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Volumn 78, Issue 3, 2000, Pages 1183-1194

Rigidity of triskelion arms and clathrin nets

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN;

EID: 0034007578     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76676-8     Document Type: Article
Times cited : (37)

References (53)
  • 1
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson, R. G. W. 1998. The caveolae membrane system. Annu. Rev. Biochem. 67:199-225.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 2
    • 0024232861 scopus 로고
    • Living with clathrin: Its role in intracellular membrane traffic
    • Brodsky, F. M. 1988. Living with clathrin: its role in intracellular membrane traffic. Science. 242:1396-1402.
    • (1988) Science , vol.242 , pp. 1396-1402
    • Brodsky, F.M.1
  • 3
    • 0025847321 scopus 로고
    • Clathrin light chains: Arrays of protein motifs that regulate coated-vesicle dynamics
    • Brodsky, F. M., B. L. Hill, S. L. Actin, L. Nathke, D. H. Wong, S. Ponnambalam, and P. Parham. 1991. Clathrin light chains: arrays of protein motifs that regulate coated-vesicle dynamics. TIBS. 16:208-213.
    • (1991) TIBS , vol.16 , pp. 208-213
    • Brodsky, F.M.1    Hill, B.L.2    Actin, S.L.3    Nathke, L.4    Wong, D.H.5    Ponnambalam, S.6    Parham, P.7
  • 4
    • 0019813567 scopus 로고
    • Assembly and packing of clathrin into coats
    • Crowther, R. A., and B. M. F. Pearse. 1981. Assembly and packing of clathrin into coats. J. Cell. Biol. 91:790-797.
    • (1981) J. Cell. Biol. , vol.91 , pp. 790-797
    • Crowther, R.A.1    Pearse, B.M.F.2
  • 6
    • 0017229778 scopus 로고
    • Electron microscopy of myosin molecules from muscle and non-muscle sources
    • Elliott, A., G. Offer, and K. Burridge. 1976. Electron microscopy of myosin molecules from muscle and non-muscle sources. Proc. R. Soc., Ser. B. 193:43-53.
    • (1976) Proc. R. Soc., Ser. B. , vol.193 , pp. 43-53
    • Elliott, A.1    Offer, G.2    Burridge, K.3
  • 7
    • 0023785596 scopus 로고
    • Cellular mechanics as an indicator of cytoskeletal structure and function
    • Elson, E. L. 1988. Cellular mechanics as an indicator of cytoskeletal structure and function. Annu. Rev. Biophys. Biophys. Chem. 17: 397-430.
    • (1988) Annu. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 397-430
    • Elson, E.L.1
  • 8
    • 0020957075 scopus 로고
    • Bending elastic modulus of red blood cell membrane derived from buckling instability in micropipet aspiration tests
    • Evans, E. 1983. Bending elastic modulus of red blood cell membrane derived from buckling instability in micropipet aspiration tests. Biophys. J. 43:27-30.
    • (1983) Biophys. J. , vol.43 , pp. 27-30
    • Evans, E.1
  • 9
    • 0025663356 scopus 로고
    • Time-dependent alterations in the deformability of human neutrophils in response to chemotactic activation
    • Frank, R. S. 1990. Time-dependent alterations in the deformability of human neutrophils in response to chemotactic activation. Blood. 76: 2606-2612.
    • (1990) Blood , vol.76 , pp. 2606-2612
    • Frank, R.S.1
  • 10
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • Gittes, F., B. Mickey, J. Nettleton, and J. Howard. 1993. Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J. Cell Biol. 120:923-934.
    • (1993) J. Cell Biol. , vol.120 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 11
    • 0023058994 scopus 로고
    • Visualization of bent helix in kinetoplast DNA by electron microscopy
    • Griffith, J., M. Bleyman, C. A. Rauch, P. A. Kitchin, and P. T. Englund. 1986. Visualization of bent helix in kinetoplast DNA by electron microscopy. Cell. 46:717-724.
    • (1986) Cell , vol.46 , pp. 717-724
    • Griffith, J.1    Bleyman, M.2    Rauch, C.A.3    Kitchin, P.A.4    Englund, P.T.5
  • 12
    • 84943997802 scopus 로고
    • Elastic properties of lipid bilayers: Theory and possible experiments
    • Helfrich, W. 1973. Elastic properties of lipid bilayers: theory and possible experiments. Z. Naturforsch. 28c:693-703.
    • (1973) Z. Naturforsch. , vol.28 C , pp. 693-703
    • Helfrich, W.1
  • 13
    • 0024501531 scopus 로고
    • Effects of cytoplasmic acidification on clathrin lattice morphology
    • Heuser, J. E. 1989. Effects of cytoplasmic acidification on clathrin lattice morphology. J. Cell. Biol. 108:402-411.
    • (1989) J. Cell. Biol. , vol.108 , pp. 402-411
    • Heuser, J.E.1
  • 14
    • 0027435603 scopus 로고
    • Topological mechanisms involved in the formation of clathrin-coated vesicles
    • Jin, A. J., and R. Nossal. 1993. Topological mechanisms involved in the formation of clathrin-coated vesicles. Biophys. J. 65:1523-1537.
    • (1993) Biophys. J. , vol.65 , pp. 1523-1537
    • Jin, A.J.1    Nossal, R.2
  • 15
    • 0030025568 scopus 로고    scopus 로고
    • F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions
    • Käs, J., H. Strey, J. X. Tang, D. Finger, R. Ezzell, E. Sackmann, and P. A. Janmey. 1996. F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions. Biophys. J. 70: 609-625.
    • (1996) Biophys. J. , vol.70 , pp. 609-625
    • Käs, J.1    Strey, H.2    Tang, J.X.3    Finger, D.4    Ezzell, R.5    Sackmann, E.6    Janmey, P.A.7
  • 16
    • 0025345414 scopus 로고
    • Clathrin and associated assembly and disassembly proteins
    • Keen, J. 1990. Clathrin and associated assembly and disassembly proteins. Annu. Rev. Biochem. 59:415-438.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 415-438
    • Keen, J.1
  • 17
    • 0018344979 scopus 로고
    • Clathrin-coated vesicles: Isolation, dissociation and factor-dependent reassociation of clathrin baskets
    • Keen, J. H., M. C. Willingham, and I. H. Pasten. 1979. Clathrin-coated vesicles: isolation, dissociation and factor-dependent reassociation of clathrin baskets. Cell 16:303-312.
    • (1979) Cell , vol.16 , pp. 303-312
    • Keen, J.H.1    Willingham, M.C.2    Pasten, I.H.3
  • 18
    • 0019435922 scopus 로고
    • Protein organization in clathrin trimers
    • Kirchhausen, T., and S. C. Harrison. 1981. Protein organization in clathrin trimers. Cell. 23:755-761.
    • (1981) Cell , vol.23 , pp. 755-761
    • Kirchhausen, T.1    Harrison, S.C.2
  • 19
    • 0022965881 scopus 로고
    • Configuration of clathrin trimers: Evidence from electron microscopy
    • Kirchhausen, T., S. C. Harrison, and J. E. Heuser. 1986. Configuration of clathrin trimers: evidence from electron microscopy. J. Ultrastruct. Res. 94:199-208.
    • (1986) J. Ultrastruct. Res. , vol.94 , pp. 199-208
    • Kirchhausen, T.1    Harrison, S.C.2    Heuser, J.E.3
  • 21
    • 0025942394 scopus 로고
    • Image averaging of flexible fibrous macromolecules: The clathrin triskelion has an elastic proximal segment
    • Kocsis, E., B. L. Trus, C. J. Steer, M. E. Bisher, and A. C. Steven. 1991. Image averaging of flexible fibrous macromolecules: the clathrin triskelion has an elastic proximal segment. J. Struct. Biol. 107:6-14.
    • (1991) J. Struct. Biol. , vol.107 , pp. 6-14
    • Kocsis, E.1    Trus, B.L.2    Steer, C.J.3    Bisher, M.E.4    Steven, A.C.5
  • 23
    • 0025874718 scopus 로고
    • Reconstitution of clathrin-coated pit budding from plasma membranes
    • Lin, H. C., M. S. Moore, D. A. Sanan, and R. G. W. Anderson. 1991. Reconstitution of clathrin-coated pit budding from plasma membranes. J. Cell. Biol. 114:881-891.
    • (1991) J. Cell. Biol. , vol.114 , pp. 881-891
    • Lin, H.C.1    Moore, M.S.2    Sanan, D.A.3    Anderson, R.G.W.4
  • 24
    • 85031641148 scopus 로고    scopus 로고
    • A thermodynamic model for clathrin basket assembly
    • Abstr.
    • Nossal, R. 1998. A thermodynamic model for clathrin basket assembly. Biophys. J. 74:95a(Abstr.).
    • (1998) Biophys. J. , vol.74
    • Nossal, R.1
  • 25
    • 0027328612 scopus 로고
    • A conformational change in the actin subunit can change the flexibility of the actin filament
    • Orlova, A., and E. H. Egelman. 1993. A conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol. Biol. 232:334-341.
    • (1993) J. Mol. Biol. , vol.232 , pp. 334-341
    • Orlova, A.1    Egelman, E.H.2
  • 27
    • 0030222108 scopus 로고    scopus 로고
    • Caveolae and caveolins
    • Parton, R. G. 1996. Caveolae and caveolins. Curr. Opin. Cell Biol. 8:542-548.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 542-548
    • Parton, R.G.1
  • 29
  • 33
    • 0030596081 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA deposited onto mica: Equilibration versus kinetic trapping studied by statistical polymer chain analysis
    • Rivetti, C. M. Guthold, and C. Bustamante. 1996. Scanning force microscopy of DNA deposited onto mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis. J. Mol. Biol. 264:919-932.
    • (1996) J. Mol. Biol. , vol.264 , pp. 919-932
    • Rivetti, C.1    Guthold, M.2    Bustamante, C.3
  • 35
    • 0030053909 scopus 로고    scopus 로고
    • Membrane dynamics in endocytosis
    • Robinson, M. S., C. Watts, and M. Zerial. 1996. Membrane dynamics in endocytosis. Cell 84:13-21.
    • (1996) Cell , vol.84 , pp. 13-21
    • Robinson, M.S.1    Watts, C.2    Zerial, M.3
  • 37
    • 0031669738 scopus 로고    scopus 로고
    • Endocytic clathrin-coated pit formation is independent of receptor internalization signal levels
    • Santini, F., M. S. Marks, and J. H. Keen. 1998. Endocytic clathrin-coated pit formation is independent of receptor internalization signal levels. Mol. Biol. Cell 9:1177-1194.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1177-1194
    • Santini, F.1    Marks, M.S.2    Keen, J.H.3
  • 38
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and L. Orci. 1996. Coat proteins and vesicle budding. Science. 271:1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 39
    • 0027639816 scopus 로고
    • Biochemical requirements for the formation of clathrin-and COP-coated transport vesicles
    • Schmid, S. L. 1993. Biochemical requirements for the formation of clathrin-and COP-coated transport vesicles. Curr. Biol. 5:621-627.
    • (1993) Curr. Biol. , vol.5 , pp. 621-627
    • Schmid, S.L.1
  • 40
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid, S. L. 1997. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu. Rev. Biochem. 66:511-548.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 41
    • 0025917331 scopus 로고
    • Stage-specific assays for coated pit formation and coated vesicle budding in vitro
    • Schmid, S. L., and E. Smythe. 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
  • 42
    • 0000811598 scopus 로고
    • Morphology of vesicles
    • R. Lipowski and A. Sackmann, editors. Chap. 8. Elsevier, Amsterdam
    • Seifert, U., and R. Lipowsky. 1995. Morphology of vesicles. In Structure and Dynamics of Membranes. R. Lipowski and A. Sackmann, editors. Chap. 8. Elsevier, Amsterdam.
    • (1995) Structure and Dynamics of Membranes
    • Seifert, U.1    Lipowsky, R.2
  • 43
    • 0018742616 scopus 로고
    • The molecular structure of human erythrocyte spectrin
    • Shotten, D. M., B. E. Burke, and D. Branton. 1979. The molecular structure of human erythrocyte spectrin. J. Mol. Biol. 131:303-329.
    • (1979) J. Mol. Biol. , vol.131 , pp. 303-329
    • Shotten, D.M.1    Burke, B.E.2    Branton, D.3
  • 44
    • 0032167614 scopus 로고    scopus 로고
    • Clathrin coats at 21 Å resolution: A cellular assembly designed to recycle multiple membrane receptors
    • Smith, C. J., N. Grigorieff, and B. M. F. Pearse. 1998. Clathrin coats at 21 Å 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.F.3
  • 45
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer, S. M., and J. E. Hinshaw. 1998. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell. 93: 1021-1029.
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 46
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei, K., V. I. Slepnev, V. Haucke, and P. De Camilli. 1999. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nature Cell Biol. 1:33-39.
    • (1999) Nature Cell Biol. , vol.1 , pp. 33-39
    • Takei, K.1    Slepnev, V.I.2    Haucke, V.3    De Camilli, P.4
  • 47
    • 0019663506 scopus 로고
    • Digital image processing of electron micrographs - The PIC system
    • Trus, B. L., and A. C. Steven. 1981. Digital image processing of electron micrographs - the PIC system. Ultramicroscopy. 6:383-386.
    • (1981) Ultramicroscopy , vol.6 , pp. 383-386
    • Trus, B.L.1    Steven, A.C.2
  • 48
    • 0019890534 scopus 로고
    • Assembly units of clathrin coats
    • Ungewickell, E., and D. Branton. 1981. Assembly units of clathrin coats. Nature (Lond). 289:420-422.
    • (1981) Nature (Lond) , vol.289 , pp. 420-422
    • Ungewickell, E.1    Branton, D.2
  • 49
    • 0022780984 scopus 로고
    • Location of the 100 kD-50 kD accessory proteins in clathrin coats
    • Vigers, G. P. A., R. A. Crowther, and B. M. F. Pearse. 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.A.1    Crowther, R.A.2    Pearse, B.M.F.3
  • 50
    • 0018182551 scopus 로고
    • Coated vesicles: Characterization, selective dissociation, and reassembly
    • Woodward, M. P., and T. F. Roth. 1978. Coated vesicles: characterization, selective dissociation, and reassembly. Proc. Natl. Acad. Sci. USA. 75:4394-4398.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4394-4398
    • Woodward, M.P.1    Roth, T.F.2
  • 52
    • 0021063734 scopus 로고
    • Assembly polypeptides from coated vesicles mediate reassembly of unique clathrin coats
    • Zaremba, S., and J. H. Keen. 1983. Assembly polypeptides from coated vesicles mediate reassembly of unique clathrin coats. J. Cell Biol. 97:1339-1347.
    • (1983) J. Cell Biol. , vol.97 , pp. 1339-1347
    • Zaremba, S.1    Keen, J.H.2
  • 53
    • 0028086353 scopus 로고
    • Role of the membrane cortex in neutrophil deformation in small pipettes
    • Zhelev, D. V., D. Needham, and R. M. Hochmuth. 1994. Role of the membrane cortex in neutrophil deformation in small pipettes. Biophys. J. 67:696-705.
    • (1994) Biophys. J. , vol.67 , pp. 696-705
    • Zhelev, D.V.1    Needham, D.2    Hochmuth, R.M.3


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