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Volumn 18, Issue 2, 2007, Pages 337-347

Internalization of large double-membrane intercellular vesicles by a clathrin-dependent endocytic process

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADAPTOR PROTEIN; CLATHRIN; DYNAMIN; MYOSIN VI; PROTEIN DAB2; UNCLASSIFIED DRUG;

EID: 33846817049     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-06-0487     Document Type: Article
Times cited : (149)

References (70)
  • 1
    • 0020462085 scopus 로고
    • Initial events during phagocytosis by macrophages viewed from outside and inside the cell: Membrane-particle interactions and clathrin
    • Aggeler, J., and Werb, Z. (1982). Initial events during phagocytosis by macrophages viewed from outside and inside the cell: membrane-particle interactions and clathrin. J. Cell Biol. 94, 613-623.
    • (1982) J. Cell Biol , vol.94 , pp. 613-623
    • Aggeler, J.1    Werb, Z.2
  • 2
    • 0038107500 scopus 로고    scopus 로고
    • Myo6 facilitates the translocation of endocytic vesicles from cell peripheries
    • Aschenbrenner, L., Lee, T., and Hasson, T. (2003). Myo6 facilitates the translocation of endocytic vesicles from cell peripheries. Mol. Biol. Cell 14, 2728-2743.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2728-2743
    • Aschenbrenner, L.1    Lee, T.2    Hasson, T.3
  • 3
    • 2342512884 scopus 로고    scopus 로고
    • Uncoated endocytic vesicles require the unconventional myosin, Myo6, for rapid transport through actin barriers
    • Aschenbrenner, L., Naccache, S. N., and Hasson, T. (2004). Uncoated endocytic vesicles require the unconventional myosin, Myo6, for rapid transport through actin barriers. Mol. Biol. Cell 15, 2253-2263.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2253-2263
    • Aschenbrenner, L.1    Naccache, S.N.2    Hasson, T.3
  • 4
    • 0032555956 scopus 로고    scopus 로고
    • Rapid turnover of connexin43 in the adult rat heart
    • Beardslee, M. A., Laing, J. G., Beyer, E. C., and Saffitz, J. E. (1998). Rapid turnover of connexin43 in the adult rat heart. Circ. Res. 83, 629-635.
    • (1998) Circ. Res , vol.83 , pp. 629-635
    • Beardslee, M.A.1    Laing, J.G.2    Beyer, E.C.3    Saffitz, J.E.4
  • 5
    • 1942438946 scopus 로고    scopus 로고
    • Pathways for degradation of connexins and gap junctions
    • Berthoud, V. M., Minogue, P. J., Laing, J. G., and Beyer, E. C. (2004). Pathways for degradation of connexins and gap junctions. Cardiovasc. Res. 62, 256-267.
    • (2004) Cardiovasc. Res , vol.62 , pp. 256-267
    • Berthoud, V.M.1    Minogue, P.J.2    Laing, J.G.3    Beyer, E.C.4
  • 6
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino, J. S., and Click, B. S. (2004). The mechanisms of vesicle budding and fusion. Cell 116, 153-166.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Click, B.S.2
  • 7
    • 0029974655 scopus 로고    scopus 로고
    • Connections with connexins: The molecular basis of direct intercellular signaling
    • Brazzone, R., White, T. W., and Paul, D. L. (1996). Connections with connexins: the molecular basis of direct intercellular signaling. Eur. J. Biochem. 238, 1-27.
    • (1996) Eur. J. Biochem , vol.238 , pp. 1-27
    • Brazzone, R.1    White, T.W.2    Paul, D.L.3
  • 8
  • 9
    • 1942445036 scopus 로고    scopus 로고
    • Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton
    • Butkevich, E., Hulsmann, S., Wenzel, D., Shirao, T., Duden, R., and Majoul, I. (2004). Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton. Curr. Biol. 14, 650-658.
    • (2004) Curr. Biol , vol.14 , pp. 650-658
    • Butkevich, E.1    Hulsmann, S.2    Wenzel, D.3    Shirao, T.4    Duden, R.5    Majoul, I.6
  • 10
    • 0024331983 scopus 로고
    • 100-kDa polypeptides in peripheral clathrin-coated vesicles are required for receptor-mediated endocytosis
    • Chin, D. J., Straubinger, R. M., Acton, S., Nèathke, I., and Brodsky, F. M. (1989). 100-kDa polypeptides in peripheral clathrin-coated vesicles are required for receptor-mediated endocytosis. Proc. Natl. Acad. Sci. USA 86, 9289-9293.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9289-9293
    • Chin, D.J.1    Straubinger, R.M.2    Acton, S.3    Nèathke, I.4    Brodsky, F.M.5
  • 11
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner, S. D., and Schmid, S. L. (2003). Regulated portals of entry into the cell. Nature 422, 37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 12
    • 0037213412 scopus 로고    scopus 로고
    • Invasion of mammalian cells by Listeria monocytogenes: Functional mimicry to subvert cellular functions
    • Cossart, P., Pizarro-Cerda, J., and Leant, M. (2003). Invasion of mammalian cells by Listeria monocytogenes: functional mimicry to subvert cellular functions. Trends Cell Biol. 13, 23-31.
    • (2003) Trends Cell Biol , vol.13 , pp. 23-31
    • Cossart, P.1    Pizarro-Cerda, J.2    Leant, M.3
  • 14
    • 1942470893 scopus 로고    scopus 로고
    • Structural bases for the chemical regulation of Connexin43 channels
    • Delmar, M., Coombs, W., Sorgen, P., Duffy, H. S., and Taffet, S. M. (2004). Structural bases for the chemical regulation of Connexin43 channels. Cardiovasc. Res. 62, 268-275.
    • (2004) Cardiovasc. Res , vol.62 , pp. 268-275
    • Delmar, M.1    Coombs, W.2    Sorgen, P.3    Duffy, H.S.4    Taffet, S.M.5
  • 16
    • 0034474693 scopus 로고    scopus 로고
    • Connexin-specific distribution within gap junctions revealed in living cells
    • Falk, M. M. (2000). Connexin-specific distribution within gap junctions revealed in living cells. J. Cell Sci. 113, 4109-4120.
    • (2000) J. Cell Sci , vol.113 , pp. 4109-4120
    • Falk, M.M.1
  • 17
    • 0019603292 scopus 로고
    • Five-hour half-life of mouse liver gap-junction protein
    • Fallon, R. F., and Goodenough, D. A. (1981). Five-hour half-life of mouse liver gap-junction protein. J. Cell Biol. 90, 521-526.
    • (1981) J. Cell Biol , vol.90 , pp. 521-526
    • Fallon, R.F.1    Goodenough, D.A.2
  • 18
  • 20
    • 0029165125 scopus 로고
    • Preparation, characterization, and structure of half gap junctional layers split with urea and EGTA
    • Ghoshroy, S., Goodenough, D. A., and Sosinsky, G. E. (1995). Preparation, characterization, and structure of half gap junctional layers split with urea and EGTA. J. Membr. Biol. 146, 15-28.
    • (1995) J. Membr. Biol , vol.146 , pp. 15-28
    • Ghoshroy, S.1    Goodenough, D.A.2    Sosinsky, G.E.3
  • 21
    • 1942503184 scopus 로고    scopus 로고
    • Gap junctions and connexin-interacting proteins
    • Giepmans, B. N. (2004). Gap junctions and connexin-interacting proteins. Cardiovasc. Res. 62, 233-245.
    • (2004) Cardiovasc. Res , vol.62 , pp. 233-245
    • Giepmans, B.N.1
  • 22
    • 0018409808 scopus 로고
    • Modulation of cell junctions during differentiation of the chicken otocyst sensory epithelium
    • Ginzberg, R. D., and Gilula, N. B. (1979). Modulation of cell junctions during differentiation of the chicken otocyst sensory epithelium. Dev. Biol. 68, 110-129.
    • (1979) Dev. Biol , vol.68 , pp. 110-129
    • Ginzberg, R.D.1    Gilula, N.B.2
  • 24
    • 0016194153 scopus 로고
    • The splitting of hepatocyte gap junctions and zonulae occludentes with hypertonic disaccharides
    • Goodenough, D. A., and Gilula, N. B. (1974). The splitting of hepatocyte gap junctions and zonulae occludentes with hypertonic disaccharides. J. Cell Biol. 61, 575-590.
    • (1974) J. Cell Biol , vol.61 , pp. 575-590
    • Goodenough, D.A.1    Gilula, N.B.2
  • 25
    • 13444301168 scopus 로고    scopus 로고
    • Actin-based motility of intracellular pathogens
    • Gouin, E., Welch, M. D., and Cossart, P. (2005). Actin-based motility of intracellular pathogens. Curr. Opin. Microbiol. 8, 35-45.
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 35-45
    • Gouin, E.1    Welch, M.D.2    Cossart, P.3
  • 26
    • 0037452070 scopus 로고    scopus 로고
    • Microbial pathogenesis and cytoskeletal function
    • Gruenheid, S., and Finlay, B. B. (2003). Microbial pathogenesis and cytoskeletal function. Nature 422, 775-781.
    • (2003) Nature , vol.422 , pp. 775-781
    • Gruenheid, S.1    Finlay, B.B.2
  • 27
    • 0027534927 scopus 로고
    • Clathrin and HA2 adaptors: Effects of potassium depletion, hypertonic medium, and cytosol acidification
    • Hansen, S. H., Sandvig, K., and van Deurs, B. (1993). Clathrin and HA2 adaptors: effects of potassium depletion, hypertonic medium, and cytosol acidification. J. Cell Biol. 121, 61-72.
    • (1993) J. Cell Biol , vol.121 , pp. 61-72
    • Hansen, S.H.1    Sandvig, K.2    van Deurs, B.3
  • 28
    • 0041327729 scopus 로고    scopus 로고
    • Myosin VI: Two distinct roles in endocytosis
    • Hasson, T. (2003). Myosin VI: two distinct roles in endocytosis. J. Cell Sci. 116, 3453-3461.
    • (2003) J. Cell Sci , vol.116 , pp. 3453-3461
    • Hasson, T.1
  • 29
    • 0027993176 scopus 로고
    • Porcine myosin-VI: Characterization of a new mammalian unconventional myosin
    • Hasson, T., and Mooseker, M. S. (1994). Porcine myosin-VI: characterization of a new mammalian unconventional myosin. J. Cell Biol. 127, 425-440.
    • (1994) J. Cell Biol , vol.127 , pp. 425-440
    • Hasson, T.1    Mooseker, M.S.2
  • 30
    • 0024595608 scopus 로고
    • Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation
    • Heuser, J. E., and Anderson, R. G. (1989). Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation. J. Cell Biol. 108, 389-400.
    • (1989) J. Cell Biol , vol.108 , pp. 389-400
    • Heuser, J.E.1    Anderson, R.G.2
  • 31
    • 0242413645 scopus 로고    scopus 로고
    • Effect of clathrin heavy chain- and α-adaptin-specific small inhibitory RNAs on endocytic accessory proteins and receptor trafficking in HeLa cells
    • Hinrichsen, L., Harborth, J., Andrees, L., Weber, K., and Ungewickell, E. J. (2003). Effect of clathrin heavy chain- and α-adaptin-specific small inhibitory RNAs on endocytic accessory proteins and receptor trafficking in HeLa cells. J. Biol. Chem. 278, 45160-45170.
    • (2003) J. Biol. Chem , vol.278 , pp. 45160-45170
    • Hinrichsen, L.1    Harborth, J.2    Andrees, L.3    Weber, K.4    Ungewickell, E.J.5
  • 32
    • 0027769639 scopus 로고
    • Endocytosis of desmosomal plaques depends on intact actin filaments and leads to a nondegradative compartment
    • Holm, P. K., Hansen, S. H., Sandvig, K., and van Deurs, B. (1993). Endocytosis of desmosomal plaques depends on intact actin filaments and leads to a nondegradative compartment. Eur. J. Cell Biol. 62, 362-371.
    • (1993) Eur. J. Cell Biol , vol.62 , pp. 362-371
    • Holm, P.K.1    Hansen, S.H.2    Sandvig, K.3    van Deurs, B.4
  • 33
    • 2542424590 scopus 로고    scopus 로고
    • Role for actin filament turnover and a myosin II motor in cytoskeleton-driven disassembly of the epithelial apical junctional complex
    • Ivanov, A. I., McCall, I. C., Parkos, C. A., and Nusrat, A. (2004a). Role for actin filament turnover and a myosin II motor in cytoskeleton-driven disassembly of the epithelial apical junctional complex. Mol. Biol. Cell 15, 2639-2651.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2639-2651
    • Ivanov, A.I.1    McCall, I.C.2    Parkos, C.A.3    Nusrat, A.4
  • 34
    • 0347360336 scopus 로고    scopus 로고
    • Endocytosis of epithelial apical junctional proteins by a clathrin-mediated pathway into a unique storage compartment
    • Ivanov, A. I., Nusrat, A., and Parkos, C. A. (2004b). Endocytosis of epithelial apical junctional proteins by a clathrin-mediated pathway into a unique storage compartment. Mol. Biol. Cell 15, 176-188.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 176-188
    • Ivanov, A.I.1    Nusrat, A.2    Parkos, C.A.3
  • 35
    • 20444420130 scopus 로고    scopus 로고
    • Gap junction- and hemichannel- independent actions of connexins
    • Jiang, J. X., and Gu, S. (2005). Gap junction- and hemichannel- independent actions of connexins. Biochim. Biophys. Acta 1711, 208-214.
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 208-214
    • Jiang, J.X.1    Gu, S.2
  • 36
    • 0036133058 scopus 로고    scopus 로고
    • Directed egress of animal viruses promotes cell-to-cell spread
    • Johnson, D. C., and Huber, M. T. (2002). Directed egress of animal viruses promotes cell-to-cell spread. J. Virol. 76, 1-8.
    • (2002) J. Virol , vol.76 , pp. 1-8
    • Johnson, D.C.1    Huber, M.T.2
  • 37
    • 0035085580 scopus 로고    scopus 로고
    • The origin of annular junctions: A mechanism of gap junction internalization
    • Jordan, K., Chodock, R., Hand, A. R., and Laird, D. W. (2001). The origin of annular junctions: a mechanism of gap junction internalization. J. Cell Sci. 114, 763-773.
    • (2001) J. Cell Sci , vol.114 , pp. 763-773
    • Jordan, K.1    Chodock, R.2    Hand, A.R.3    Laird, D.W.4
  • 38
    • 0033012698 scopus 로고    scopus 로고
    • Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells
    • Jordan, K., Solan, J. L., Dominguez, M., Sia, M., Hand, A., Lampe, P. D., and Laird, D. W. (1999). Trafficking, assembly, and function of a connexin43-green fluorescent protein chimera in live mammalian cells. Mol. Biol. Cell 10, 2033-2050.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2033-2050
    • Jordan, K.1    Solan, J.L.2    Dominguez, M.3    Sia, M.4    Hand, A.5    Lampe, P.D.6    Laird, D.W.7
  • 39
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • Kumar, N. M., and Gilula, N. B. (1996). The gap junction communication channel. Cell 84, 381-388.
    • (1996) Cell , vol.84 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 40
    • 1942470517 scopus 로고    scopus 로고
    • The effects of connexin phosphorylation on gap junctional communication
    • Lampe, P. D., and Lau, A. F. (2004). The effects of connexin phosphorylation on gap junctional communication. Int. J. Biochem. Cell Biol. 36, 1171-1186.
    • (2004) Int. J. Biochem. Cell Biol , vol.36 , pp. 1171-1186
    • Lampe, P.D.1    Lau, A.F.2
  • 41
    • 0018570734 scopus 로고
    • Evidence for the participation of actin microfilaments and bristle coats in the internalization of gap junction membrane
    • Larsen, W. J., Tung, H. N., Murray, S. A., and Swenson, C. A. (1979). Evidence for the participation of actin microfilaments and bristle coats in the internalization of gap junction membrane. J. Cell Biol. 83, 576-587.
    • (1979) J. Cell Biol , vol.83 , pp. 576-587
    • Larsen, W.J.1    Tung, H.N.2    Murray, S.A.3    Swenson, C.A.4
  • 42
    • 0036677449 scopus 로고    scopus 로고
    • Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells
    • Lauf, U., Giepmans, B. N., Lopez, P., Braconnot, S., Chen, S. C., and Falk, M. M. (2002). Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc. Natl. Acad. Sci. USA 99, 10446-10451.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10446-10451
    • Lauf, U.1    Giepmans, B.N.2    Lopez, P.3    Braconnot, S.4    Chen, S.C.5    Falk, M.M.6
  • 43
    • 0021723007 scopus 로고
    • Degradation of annular gap junctions of the equine hoof wall
    • Leach, D. H., and Oliphant, L. W. (1984). Degradation of annular gap junctions of the equine hoof wall. Acta Anat. 120, 214-219.
    • (1984) Acta Anat , vol.120 , pp. 214-219
    • Leach, D.H.1    Oliphant, L.W.2
  • 44
    • 30044446000 scopus 로고    scopus 로고
    • Endocytic processing of connexin43 gap junctions: A morphological study
    • Leithe, E., Brech, A., and Rivedal, E. (2006). Endocytic processing of connexin43 gap junctions: a morphological study. Biochem. J. 393, 59-67.
    • (2006) Biochem. J , vol.393 , pp. 59-67
    • Leithe, E.1    Brech, A.2    Rivedal, E.3
  • 45
    • 1842426940 scopus 로고    scopus 로고
    • A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of epithelial cells
    • Matsuda, M., Kubo, A., Furuse, M., and Tsukita, S. (2004). A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of epithelial cells. J. Cell Sci. 117, 1247-1257.
    • (2004) J. Cell Sci , vol.117 , pp. 1247-1257
    • Matsuda, M.1    Kubo, A.2    Furuse, M.3    Tsukita, S.4
  • 46
    • 33749487743 scopus 로고    scopus 로고
    • The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH
    • Mauer, M. E., and Cooper, J. A. (2006). The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH. J. Cell Sci. 119, 4235-4246.
    • (2006) J. Cell Sci , vol.119 , pp. 4235-4246
    • Mauer, M.E.1    Cooper, J.A.2
  • 47
    • 0021957685 scopus 로고
    • Fate of intercellular junctions in isolated adult rat cardiac cells
    • Mazet, F., Wittenberg, B. A., and Spray, D. C. (1985). Fate of intercellular junctions in isolated adult rat cardiac cells. Circ. Res. 56, 195-204.
    • (1985) Circ. Res , vol.56 , pp. 195-204
    • Mazet, F.1    Wittenberg, B.A.2    Spray, D.C.3
  • 48
    • 4544378532 scopus 로고    scopus 로고
    • Mitochondrial fusion intermediates revealed in vitro
    • Meeusen, S., McCaffery, J. M., and Nunnari, J. (2004). Mitochondrial fusion intermediates revealed in vitro. Science 305, 1747-1752.
    • (2004) Science , vol.305 , pp. 1747-1752
    • Meeusen, S.1    McCaffery, J.M.2    Nunnari, J.3
  • 49
    • 3042794632 scopus 로고    scopus 로고
    • Seeing is believing: Imaging actin dynamics at single sites of endocytosis
    • Merrifield, C. J. (2004). Seeing is believing: imaging actin dynamics at single sites of endocytosis. Trends Cell Biol. 14, 352-358.
    • (2004) Trends Cell Biol , vol.14 , pp. 352-358
    • Merrifield, C.J.1
  • 50
    • 0037119952 scopus 로고    scopus 로고
    • Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor
    • Mishra, S. K., Keyel, P. A., Hawryluk, M. J., Agostinelli, N. R., Watkins, S. C., and Traub, L. M. (2002). Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor. EMBO J. 21, 4915-4926.
    • (2002) EMBO J , vol.21 , pp. 4915-4926
    • Mishra, S.K.1    Keyel, P.A.2    Hawryluk, M.J.3    Agostinelli, N.R.4    Watkins, S.C.5    Traub, L.M.6
  • 51
    • 20444404602 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to channel gating
    • Moreno, A. P. (2005). Connexin phosphorylation as a regulatory event linked to channel gating. Biochim. Biophys. Acta 1711, 164-171.
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 164-171
    • Moreno, A.P.1
  • 52
    • 0036242467 scopus 로고    scopus 로고
    • Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton
    • Morris, S. M., Arden, S. D., Roberts, R. C., Kendrick-Jones, J., Cooper, J. A., Luzio, J. P., and Buss, F. (2002). Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton. Traffic 3, 331-341.
    • (2002) Traffic , vol.3 , pp. 331-341
    • Morris, S.M.1    Arden, S.D.2    Roberts, R.C.3    Kendrick-Jones, J.4    Cooper, J.A.5    Luzio, J.P.6    Buss, F.7
  • 53
    • 0035099375 scopus 로고    scopus 로고
    • Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2
    • Morris, S. M., and Cooper, J. A. (2001). Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2. Traffic 2, 111-123.
    • (2001) Traffic , vol.2 , pp. 111-123
    • Morris, S.M.1    Cooper, J.A.2
  • 54
    • 0042232673 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis in AP-2-depleted cells
    • Motley, A., Bright, N. A., Seaman, M. N., and Robinson, M. S. (2003). Clathrin-mediated endocytosis in AP-2-depleted cells. J. Cell Biol. 162, 909-918.
    • (2003) J. Cell Biol , vol.162 , pp. 909-918
    • Motley, A.1    Bright, N.A.2    Seaman, M.N.3    Robinson, M.S.4
  • 55
    • 0031214677 scopus 로고    scopus 로고
    • Relationship of cytoskeletal filaments to annular gap junction expression in human adrenal cortical tumor cells in culture
    • Murray, S. A., Williams, S. Y., Dillard, C. Y., Narayanan, S. K., and McCauley, J. (1997). Relationship of cytoskeletal filaments to annular gap junction expression in human adrenal cortical tumor cells in culture. Exp. Cell Res. 234, 398-404.
    • (1997) Exp. Cell Res , vol.234 , pp. 398-404
    • Murray, S.A.1    Williams, S.Y.2    Dillard, C.Y.3    Narayanan, S.K.4    McCauley, J.5
  • 56
    • 0027252759 scopus 로고
    • Ultrastructural analysis of gap junctions in C6 glioma cells transfected with connexin43 cDNA
    • Naus, C. C., Hearn, S., Zhu, D., Nicholson, B. J., and Shivers, R. R. (1993). Ultrastructural analysis of gap junctions in C6 glioma cells transfected with connexin43 cDNA. Exp. Cell Res. 206, 72-84.
    • (1993) Exp. Cell Res , vol.206 , pp. 72-84
    • Naus, C.C.1    Hearn, S.2    Zhu, D.3    Nicholson, B.J.4    Shivers, R.R.5
  • 57
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans, L., Pèuntener, D., and Helenius, A. (2002). Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296, 535-539.
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Pèuntener, D.2    Helenius, A.3
  • 58
    • 0019155919 scopus 로고
    • Autophagic sequestration of internalized gap junctions in rat liver
    • Pfeifer, U. (1980). Autophagic sequestration of internalized gap junctions in rat liver. Eur. J. Cell Biol. 21, 244-246.
    • (1980) Eur. J. Cell Biol , vol.21 , pp. 244-246
    • Pfeifer, U.1
  • 59
    • 0037343168 scopus 로고    scopus 로고
    • Organization and dynamics of growing microtubule plus ends during early mitosis
    • Piehl, M., and Cassimeris, L. (2003). Organization and dynamics of growing microtubule plus ends during early mitosis. Mol. Biol. Cell 14, 916-925.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 916-925
    • Piehl, M.1    Cassimeris, L.2
  • 61
    • 0042030808 scopus 로고    scopus 로고
    • Lysosomal and proteasomal degradation play distinct roles in the life cycle of Cx43 in gap junctional intercellular communication-deficient and -competent breast tumor cells
    • Qin, H., Shao, Q., Igdoura, S. A., Alaoui-Jamali, M. A., and Laird, D. W. (2003). Lysosomal and proteasomal degradation play distinct roles in the life cycle of Cx43 in gap junctional intercellular communication-deficient and -competent breast tumor cells. J. Biol. Chem. 278, 30005-30014.
    • (2003) J. Biol. Chem , vol.278 , pp. 30005-30014
    • Qin, H.1    Shao, Q.2    Igdoura, S.A.3    Alaoui-Jamali, M.A.4    Laird, D.W.5
  • 62
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual influenza viruses during viral entry
    • Rust, M. J., Lakadamyali, M., Zhang, F., and Zhuang, X. (2004). Assembly of endocytic machinery around individual influenza viruses during viral entry. Nat. Struct. Mol. Biol. 11, 567-573.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3    Zhuang, X.4
  • 65
    • 0037672616 scopus 로고    scopus 로고
    • A tyrosine-based sorting signal is involved in connexin43 stability and gap junction turnover
    • Thomas, M. A., Zosso, N., Scerri, I., Demaurex, N., Chanson, M., and Staub, O. (2003). A tyrosine-based sorting signal is involved in connexin43 stability and gap junction turnover. J. Cell Sci. 116, 2213-2222.
    • (2003) J. Cell Sci , vol.116 , pp. 2213-2222
    • Thomas, M.A.1    Zosso, N.2    Scerri, I.3    Demaurex, N.4    Chanson, M.5    Staub, O.6
  • 66
    • 0242330147 scopus 로고    scopus 로고
    • Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection
    • Traub, L. M. (2003). Sorting it out: AP-2 and alternate clathrin adaptors in endocytic cargo selection. J. Cell Biol. 163, 203-208.
    • (2003) J. Cell Biol , vol.163 , pp. 203-208
    • Traub, L.M.1
  • 67
    • 20544465126 scopus 로고    scopus 로고
    • Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane
    • Traub, L. M. (2005). Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane. Biochim. Biophys. Acta 1744, 415-437.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 415-437
    • Traub, L.M.1
  • 68
    • 0032547744 scopus 로고    scopus 로고
    • Visualization of phosphoinositides that bind pleckstrin homology domains: Calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools
    • Varnai, P., and Balla, T. (1998). Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools. J. Cell Biol. 143, 501-510.
    • (1998) J. Cell Biol , vol.143 , pp. 501-510
    • Varnai, P.1    Balla, T.2
  • 69
    • 26944438047 scopus 로고    scopus 로고
    • Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells
    • Veiga, E., and Cossart, P. (2005). Listeria hijacks the clathrin-dependent endocytic machinery to invade mammalian cells. Nat. Cell Biol. 7, 894-900.
    • (2005) Nat. Cell Biol , vol.7 , pp. 894-900
    • Veiga, E.1    Cossart, P.2
  • 70
    • 12844265252 scopus 로고    scopus 로고
    • A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis
    • Yarar, D., Waterman-Storer, C. M., and Schmid, S. L. (2005). A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis. Mol. Biol. Cell 16, 964-975.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 964-975
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.3


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