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Volumn 6, Issue , 2015, Pages

Dynamic caveolae exclude bulk membrane proteins and are required for sorting of excess glycosphingolipids

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLIN 1; CAVIN 1; CLATHRIN; GLYCOSPHINGOLIPID; GREEN FLUORESCENT PROTEIN; MEMBRANE LIPID; MEMBRANE PROTEIN; PROTEIN TAG; UNCLASSIFIED DRUG; PHOTOPROTEIN; RECOMBINANT PROTEIN; RED FLUORESCENT PROTEIN;

EID: 84928383355     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7867     Document Type: Article
Times cited : (80)

References (70)
  • 1
    • 84872959202 scopus 로고    scopus 로고
    • Caveolae as plasma membrane sensors, protectors and organizers
    • Parton, R. G. & del Pozo, M. A. Caveolae as plasma membrane sensors, protectors and organizers. Nat. Rev. Mol. Cell Biol. 14, 98-112 (2013).
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 98-112
    • Parton, R.G.1    Del Pozo, M.A.2
  • 2
    • 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
  • 3
    • 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
  • 4
    • 84883200920 scopus 로고    scopus 로고
    • Molecular composition and ultrastructure of the caveolar coat complex
    • Ludwig, A. et al. Molecular composition and ultrastructure of the caveolar coat complex. PLoS Biol. 11, e1001640 (2013).
    • (2013) PLoS Biol. , vol.11 , pp. e1001640
    • Ludwig, A.1
  • 5
    • 84898722791 scopus 로고    scopus 로고
    • Single-molecule analysis reveals self assembly and nanoscale segregation of two distinct cavin subcomplexes on caveolae
    • Gambin, Y. et al. Single-molecule analysis reveals self assembly and nanoscale segregation of two distinct cavin subcomplexes on caveolae. Elife 3, e01434 (2013).
    • (2013) Elife , vol.3 , pp. e01434
    • Gambin, Y.1
  • 6
    • 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 (2009).
    • (2009) Traffic , vol.11 , pp. 361-382
    • Hayer, A.1    Stoeber, M.2    Bissig, C.3    Helenius, A.4
  • 7
    • 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. Nat. Cell Biol. 11, 807-814 (2009).
    • (2009) Nat. Cell Biol. , vol.11 , pp. 807-814
    • Hansen, C.G.1    Bright, N.A.2    Howard, G.3    Nichols, B.J.4
  • 8
    • 79961148348 scopus 로고    scopus 로고
    • MURC/Cavin-4 and cavin family members form tissuespecific caveolar complexes
    • Bastiani, M. et al. MURC/Cavin-4 and cavin family members form tissuespecific caveolar complexes. J. Cell Biol. 22, 22 (2009).
    • (2009) J. Cell Biol. , vol.22 , pp. 22
    • Bastiani, M.1
  • 9
    • 42949174820 scopus 로고    scopus 로고
    • A critical role of cavin (polymerase i and transcript release factor) in caveolae formation and organization
    • Liu, L. & Pilch, P. F. A critical role of cavin (polymerase I and transcript release factor) in caveolae formation and organization. J. Biol. Chem. 283, 4314-4322 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 4314-4322
    • Liu, L.1    Pilch, P.F.2
  • 10
    • 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
  • 12
    • 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
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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
  • 18
    • 84867397589 scopus 로고    scopus 로고
    • Ultrastructural freeze-fracture immunolabeling identifies plasma membrane-localized syndapin II as a crucial factor in shaping caveolae
    • Koch, D., Westermann, M., Kessels, M. M. & Qualmann, B. Ultrastructural freeze-fracture immunolabeling identifies plasma membrane-localized syndapin II as a crucial factor in shaping caveolae. Histochem. Cell Biol. 138, 215-230 (2012).
    • (2012) Histochem. Cell Biol. , vol.138 , pp. 215-230
    • Koch, D.1    Westermann, M.2    Kessels, M.M.3    Qualmann, B.4
  • 19
    • 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
  • 20
    • 0035851197 scopus 로고    scopus 로고
    • Caveolin-1 null mice are viable but show evidence of hyperproliferative and vascular abnormalities
    • Razani, B. et al. Caveolin-1 null mice are viable but show evidence of hyperproliferative and vascular abnormalities. J. Biol. Chem. 276, 38121-38138 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 38121-38138
    • Razani, B.1
  • 21
    • 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
  • 22
    • 84884686757 scopus 로고    scopus 로고
    • Caveolae internalization repairs wounded cells and muscle fibers
    • Corrotte, M. et al. Caveolae internalization repairs wounded cells and muscle fibers. Elife 2, e00926 (2013).
    • (2013) Elife , vol.2 , pp. e00926
    • Corrotte, M.1
  • 23
    • 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
  • 24
    • 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 , pp. e1000874
    • Rajab, A.1
  • 25
    • 65249110451 scopus 로고    scopus 로고
    • Caveolin-2 is required for apical lipid trafficking and suppresses basolateral recycling defects in the intestine of Caenorhabditis elegans
    • Parker, S., Walker, D. S., Ly, S. & Baylis, H. A. Caveolin-2 is required for apical lipid trafficking and suppresses basolateral recycling defects in the intestine of Caenorhabditis elegans. Mol. Biol. Cell 20, 1763-1771 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1763-1771
    • Parker, S.1    Walker, D.S.2    Ly, S.3    Baylis, H.A.4
  • 26
    • 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
  • 27
    • 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. 119, 2623-2633 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 2623-2633
    • Hayashi, Y.K.1
  • 28
    • 84896916990 scopus 로고    scopus 로고
    • Pleiotropic effects of cavin-1 deficiency on lipid metabolism
    • Ding, S. Y. et al. Pleiotropic effects of cavin-1 deficiency on lipid metabolism. J. Biol. Chem. 289, 8473-8483 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 8473-8483
    • Ding, S.Y.1
  • 29
    • 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
  • 30
    • 84863416895 scopus 로고    scopus 로고
    • Altered mitochondrial function and metabolic inflexibility associated with loss of caveolin-1
    • Wernstedt Asterholm, I., 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
    • Wernstedt Asterholm, I.1    Mundy, D.I.2    Weng, J.3    Anderson, R.G.4    Scherer, P.E.5
  • 31
    • 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
  • 32
    • 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. Nat. Cell Biol. 3, 473-483 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 33
    • 0345706824 scopus 로고    scopus 로고
    • Caveosomes and endocytosis of lipid rafts
    • Nichols, B. Caveosomes and endocytosis of lipid rafts. J. Cell Sci. 116, 4707-4714 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 4707-4714
    • Nichols, B.1
  • 34
    • 0036094927 scopus 로고    scopus 로고
    • A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex
    • Nichols, B. J. A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex. Nat. Cell Biol. 4, 374-378 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 374-378
    • Nichols, B.J.1
  • 35
    • 79955436301 scopus 로고    scopus 로고
    • Role of endosomes in simian virus 40 entry and infection
    • Engel, S. et al. Role of endosomes in simian virus 40 entry and infection. J. Virol. 85, 4198-4211 (2011).
    • (2011) J. Virol. , vol.85 , pp. 4198-4211
    • Engel, S.1
  • 36
    • 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
  • 37
    • 78049499223 scopus 로고    scopus 로고
    • Revisiting caveolin trafficking: The end of the caveosome
    • Parton, R. G. & Howes, M. T. Revisiting caveolin trafficking: the end of the caveosome. J. Cell Biol. 191, 439-441 (2010).
    • (2010) J. Cell Biol. , vol.191 , pp. 439-441
    • Parton, R.G.1    Howes, M.T.2
  • 38
    • 0037113074 scopus 로고    scopus 로고
    • Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton
    • Mundy, D. I., Machleidt, T., Ying, Y. S., Anderson, R. G. & Bloom, G. S. Dual control of caveolar membrane traffic by microtubules and the actin cytoskeleton. J. Cell. Sci. 115, 4327-4339 (2002).
    • (2002) J. Cell. Sci. , vol.115 , pp. 4327-4339
    • Mundy, D.I.1    Machleidt, T.2    Ying, Y.S.3    Anderson, R.G.4    Bloom, G.S.5
  • 39
    • 84878592690 scopus 로고    scopus 로고
    • Deletion of cavin genes reveals tissue-specific mechanisms for morphogenesis of endothelial caveolae
    • Hansen, C. G., Shvets, E., Howard, G., Riento, K. & Nichols, B. J. Deletion of cavin genes reveals tissue-specific mechanisms for morphogenesis of endothelial caveolae. Nat. Commun. 4, 1831 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1831
    • Hansen, C.G.1    Shvets, E.2    Howard, G.3    Riento, K.4    Nichols, B.J.5
  • 40
    • 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
  • 41
    • 84964312390 scopus 로고    scopus 로고
    • Clathrin-independent pathways do not contribute significantly to endocytic flux
    • Bitsikas, V., Correa, Jr. I. R. & Nichols, B. J. Clathrin-independent pathways do not contribute significantly to endocytic flux. Elife 3, e03970 (2014).
    • (2014) Elife , vol.3 , pp. e03970
    • Bitsikas, V.1    Correa, I.R.2    Nichols, B.J.3
  • 42
    • 84864025624 scopus 로고    scopus 로고
    • Structure-based reassessment of the caveolin signaling model: Do caveolae regulate signaling through caveolin-protein interactions?
    • 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) Dev. Cell. , vol.23 , pp. 11-20
    • Collins, B.M.1    Davis, M.J.2    Hancock, J.F.3    Parton, R.G.4
  • 43
    • 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
  • 44
    • 84895770533 scopus 로고    scopus 로고
    • Caveolae regulate the nanoscale organization of the plasma membrane to remotely control Ras signaling
    • Ariotti, N. et al. Caveolae regulate the nanoscale organization of the plasma membrane to remotely control Ras signaling. J. Cell Biol. 204, 777-792 (2014).
    • (2014) J. Cell Biol. , vol.204 , pp. 777-792
    • Ariotti, N.1
  • 45
    • 0035817629 scopus 로고    scopus 로고
    • Clathrin-dependent and -independent internalization of plasma membrane sphingolipids initiates two Golgi targeting pathways
    • Puri, V. et al. Clathrin-dependent and -independent internalization of plasma membrane sphingolipids initiates two Golgi targeting pathways. J. Cell Biol. 154, 535-547 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 535-547
    • Puri, V.1
  • 46
    • 2442688008 scopus 로고    scopus 로고
    • Pathways followed by protein toxins into cells
    • Sandvig, K. et al. Pathways followed by protein toxins into cells. Int. J. Med. Microbiol. 293, 483-490 (2004).
    • (2004) Int. J. Med. Microbiol. , vol.293 , pp. 483-490
    • Sandvig, K.1
  • 47
    • 36749032244 scopus 로고    scopus 로고
    • Shiga toxin induces tubular membrane invaginations for its uptake into cells
    • Romer, W. et al. Shiga toxin induces tubular membrane invaginations for its uptake into cells. Nature 450, 670-675 (2007).
    • (2007) Nature , vol.450 , pp. 670-675
    • Romer, W.1
  • 48
    • 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. Nat. Cell. Biol. 13, 331-337 (2011).
    • (2011) Nat. Cell. Biol. , vol.13 , pp. 331-337
    • Doyon, J.B.1
  • 49
    • 84873734105 scopus 로고    scopus 로고
    • RNA-guided human genome engineering via Cas9
    • Mali, P. et al. RNA-guided human genome engineering via Cas9. Science 339, 823-826 (2013).
    • (2013) Science , vol.339 , pp. 823-826
    • Mali, P.1
  • 50
    • 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
  • 51
    • 21844454457 scopus 로고    scopus 로고
    • Kinase-regulated quantal assemblies and kiss-andrun recycling of caveolae
    • Pelkmans, L. & Zerial, M. Kinase-regulated quantal assemblies and kiss-andrun recycling of caveolae. Nature 436, 128-133 (2005).
    • (2005) Nature , vol.436 , pp. 128-133
    • Pelkmans, L.1    Zerial, M.2
  • 52
    • 0035135419 scopus 로고    scopus 로고
    • Simultaneous binding of PtdIns(45)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes
    • Ford, M. G. et al. Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes. Science 291, 1051-1055 (2001).
    • (2001) Science , vol.291 , pp. 1051-1055
    • Ford, M.G.1
  • 53
    • 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
  • 55
    • 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
  • 56
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma, P. et al. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 116, 577-589 (2004).
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1
  • 57
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • Mayor, S., Rothberg, K. G. & Maxfield, F. R. Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science 264, 1948-1951 (1994).
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 58
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • Kenworthy, A. K., Petranova, N. & Edidin, M. High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol. Biol. Cell. 11, 1645-1655 (2000).
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 59
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • Glebov, O. O. & Nichols, B. J. Lipid raft proteins have a random distribution during localized activation of the T-cell receptor. Nat. Cell Biol. 6, 238-243 (2004).
    • (2004) Nat. Cell Biol. , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 60
    • 84869458315 scopus 로고    scopus 로고
    • Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy
    • Martell, J. D. et al. Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy. Nat. Biotechnol. 30, 1143-1148 (2012).
    • (2012) Nat. Biotechnol. , vol.30 , pp. 1143-1148
    • Martell, J.D.1
  • 61
    • 33645292025 scopus 로고    scopus 로고
    • Membrane microdomains, caveolae, and caveolar endocytosis of sphingolipids
    • Cheng, Z. J., Singh, R. D., Marks, D. L. & Pagano, R. E. Membrane microdomains, caveolae, and caveolar endocytosis of sphingolipids. Mol. Membr. Biol. 23, 101-110 (2006).
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 101-110
    • Cheng, Z.J.1    Singh, R.D.2    Marks, D.L.3    Pagano, R.E.4
  • 62
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • Mayor, S. & Pagano, R. E. Pathways of clathrin-independent endocytosis. Nat. Rev. Mol. Cell Biol. 8, 603-612 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 63
    • 13444310587 scopus 로고    scopus 로고
    • Ultrastructural identification of uncoated caveolinindependent early endocytic vehicles
    • Kirkham, M. et al. Ultrastructural identification of uncoated caveolinindependent early endocytic vehicles. J. Cell Biol. 168, 465-476 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 465-476
    • Kirkham, M.1
  • 64
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • Simons, K. & Ikonen, E. How cells handle cholesterol. Science 290, 1721-1726 (2000).
    • (2000) Science , vol.290 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 65
    • 0031687965 scopus 로고    scopus 로고
    • Cholesterol distribution in living cells: Fluorescence imaging using dehydroergosterol as a fluorescent cholesterol analog
    • Mukherjee, S., Zha, X., Tabas, I. & Maxfield, F. R. Cholesterol distribution in living cells: fluorescence imaging using dehydroergosterol as a fluorescent cholesterol analog. Biophys. J. 75, 1915-1925 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 1915-1925
    • Mukherjee, S.1    Zha, X.2    Tabas, I.3    Maxfield, F.R.4
  • 66
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrinindependent endocytic pathway in mammalian cells
    • Glebov, O. O., Bright, N. A. & Nichols, B. J. Flotillin-1 defines a clathrinindependent endocytic pathway in mammalian cells. Nat. Cell Biol. 8, 46-54 (2006).
    • (2006) Nat. Cell Biol. , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 67
    • 33847328318 scopus 로고    scopus 로고
    • Modulation of lateral diffusion in the plasma membrane by protein density
    • Frick, M., Schmidt, K. & Nichols, B. J. Modulation of lateral diffusion in the plasma membrane by protein density. Curr. Biol. 17, 462-467 (2007).
    • (2007) Curr. Biol. , vol.17 , pp. 462-467
    • Frick, M.1    Schmidt, K.2    Nichols, B.J.3
  • 68
    • 80255134581 scopus 로고    scopus 로고
    • Surrogate reporters for enrichment of cells with nuclease-induced mutations
    • Kim, H. et al. Surrogate reporters for enrichment of cells with nuclease-induced mutations. Nat. Methods 8, 941-943 (2011).
    • (2011) Nat. Methods , vol.8 , pp. 941-943
    • Kim, H.1
  • 69
    • 34248562159 scopus 로고    scopus 로고
    • Fusion PCR and gene targeting in Aspergillus nidulans
    • Szewczyk, E. et al. Fusion PCR and gene targeting in Aspergillus nidulans. Nat. Protoc. 1, 3111-3120 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 3111-3120
    • Szewczyk, E.1
  • 70
    • 0037119406 scopus 로고    scopus 로고
    • Rapid nonvesicular transport of sterol between the plasma membrane domains of polarized hepatic cells
    • Wustner, D., Herrmann, A., Hao, M. & Maxfield, F. R. Rapid nonvesicular transport of sterol between the plasma membrane domains of polarized hepatic cells. J. Biol. Chem. 277, 30325-30336 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 30325-30336
    • Wustner, D.1    Herrmann, A.2    Hao, M.3    Maxfield, F.R.4


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