulation and adipose tissue fibrosis: role of collagen VI. Mol. Cell. Biol. 29, 1575-1591 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1575-1591
    • Khan, T.1
  • 176
    • 84860501617 scopus 로고    scopus 로고
    • Plasma membrane stress induces relocalization of Slm proteins and activation of TORC2 to promote sphingolipid synthesis
    • Berchtold, D. et al. Plasma membrane stress induces relocalization of Slm proteins and activation of TORC2 to promote sphingolipid synthesis. Nature Cell Biol. 14, 542-547 (2012).
    • (2012) Nature Cell Biol. , vol.14 , pp. 542-547
    • Berchtold, D.1
  • 177
    • 47249163819 scopus 로고    scopus 로고
    • Depletion of β-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1
    • Styers, M. L., O'Connor, A. K., Grabski, R., Cormet-Boyaka, E. & Sztul, E. Depletion of β-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1. Am. J. Physiol. Cell Physiol. 294, C1485-C1498 (2008).
    • (2008) Am. J. Physiol. Cell Physiol. , vol.294
    • Styers, M.L.1    O'Connor, A.K.2    Grabski, R.3    Cormet-Boyaka, E.4    Sztul, E.5
  • 178
    • 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
  • 179
    • 24144431634 scopus 로고    scopus 로고
    • Assembly and trafficking of caveolar domains in the cell: Caveolae as stable, cargo-triggered, vesicular transporters
    • 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).
    • (2005) J. Cell Biol. , vol.170 , pp. 769-779
    • Tagawa, A.1
  • 180
    • 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
  • 181
    • 79151475087 scopus 로고    scopus 로고
    • PTRF-cavin-1 expression decreases the migration of PC3 prostate cancer cells: Role of matrix metalloprotease 9
    • Aung, C. S., Hill, M. M., Bastiani, M., Parton, R. G. & Parat, M. O. PTRF-cavin-1 expression decreases the migration of PC3 prostate cancer cells: role of matrix metalloprotease 9. Eur. J. Cell Biol. 90, 136-142 (2011).
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 136-142
    • Aung, C.S.1    Hill, M.M.2    Bastiani, M.3    Parton, R.G.4    Parat, M.O.5
  • 182
    • 77958474331 scopus 로고    scopus 로고
    • Changes in caveolae, caveolin, and polymerase 1 and transcript release factor (PTRF) expression in prostate cancer progression
    • Gould, M. L., Williams, G. & Nicholson, H. D. Changes in caveolae, caveolin, and polymerase 1 and transcript release factor (PTRF) expression in prostate cancer progression. Prostate 70, 1609-1621 (2010).
    • (2010) Prostate , vol.70 , pp. 1609-1621
    • Gould, M.L.1    Williams, G.2    Nicholson, H.D.3
  • 183
    • 79952280348 scopus 로고    scopus 로고
    • Rapid and efficient clathrin-mediated endocytosis revealed in genome-edited mammalian cells
    • Doyon, J. B. et al. Rapid and efficient clathrin-mediated endocytosis revealed in genome-edited mammalian cells. Nature Cell Biol. 13, 331-337 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 331-337
    • Doyon, J.B.1
  • 184
    • 84862759223 scopus 로고    scopus 로고
    • Stressing caveolae new role in cell mechanics
    • Nassoy, P. & Lamaze, C. Stressing caveolae new role in cell mechanics. Trends Cell Biol. 22, 381-389 (2012).
    • (2012) Trends Cell Biol. , vol.22 , pp. 381-389
    • Nassoy, P.1    Lamaze, C.2
  • 185
    • 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
  • 186
    • 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
  • 187
    • 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
  • 188
    • 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
  • 189
    • 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
  • 190
    • 1842556210 scopus 로고    scopus 로고
    • Dysferlin and the plasma membrane repair in muscular dystrophy
    • Bansal, D. & Campbell, K. P. Dysferlin and the plasma membrane repair in muscular dystrophy. Trends Cell Biol. 14, 206-213 (2004).
    • (2004) Trends Cell Biol. , vol.14 , pp. 206-213
    • Bansal, D.1    Campbell, K.P.2
  • 191
    • 33751016041 scopus 로고    scopus 로고
    • Mutant caveolin-3 induces persistent late sodium current and is associated with long-QT syndrome
    • Vatta, M. et al. Mutant caveolin-3 induces persistent late sodium current and is associated with long-QT syndrome. Circulation 11 4, 2104-2112 (2006).
    • (2006) Circulation , vol.11 , pp. 42104-42112
    • Vatta, M.1
  • 192
    • 41549088813 scopus 로고    scopus 로고
    • Heterozygous C AV 1 frameshift mutations (MIM 601047) in patients with atypical partial lipodystrophy and hypertriglyceridemia
    • Cao, H., Alston, L., Ruschman, J. & Hegele, R. A. Heterozygous C AV 1 frameshift mutations (MIM 601047) in patients with atypical partial lipodystrophy and hypertriglyceridemia. Lipids Health Dis. 7, 3 (2008).
    • (2008) Lipids Health Dis. , vol.7 , pp. 3
    • Cao, H.1    Alston, L.2    Ruschman, J.3    Hegele, R.A.4
  • 193
    • 77957244115 scopus 로고    scopus 로고
    • A Japanese child with asymptomatic elevation of serum creatine kinase shows PTRF-CAVIN mutation matching with congenital generalized lipodystrophy type 4
    • Dwianingsih, E. K. et al. A Japanese child with asymptomatic elevation of serum creatine kinase shows PTRF-CAVIN mutation matching with congenital generalized lipodystrophy type 4. Mol. Genet. Metab. 101, 233-237 (2010).
    • (2010) Mol. Genet. Metab. , vol.101 , pp. 233-237
    • Dwianingsih, E.K.1
  • 194
    • 77956097576 scopus 로고    scopus 로고
    • Congenital generalized lipodystrophy, type 4 (CGL4) associated with myopathy due to novel PTRF mutations
    • Shastry, S. et al. Congenital generalized lipodystrophy, type 4 (CGL4) associated with myopathy due to novel PTRF mutations. Am. J. Med. Genet. A 152A, 2245-2253 (2010).
    • (2010) Am. J. Med. Genet. A , vol.152 A , pp. 2245-2253
    • Shastry, S.1
  • 195
    • 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
  • 196
    • 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
  • 197
    • 66549114050 scopus 로고    scopus 로고
    • An absence of stromal caveolin-1 expression predicts early tumor recurrence and poor clinical outcome in human breast cancers
    • Witkiewicz, A. K. et al. An absence of stromal caveolin-1 expression predicts early tumor recurrence and poor clinical outcome in human breast cancers. Am. J. Pathol. 174, 2023-2034 (2009).
    • (2009) Am. J. Pathol. , vol.174 , pp. 2023-2034
    • Witkiewicz, A.K.1
  • 198
    • 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
  • 199
    • 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
  • 200
    • 84856220891 scopus 로고    scopus 로고
    • Non-existence of caveolin-1 gene mutations in human breast cancer
    • Patani, N. et al. Non-existence of caveolin-1 gene mutations in human breast cancer. Breast Cancer Res. Treat. 131, 307-310 (2012).
    • (2012) Breast Cancer Res. Treat. , vol.131 , pp. 307-310
    • Patani, N.1
  • 201
    • 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
  • 202
    • 68549085187 scopus 로고    scopus 로고
    • Caveolin-1 tumor-promoting role in human melanoma
    • Felicetti, F. et al. Caveolin-1 tumor-promoting role in human melanoma. Int. J. Cancer 125, 1514-1522 (2009).
    • (2009) Int. J. Cancer , vol.125 , pp. 1514-1522
    • Felicetti, F.1
  • 203
    • 0032831879 scopus 로고    scopus 로고
    • 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    Caveolin, G.A.4
  • 204
    • 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
  • 205
    • 84860508683 scopus 로고    scopus 로고
    • Genetic ablation of Cav1 differentially affects melanoma tumor growth and metastasis in mice. Role of Cav1 in Shh heterotypic signaling and transendothelial migration
    • Capozza, F. et al. Genetic ablation of Cav1 differentially affects melanoma tumor growth and metastasis in mice. Role of Cav1 in Shh heterotypic signaling and transendothelial migration. Cancer Res. 72, 2262-2274 (2012).
    • (2012) Cancer Res. , vol.72 , pp. 2262-2274
    • Capozza, F.1
  • 206
    • 77957339515 scopus 로고    scopus 로고
    • CAV1 inhibits metastatic potential in melanomas through suppression of the integrin/Src/FAK signaling pathway
    • Trimmer, C. et al. CAV1 inhibits metastatic potential in melanomas through suppression of the integrin/Src/FAK signaling pathway. Cancer Res. 70, 7489-7499 (2010).
    • (2010) Cancer Res. , vol.70 , pp. 7489-7499
    • Trimmer, C.1
  • 207
    • 0035503031 scopus 로고    scopus 로고
    • Inactivation of human SRBC, located within the 11p15.5-p15.4 tumor suppressor region, in breast and lung cancers
    • Xu, X. L. et al. Inactivation of human SRBC, located within the 11p15.5-p15.4 tumor suppressor region, in breast and lung cancers. Cancer Res. 61, 7943-7949 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 7943-7949
    • Xu, X.L.1
  • 208
    • 30544454326 scopus 로고    scopus 로고
    • Expression of the candidate tumor suppressor gene hSRBC is frequently lost in primary lung cancers with and without DNA methylation
    • Zochbauer-Muller, S. et al. Expression of the candidate tumor suppressor gene hSRBC is frequently lost in primary lung cancers with and without DNA methylation. Oncogene 24, 6249-6255 (2005).
    • (2005) Oncogene , vol.24 , pp. 6249-6255
    • Zochbauer-Muller, S.1
  • 209
    • 84055177023 scopus 로고    scopus 로고
    • Down-regulation of the cavin family proteins in breast cancer
    • Bai, L. et al. Down-regulation of the cavin family proteins in breast cancer. J. Cell Biochem. 113, 322-328 (2012).
    • (2012) J. Cell Biochem. , vol.113 , pp. 322-328
    • Bai, L.1
  • 210
    • 33645216741 scopus 로고    scopus 로고
    • Biogenesis of caveolae: A structural model for caveolin-induced domain formation
    • Parton, R. G., Hanzal-Bayer, M. & Hancock, J. F. Biogenesis of caveolae: a structural model for caveolin-induced domain formation. J. Cell Sci. 11 9, 787-796 (2006).
    • (2006) J. Cell Sci. , vol.11 , pp. 9787-9796
    • Parton, R.G.1    Hanzal-Bayer, M.2    Hancock, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.