메뉴 건너뛰기




Volumn 63, Issue 16, 2006, Pages 1823-1832

The cellular functions of clathrin

Author keywords

Adaptor; Cancer; Clathrin; Dynamin; Endocytosis; Mitosis; TIRFM

Indexed keywords

CLATHRIN;

EID: 33747247518     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5587-0     Document Type: Review
Times cited : (107)

References (101)
  • 2
    • 3142523461 scopus 로고    scopus 로고
    • COP and clathrin-coated vesicle budding: Different pathways, common approaches
    • McMahon, H. T. and Mills, I. G. (2004) COP and clathrin-coated vesicle budding: different pathways, common approaches. Curr. Opin. Cell Biol. 16, 379-391.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 379-391
    • McMahon, H.T.1    Mills, I.G.2
  • 4
    • 0000636835 scopus 로고
    • Yolk protein uptake in the oocyte of the mosquito Aedes aegypti. L.
    • Roth, T. F. and Porter, K. R. (1964) Yolk protein uptake in the oocyte of the mosquito Aedes aegypti. L. J. Cell Biol. 20, 313-332.
    • (1964) J. Cell Biol. , vol.20 , pp. 313-332
    • Roth, T.F.1    Porter, K.R.2
  • 5
    • 0014541501 scopus 로고
    • The 'vesicle in a basket'. a morphological study of the coated vesicle isolated from the nerve endings of the guinea pig brain, with special reference to the mechanism of membrane movements
    • Kanaseki, T. and Kadota, K. (1969) The 'vesicle in a basket'. A morphological study of the coated vesicle isolated from the nerve endings of the guinea pig brain, with special reference to the mechanism of membrane movements. J. Cell Biol. 42, 202-220.
    • (1969) J. Cell Biol. , vol.42 , pp. 202-220
    • Kanaseki, T.1    Kadota, K.2
  • 7
    • 0016834909 scopus 로고
    • Coated vesicles from pig brain: Purification and biochemical characterization
    • Pearse, B. M. (1975) Coated vesicles from pig brain: purification and biochemical characterization. J. Mol. Biol. 97, 93-98.
    • (1975) J. Mol. Biol. , vol.97 , pp. 93-98
    • Pearse, B.M.1
  • 8
    • 0006496113 scopus 로고
    • Clathrin: A unique protein associated with intracellular transfer of membrane by coated vesicles
    • USA
    • Pearse, B. M. (1976) Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles. Proc. Natl. Acad. Sci. USA 73, 1255-1259.
    • (1976) Proc. Natl. Acad. Sci. , vol.73 , pp. 1255-1259
    • Pearse, B.M.1
  • 9
    • 0019890534 scopus 로고
    • Assembly units of clathrin coats
    • Ungewickell, E. and Branton, D. (1981) Assembly units of clathrin coats. Nature 289, 420-422.
    • (1981) Nature , vol.289 , pp. 420-422
    • Ungewickell, E.1    Branton, D.2
  • 10
    • 0019435922 scopus 로고
    • Protein organization in clathrin trimers
    • Kirchhausen, T. and Harrison, S. C. (1981) Protein organization in clathrin trimers. Cell 23, 755-761.
    • (1981) Cell , vol.23 , pp. 755-761
    • Kirchhausen, T.1    Harrison, S.C.2
  • 13
    • 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
  • 14
    • 1842556279 scopus 로고    scopus 로고
    • Adaptable adaptors for coated vesicles
    • Robinson, M. S. (2004) Adaptable adaptors for coated vesicles. Trends Cell Biol. 14, 167-174.
    • (2004) Trends Cell Biol. , vol.14 , pp. 167-174
    • Robinson, M.S.1
  • 15
  • 16
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J. S. and Traub, L. M. (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72, 395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 17
    • 3042806469 scopus 로고    scopus 로고
    • Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration
    • Towler, M. C., Gleeson, P. A., Hoshino, S., Rahkila, P., Manalo, V., Ohkoshi, N., Ordahl, C., Parton, R. G. and Brodsky, F. M. (2004) Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration. Mol. Biol. Cell 15, 3181-3195.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3181-3195
    • Towler, M.C.1    Gleeson, P.A.2    Hoshino, S.3    Rahkila, P.4    Manalo, V.5    Ohkoshi, N.6    Ordahl, C.7    Parton, R.G.8    Brodsky, F.M.9
  • 18
    • 18944395674 scopus 로고    scopus 로고
    • Clathrin heavy and light chain isoforms originated by independent mechanisms of gene duplication during chordate evolution
    • USA
    • Wakeham, D. E., Abi-Rached, L., Towler, M. C., Wilbur, J. D., Parham, P. and Brodsky, F. M. (2005) Clathrin heavy and light chain isoforms originated by independent mechanisms of gene duplication during chordate evolution. Proc. Natl. Acad. Sci. USA 102, 7209-7214.
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 7209-7214
    • Wakeham, D.E.1    Abi-Rached, L.2    Towler, M.C.3    Wilbur, J.D.4    Parham, P.5    Brodsky, F.M.6
  • 20
    • 0022780984 scopus 로고
    • Location of the 100 kd-50 kd accessory proteins in clathrin coats
    • Vigers, G. P., Crowther, R. A. and Pearse, B. M. (1986) Location of the 100 kd-50 kd accessory proteins in clathrin coats. EMBO J. 5, 2079-2085.
    • (1986) EMBO J. , vol.5 , pp. 2079-2085
    • Vigers, G.P.1    Crowther, R.A.2    Pearse, B.M.3
  • 21
    • 0022684837 scopus 로고
    • Three-dimensional structure of clathrin cages in ice
    • Vigers, G. P., Crowther, R. A. and Pearse, B. M. (1986) Three-dimensional structure of clathrin cages in ice. EMBO J. 5, 529-534.
    • (1986) EMBO J. , vol.5 , pp. 529-534
    • Vigers, G.P.1    Crowther, R.A.2    Pearse, B.M.3
  • 23
    • 0032167614 scopus 로고    scopus 로고
    • Clathrin coats at 21 A resolution: A cellular assembly designed to recycle multiple membrane receptors
    • Smith, C. J., Grigorieff, N. and Pearse, B. M. (1998) Clathrin coats at 21 A resolution: a cellular assembly designed to recycle multiple membrane receptors. EMBO J. 17, 4943-4953.
    • (1998) EMBO J. , vol.17 , pp. 4943-4953
    • Smith, C.J.1    Grigorieff, N.2    Pearse, B.M.3
  • 24
    • 0033153279 scopus 로고    scopus 로고
    • Functional organization of clathrin in coats: Combining electron cryomicroscopy and X-ray crystallography
    • Musacchio, A., Smith, C. J., Roseman, A. M., Harrison, S. C., Kirchhausen, T. and Pearse, B. M. (1999) Functional organization of clathrin in coats: combining electron cryomicroscopy and X-ray crystallography. Mol. Cell 3, 761-770.
    • (1999) Mol. Cell , vol.3 , pp. 761-770
    • Musacchio, A.1    Smith, C.J.2    Roseman, A.M.3    Harrison, S.C.4    Kirchhausen, T.5    Pearse, B.M.6
  • 25
    • 0032514995 scopus 로고    scopus 로고
    • Atomic structure of clathrin: A beta propeller terminal domain joins an alpha zigzag linker
    • ter Haar, E., Musacchio, A., Harrison, S. C. and Kirchhausen, T. (1998) Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker. Cell 95, 563-573.
    • (1998) Cell , vol.95 , pp. 563-573
    • Ter Haar, E.1    Musacchio, A.2    Harrison, S.C.3    Kirchhausen, T.4
  • 26
    • 0033967923 scopus 로고    scopus 로고
    • Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin
    • USA
    • ter Haar, E., Harrison, S. C. and Kirchhausen, T. (2000) Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin. Proc. Natl. Acad. Sci. USA 97, 1096-1100.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 1096-1100
    • Ter Haar, E.1    Harrison, S.C.2    Kirchhausen, T.3
  • 27
    • 1442335990 scopus 로고    scopus 로고
    • Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller
    • Miele, A. E., Watson, P. J., Evans, P. R., Traub, L. M. and Owen, D. J. (2004) Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller. Nat. Struct. Mol. Biol. 11, 242-248.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 242-248
    • Miele, A.E.1    Watson, P.J.2    Evans, P.R.3    Traub, L.M.4    Owen, D.J.5
  • 30
    • 10344227184 scopus 로고    scopus 로고
    • Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating
    • Fotin, A., Cheng, Y., Grigorieff, N., Walz, T., Harrison, S. C. and Kirchhausen, T. (2004) Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating. Nature 432, 649-653.
    • (2004) Nature , vol.432 , pp. 649-653
    • Fotin, A.1    Cheng, Y.2    Grigorieff, N.3    Walz, T.4    Harrison, S.C.5    Kirchhausen, T.6
  • 31
    • 15844419751 scopus 로고    scopus 로고
    • New faces of the familiar clathrin lattice
    • Wilbur, J. D., Hwang, P. K. and Brodsky, F. M. (2005) New faces of the familiar clathrin lattice. Traffic 6, 346-350.
    • (2005) Traffic , vol.6 , pp. 346-350
    • Wilbur, J.D.1    Hwang, P.K.2    Brodsky, F.M.3
  • 34
  • 35
    • 0021092725 scopus 로고
    • Clathrin heavy chain, light chain interactions
    • Winkler, F. K. and Stanley, K. K. (1983) Clathrin heavy chain, light chain interactions. EMBO J. 2, 1393-1400.
    • (1983) EMBO J. , vol.2 , pp. 1393-1400
    • Winkler, F.K.1    Stanley, K.K.2
  • 36
    • 18744400775 scopus 로고    scopus 로고
    • Clathrin light and heavy chain interface: Alpha-helix binding superhelix loops via critical tryptophans
    • Chen, C. Y., Reese, M. L., Hwang, P. K., Ota, N., Agard, D. and Brodsky, F. M. (2002) Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans. EMBO J. 21, 6072-6082.
    • (2002) EMBO J. , vol.21 , pp. 6072-6082
    • Chen, C.Y.1    Reese, M.L.2    Hwang, P.K.3    Ota, N.4    Agard, D.5    Brodsky, F.M.6
  • 37
    • 0025254061 scopus 로고
    • Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3
    • Scarmato, P. and Kirchhausen, T. (1990) Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3. J. Biol. Chem. 265, 3661-3668.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3661-3668
    • Scarmato, P.1    Kirchhausen, T.2
  • 38
  • 39
    • 0021092754 scopus 로고
    • Biochemical and immunological studies on clathrin light chains and their binding sites on clathrin triskelions
    • Ungewickell, E. (1983) Biochemical and immunological studies on clathrin light chains and their binding sites on clathrin triskelions. EMBO J. 2, 1401-1408.
    • (1983) EMBO J. , vol.2 , pp. 1401-1408
    • Ungewickell, E.1
  • 40
    • 0027195836 scopus 로고
    • Immunoelectron microscopic evidence for the extended conformation of light chains in clathrin trimers
    • Kirchhausen, T. and Toyoda, T. (1993) Immunoelectron microscopic evidence for the extended conformation of light chains in clathrin trimers. J. Biol. Chem. 268, 10268-10273.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10268-10273
    • Kirchhausen, T.1    Toyoda, T.2
  • 41
    • 0026503136 scopus 로고
    • Folding and trimerization of clathrin subunits at the triskelion hub
    • Nathke, I. S., Heuser, J., Lupas, A., Stock, J., Turck, C. W. and Brodsky, F. M. (1992) Folding and trimerization of clathrin subunits at the triskelion hub. Cell 68, 899-910.
    • (1992) Cell , vol.68 , pp. 899-910
    • Nathke, I.S.1    Heuser, J.2    Lupas, A.3    Stock, J.4    Turck, C.W.5    Brodsky, F.M.6
  • 43
    • 0032473362 scopus 로고    scopus 로고
    • Clathrin self-assembly is regulated by three light-chain residues controlling the formation of critical salt bridges
    • Ybe, J. A., Greene, B., Liu, S. H., Pley, U., Parham, P. and Brodsky, F. M. (1998) Clathrin self-assembly is regulated by three light-chain residues controlling the formation of critical salt bridges. EMBO J. 17, 1297-1303.
    • (1998) EMBO J. , vol.17 , pp. 1297-1303
    • Ybe, J.A.1    Greene, B.2    Liu, S.H.3    Pley, U.4    Parham, P.5    Brodsky, F.M.6
  • 44
    • 0033754656 scopus 로고    scopus 로고
    • Complete reconstitution of clathrin basket formation with recombinant protein fragments: Adaptor control of clathrin self-assembly
    • Greene, B., Liu, S. H., Wilde, A. and Brodsky, F. M. (2000) Complete reconstitution of clathrin basket formation with recombinant protein fragments: adaptor control of clathrin self-assembly. Traffic 1, 69-75.
    • (2000) Traffic , vol.1 , pp. 69-75
    • Greene, B.1    Liu, S.H.2    Wilde, A.3    Brodsky, F.M.4
  • 45
    • 20444422844 scopus 로고    scopus 로고
    • Clathrin-dependent and clathrin-independent retrieval of synaptic vesicles in retinal bipolar cells
    • Jockusch, W. J., Praefcke, G. J., McMahon, H. T. and Lagnado, L. (2005) Clathrin-dependent and clathrin-independent retrieval of synaptic vesicles in retinal bipolar cells. Neuron 46, 869-878.
    • (2005) Neuron , vol.46 , pp. 869-878
    • Jockusch, W.J.1    Praefcke, G.J.2    McMahon, H.T.3    Lagnado, L.4
  • 46
    • 0346242691 scopus 로고    scopus 로고
    • Endocytosis at the synaptic terminal
    • Royle, S. J. and Lagnado, L. (2003) Endocytosis at the synaptic terminal. J. Physiol. 553, 345-355.
    • (2003) J. Physiol. , vol.553 , pp. 345-355
    • Royle, S.J.1    Lagnado, L.2
  • 47
    • 0023734573 scopus 로고
    • Structure of human clathrin light chains. Conservation of light chain polymorphism in three mammalian species
    • Jackson, A. P. and Parham, P. (1988) Structure of human clathrin light chains. Conservation of light chain polymorphism in three mammalian species. J. Biol. Chem. 263, 16688-16695.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16688-16695
    • Jackson, A.P.1    Parham, P.2
  • 48
    • 0023127462 scopus 로고
    • Clathrin light chains contain brain-specific insertion sequences and a region of homology with intermediate filaments
    • Jackson, A. P., Seow, H. F., Holmes, N., Drickamer, K. and Parham, P. (1987) Clathrin light chains contain brain-specific insertion sequences and a region of homology with intermediate filaments. Nature 326, 154-159.
    • (1987) Nature , vol.326 , pp. 154-159
    • Jackson, A.P.1    Seow, H.F.2    Holmes, N.3    Drickamer, K.4    Parham, P.5
  • 49
    • 0028906643 scopus 로고
    • The interaction of calmodulin with clathrin-coated vesicles, triskelions, and light chains. Localization of a binding site
    • Pley, U. M., Hill, B. L., Alibert, C., Brodsky, F. M. and Parham, P. (1995) The interaction of calmodulin with clathrin-coated vesicles, triskelions, and light chains. Localization of a binding site. J. Biol. Chem. 270, 2395-2402.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2395-2402
    • Pley, U.M.1    Hill, B.L.2    Alibert, C.3    Brodsky, F.M.4    Parham, P.5
  • 51
    • 27644592393 scopus 로고    scopus 로고
    • Dynamics of endocytic vesicle creation
    • Perrais, D. and Merrifield, C. J. (2005) Dynamics of endocytic vesicle creation. Dev. Cell 9, 581-592.
    • (2005) Dev. Cell , vol.9 , pp. 581-592
    • Perrais, D.1    Merrifield, C.J.2
  • 52
    • 2442640306 scopus 로고    scopus 로고
    • Understanding living clathrin-coated pits
    • Rappoport, J. Z., Simon, S. M. and Bemnerah, A. (2004) Understanding living clathrin-coated pits. Traffic 5, 327-337.
    • (2004) Traffic , vol.5 , pp. 327-337
    • Rappoport, J.Z.1    Simon, S.M.2    Bemnerah, A.3
  • 53
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield, C. J., Feldman, M. E., Wan, L. and Almers, W. (2002) Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat. Cell Biol. 4, 691-698.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 55
    • 0022619530 scopus 로고
    • Immunofluorescent localization of 100K coated vesicle proteins
    • Robinson, M. S. and Pearse, B. M. (1986) Immunofluorescent localization of 100K coated vesicle proteins. J. Cell Biol. 102, 48-54.
    • (1986) J. Cell Biol. , vol.102 , pp. 48-54
    • Robinson, M.S.1    Pearse, B.M.2
  • 58
    • 24944525034 scopus 로고    scopus 로고
    • Differential control of clathrin subunit dynamics measured with EW-FRAP Microscopy
    • Loerke, D., Wienisch, M., Kochubey, O. and Klingauf, J. (2005) Differential control of clathrin subunit dynamics measured with EW-FRAP Microscopy. Traffic 6, 918-929.
    • (2005) Traffic , vol.6 , pp. 918-929
    • Loerke, D.1    Wienisch, M.2    Kochubey, O.3    Klingauf, J.4
  • 59
    • 0034760118 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • Axelrod, D. (2001) Total internal reflection fluorescence microscopy in cell biology. Traffic 2, 764-774.
    • (2001) Traffic , vol.2 , pp. 764-774
    • Axelrod, D.1
  • 60
    • 19344375254 scopus 로고    scopus 로고
    • Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells
    • Merrifield, C. J., Perrais, D. and Zenisek, D. (2005) Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells. Cell 121, 593-606.
    • (2005) Cell , vol.121 , pp. 593-606
    • Merrifield, C.J.1    Perrais, D.2    Zenisek, D.3
  • 61
    • 0025917331 scopus 로고
    • Stage-specific assays for coated pit formation and coated vesicle budding in vitro
    • Schmid, S. L. and Smythe, E. (1991) Stage-specific assays for coated pit formation and coated vesicle budding in vitro. J. Cell Biol. 114, 869-880.
    • (1991) J. Cell Biol. , vol.114 , pp. 869-880
    • Schmid, S.L.1    Smythe, E.2
  • 62
    • 0023552995 scopus 로고
    • Deep-etch visualization of 27S clathrin: A tetrahedral tetramer
    • Heuser, J. E., Keen, J. H., Amende, L. M., Lippoldt, R. E. and Prasad, K. (1987) Deep-etch visualization of 27S clathrin: a tetrahedral tetramer. J. Cell Biol. 105, 1999-2009.
    • (1987) J. Cell Biol. , vol.105 , pp. 1999-2009
    • Heuser, J.E.1    Keen, J.H.2    Amende, L.M.3    Lippoldt, R.E.4    Prasad, K.5
  • 63
    • 0022344231 scopus 로고
    • A test of clathrin function in protein secretion and cell growth
    • Payne, G. S. and Schekman, R. (1985) A test of clathrin function in protein secretion and cell growth. Science 230, 1009-1014.
    • (1985) Science , vol.230 , pp. 1009-1014
    • Payne, G.S.1    Schekman, R.2
  • 64
    • 0023663065 scopus 로고
    • Clathrin requirement for normal growth of yeast
    • Lemmon, S. K. and Jones, E. W. (1987) Clathrin requirement for normal growth of yeast. Science 238, 504-509.
    • (1987) Science , vol.238 , pp. 504-509
    • Lemmon, S.K.1    Jones, E.W.2
  • 65
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin- and actin-mediated endocytosis machinery
    • Kaksonen, M., Toret, C. P. and Drubin, D. G. (2005) A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell 123, 305-320.
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 66
    • 28444456720 scopus 로고    scopus 로고
    • Cell biology: Protein choreography
    • Duncan, M. C. and Payne, G. S. (2005) Cell biology: protein choreography. Nature 438, 571-573.
    • (2005) Nature , vol.438 , pp. 571-573
    • Duncan, M.C.1    Payne, G.S.2
  • 67
    • 0026671869 scopus 로고
    • Clathrin heavy chain is required for pinocytosis, the presence of large vacuoles, and development in Dictyostelium
    • O'Halloran, T. J. and Anderson, R. G. (1992) Clathrin heavy chain is required for pinocytosis, the presence of large vacuoles, and development in Dictyostelium. J. Cell Biol. 118, 1371-1377.
    • (1992) J. Cell Biol. , vol.118 , pp. 1371-1377
    • O'Halloran, T.J.1    Anderson, R.G.2
  • 68
    • 0033972607 scopus 로고    scopus 로고
    • Clathrin plays a novel role in the regulation of cell polarity, pseudopod formation, uropod stability and motility in Dictyostelium
    • Wessels, D., Reynolds, J., Johnson, O., Voss, E., Burns, R., Daniels, K., Garrad, E., O'Halloran, T. J. and Soll, D. R. (2000) Clathrin plays a novel role in the regulation of cell polarity, pseudopod formation, uropod stability and motility in Dictyostelium. J. Cell Sci. 113, 21-36.
    • (2000) J. Cell Sci. , vol.113 , pp. 21-36
    • Wessels, D.1    Reynolds, J.2    Johnson, O.3    Voss, E.4    Burns, R.5    Daniels, K.6    Garrad, E.7    O'Halloran, T.J.8    Soll, D.R.9
  • 69
    • 0030825334 scopus 로고    scopus 로고
    • A novel role for clathrin in cytokinesis
    • USA
    • Niswonger, M. L. and O'Halloran, T. J. (1997) A novel role for clathrin in cytokinesis. Proc. Natl. Acad. Sci. USA 94, 8575-8578.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 8575-8578
    • Niswonger, M.L.1    O'Halloran, T.J.2
  • 70
    • 0035114361 scopus 로고    scopus 로고
    • Cytokinesis failure in clathrin-minus cells is caused by cleavage furrow instability
    • Gerald, N. J., Damer, C. K., O'Halloran, T. J. and De Lozanne, A. (2001) Cytokinesis failure in clathrin-minus cells is caused by cleavage furrow instability. Cell Motil. Cytoskeleton 48, 213-223.
    • (2001) Cell Motil. Cytoskeleton , vol.48 , pp. 213-223
    • Gerald, N.J.1    Damer, C.K.2    O'Halloran, T.J.3    De Lozanne, A.4
  • 71
    • 0032734242 scopus 로고    scopus 로고
    • Receptor-mediated endocytosis in the Caenorhabditis elegans oocyte
    • Grant, B. and Hirsh, D. (1999) Receptor-mediated endocytosis in the Caenorhabditis elegans oocyte. Mol. Biol. Cell 10, 4311-4326.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4311-4326
    • Grant, B.1    Hirsh, D.2
  • 72
    • 0141530903 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis is essential in Trypanosoma brucei
    • Allen, C. L., Goulding, D. and Field, M. C. (2003) Clathrin-mediated endocytosis is essential in Trypanosoma brucei. EMBO J. 22, 4991-5002.
    • (2003) EMBO J. , vol.22 , pp. 4991-5002
    • Allen, C.L.1    Goulding, D.2    Field, M.C.3
  • 73
    • 0027257424 scopus 로고
    • The Drosophila clathrin heavy chain gene: Clathrin function is essential in a multicellular organism
    • Bazinet, C., Katzen, A. L., Morgan, M., Mahowald, A. P. and Lemmon, S. K. (1993) The Drosophila clathrin heavy chain gene: clathrin function is essential in a multicellular organism. Genetics 134, 1119-1134.
    • (1993) Genetics , vol.134 , pp. 1119-1134
    • Bazinet, C.1    Katzen, A.L.2    Morgan, M.3    Mahowald, A.P.4    Lemmon, S.K.5
  • 74
    • 0034657033 scopus 로고    scopus 로고
    • mu1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors
    • Meyer, C., Zizioli, D., Lausmann, S., Eskelinen, E. L., Hamann, J., Saftig, P., von Figura, K. and Schu, P. (2000) mu1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J. 19, 2193-2203.
    • (2000) EMBO J. , vol.19 , pp. 2193-2203
    • Meyer, C.1    Zizioli, D.2    Lausmann, S.3    Eskelinen, E.L.4    Hamann, J.5    Saftig, P.6    Von Figura, K.7    Schu, P.8
  • 76
    • 0037200068 scopus 로고    scopus 로고
    • Controlled elimination of clathrin heavy-chain expression in DT40 lymphocytes
    • Wettey, F. R., Hawkins, S. F., Stewart, A., Luzio, J. P., Howard, J. C. and Jackson, A. P. (2002) Controlled elimination of clathrin heavy-chain expression in DT40 lymphocytes. Science 297, 1521-1525.
    • (2002) Science , vol.297 , pp. 1521-1525
    • Wettey, F.R.1    Hawkins, S.F.2    Stewart, A.3    Luzio, J.P.4    Howard, J.C.5    Jackson, A.P.6
  • 77
    • 17844394685 scopus 로고    scopus 로고
    • Clathrin is required for the function of the mitotic spindle
    • Royle, S. J., Bright, N. A. and Lagnado, L. (2005) Clathrin is required for the function of the mitotic spindle. Nature 434, 1152-1157.
    • (2005) Nature , vol.434 , pp. 1152-1157
    • Royle, S.J.1    Bright, N.A.2    Lagnado, L.3
  • 78
    • 0242413645 scopus 로고    scopus 로고
    • Effect of clathrin heavy chain- and alpha-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 alpha-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
  • 79
    • 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
  • 80
    • 0027183419 scopus 로고
    • Membrane partitioning during cell division
    • Warren, G. (1993) Membrane partitioning during cell division. Annu. Rev. Biochem. 62, 323-348.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 323-348
    • Warren, G.1
  • 81
    • 0022273282 scopus 로고
    • Changes in the distribution of membranous organelles during mouse early development
    • Maro, B., Johnson, M. H., Pickering, S. J. and Louvard, D. (1985) Changes in the distribution of membranous organelles during mouse early development. J. Embryol. Exp. Morphol. 90, 287-309.
    • (1985) J. Embryol. Exp. Morphol. , vol.90 , pp. 287-309
    • Maro, B.1    Johnson, M.H.2    Pickering, S.J.3    Louvard, D.4
  • 84
    • 0035807883 scopus 로고    scopus 로고
    • Analysis of mitotic microtubule-associated proteins using mass spectrometry identifies astrin, a spindle-associated protein
    • USA
    • Mack, G. J. and Compton, D. A. (2001) Analysis of mitotic microtubule-associated proteins using mass spectrometry identifies astrin, a spindle-associated protein. Proc. Natl. Acad. Sci. USA 98, 14434-14439.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 14434-14439
    • Mack, G.J.1    Compton, D.A.2
  • 85
    • 0033782853 scopus 로고    scopus 로고
    • Spindle assembly in animal cells
    • Compton, D. A. (2000) Spindle assembly in animal cells. Annu. Rev. Biochem. 69, 95-114.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 95-114
    • Compton, D.A.1
  • 86
    • 0014782523 scopus 로고
    • Intermicrotubule bridges in mitotic spindle apparatus
    • Hepler, P. K., McIntosh, J. R. and Cleland, S. (1970) Intermicrotubule bridges in mitotic spindle apparatus. J. Cell Biol. 45, 438-444.
    • (1970) J. Cell Biol. , vol.45 , pp. 438-444
    • Hepler, P.K.1    McIntosh, J.R.2    Cleland, S.3
  • 87
    • 0003150825 scopus 로고
    • Surface specializations of absorbing cells
    • Fawcett, D. W. (1965) surface specializations of absorbing cells. J. Histochem. Cytochem. 13, 75-91.
    • (1965) J. Histochem. Cytochem. , vol.13 , pp. 75-91
    • Fawcett, D.W.1
  • 88
    • 0023464741 scopus 로고
    • Coated pits in interphase and mitotic A431 cells
    • Pypaert, M., Lucocq, J. M. and Warren, G. (1987) Coated pits in interphase and mitotic A431 cells. Eur. J. Cell Biol. 45, 23-29.
    • (1987) Eur. J. Cell Biol. , vol.45 , pp. 23-29
    • Pypaert, M.1    Lucocq, J.M.2    Warren, G.3
  • 89
    • 0026063260 scopus 로고
    • Mitotic cytosol inhibits invagination of coated pits in broken mitotic cells
    • Pypaert, M., Mundy, D., Souter, E., Labbe, J. C. and Warren, G. (1991) Mitotic cytosol inhibits invagination of coated pits in broken mitotic cells. J. Cell Biol. 114, 1159-1166.
    • (1991) J. Cell Biol. , vol.114 , pp. 1159-1166
    • Pypaert, M.1    Mundy, D.2    Souter, E.3    Labbe, J.C.4    Warren, G.5
  • 91
    • 0141545024 scopus 로고    scopus 로고
    • Nup358 integrates nuclear envelope breakdown with kinetochore assembly
    • Salina, D., Enarson, P., Rattner, J. B. and Burke, B. (2003) Nup358 integrates nuclear envelope breakdown with kinetochore assembly. J. Cell Biol. 162, 991-1001.
    • (2003) J. Cell Biol. , vol.162 , pp. 991-1001
    • Salina, D.1    Enarson, P.2    Rattner, J.B.3    Burke, B.4
  • 92
    • 0037128207 scopus 로고    scopus 로고
    • SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles
    • Joseph, J., Tan, S. H., Karpova, T. S., McNally, J. G. and Dasso, M. (2002) SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles. J. Cell Biol. 156, 595-602.
    • (2002) J. Cell Biol. , vol.156 , pp. 595-602
    • Joseph, J.1    Tan, S.H.2    Karpova, T.S.3    McNally, J.G.4    Dasso, M.5
  • 93
    • 0346668247 scopus 로고    scopus 로고
    • The large GTPase dynamin associates with the spindle midzone and is required for cytokinesis
    • Thompson, H. M., Skop, A. R., Euteneuer, U., Meyer, B. J. and McNiven, M. A. (2002) The large GTPase dynamin associates with the spindle midzone and is required for cytokinesis. Curr. Biol. 12, 2111-2117.
    • (2002) Curr. Biol. , vol.12 , pp. 2111-2117
    • Thompson, H.M.1    Skop, A.R.2    Euteneuer, U.3    Meyer, B.J.4    McNiven, M.A.5
  • 94
    • 2342574188 scopus 로고    scopus 로고
    • Dynamin 2 binds gamma-tubulin and participates in centrosome cohesion
    • Thompson, H. M., Cao, H., Chen, J., Euteneuer, U. and McNiven, M. A. (2004) Dynamin 2 binds gamma-tubulin and participates in centrosome cohesion. Nat. Cell Biol. 6, 335-342.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 335-342
    • Thompson, H.M.1    Cao, H.2    Chen, J.3    Euteneuer, U.4    McNiven, M.A.5
  • 95
    • 9244263076 scopus 로고    scopus 로고
    • Aneuploidy and cancer
    • Rajagopalan, H. and Lengauer, C. (2004) Aneuploidy and cancer. Nature 432, 338-341.
    • (2004) Nature , vol.432 , pp. 338-341
    • Rajagopalan, H.1    Lengauer, C.2
  • 96
    • 0041353435 scopus 로고    scopus 로고
    • A novel CLTC-TFE3 gene fusion in pediatric renal adenocarcinoma with t(X;17)(p11.2;q23)
    • Argani, P., Lui, M. Y., Couturier, J., Bouvier, R., Fournet, J. C. and Ladanyi, M. (2003) A novel CLTC-TFE3 gene fusion in pediatric renal adenocarcinoma with t(X;17)(p11.2;q23). Oncogene 22, 5374-5378.
    • (2003) Oncogene , vol.22 , pp. 5374-5378
    • Argani, P.1    Lui, M.Y.2    Couturier, J.3    Bouvier, R.4    Fournet, J.C.5    Ladanyi, M.6
  • 100
    • 0034658434 scopus 로고    scopus 로고
    • Further demonstration of the diversity of chromosomal changes involving 2p23 in ALK-positive lymphoma: 2 cases expressing ALK kinase fused to CLTCL (clathrin chain polypeptide-like)
    • Touriol, C., Greenland, C., Lamant, L., Pulford, K., Bernard, F., Rousset, T., Mason, D. Y. and Delsol, G. (2000) Further demonstration of the diversity of chromosomal changes involving 2p23 in ALK-positive lymphoma: 2 cases expressing ALK kinase fused to CLTCL (clathrin chain polypeptide-like). Blood 95, 3204-3207.
    • (2000) Blood , vol.95 , pp. 3204-3207
    • Touriol, C.1    Greenland, C.2    Lamant, L.3    Pulford, K.4    Bernard, F.5    Rousset, T.6    Mason, D.Y.7    Delsol, G.8
  • 101
    • 2342635959 scopus 로고    scopus 로고
    • Anaplastic lymphoma kinase proteins in growth control and cancer
    • Pulford, K., Morris, S. W. and Turturro, F. (2004) Anaplastic lymphoma kinase proteins in growth control and cancer. J. Cell Physiol. 199, 330-358.
    • (2004) J. Cell Physiol. , vol.199 , pp. 330-358
    • Pulford, K.1    Morris, S.W.2    Turturro, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.