메뉴 건너뛰기




Volumn 3, Issue 6, 1999, Pages 761-770

Functional organization of clathrin in coats: Combining electron cryomicroscopy and x-ray crystallography

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CLATHRIN;

EID: 0033153279     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(01)80008-3     Document Type: Article
Times cited : (96)

References (51)
  • 1
    • 0345012707 scopus 로고
    • Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane
    • Ahle, S., Mann, A., Eichelsbacher, U., and Ungewickell, E. (1988). Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane. EMBO J. 7, 919-929.
    • (1988) EMBO J. , vol.7 , pp. 919-929
    • Ahle, S.1    Mann, A.2    Eichelsbacher, U.3    Ungewickell, E.4
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994). The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 5
    • 0019813567 scopus 로고
    • Assembly and packing of clathrin into coats
    • Crowther, R.A., and Pearse, B.M. (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.2
  • 7
    • 0031941591 scopus 로고    scopus 로고
    • Assembly of clathrin coats disrupts the association between Eps15 and AP-2 adaptors
    • Cupers, P., Jadhav, A.P., and Kirchhausen, T. (1998). Assembly of clathrin coats disrupts the association between Eps15 and AP-2 adaptors. J. Biol. Chem. 273, 1847-1850.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1847-1850
    • Cupers, P.1    Jadhav, A.P.2    Kirchhausen, T.3
  • 9
    • 0019707963 scopus 로고
    • SPIDER - A modular software system for electron image processing
    • Frank, J., Shimkin, B., and Dowse, H. (1981). SPIDER - A modular software system for electron image processing. Ultramicroscopy 6, 343-358.
    • (1981) Ultramicroscopy , vol.6 , pp. 343-358
    • Frank, J.1    Shimkin, B.2    Dowse, H.3
  • 10
    • 0029975088 scopus 로고    scopus 로고
    • Spider and web - Processing and visualization of images in 3d electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y.H., Ladjadj, M., and Leith, A. (1996). Spider and web - Processing and visualization of images in 3d electron microscopy and related fields. J. Struct. Biol. 116, 190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.H.5    Ladjadj, M.6    Leith, A.7
  • 11
    • 0027330921 scopus 로고
    • The β1 and β2 subunits of the AP complexes are the clathrin coat assembly components
    • Gallusser, A., and Kirchhausen, T. (1993). The β1 and β2 subunits of the AP complexes are the clathrin coat assembly components. EMBO J. 12, 5237-5244.
    • (1993) EMBO J. , vol.12 , pp. 5237-5244
    • Gallusser, A.1    Kirchhausen, T.2
  • 12
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman, O.B., Jr., Krupnick, J.G., Gurevich, V.V., Benovic, J.L., and Keen, J.H. (1997). Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. J. Biol. Chem. 272, 15017-15022.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15017-15022
    • Goodman O.B., Jr.1    Krupnick, J.G.2    Gurevich, V.V.3    Benovic, J.L.4    Keen, J.H.5
  • 13
    • 0018827560 scopus 로고
    • Three-dimensional visualization of coated vesicle formation in fibroblasts
    • Heuser, J. (1980). Three-dimensional visualization of coated vesicle formation in fibroblasts. J. Cell Biol. 84, 560-583.
    • (1980) J. Cell Biol. , vol.84 , pp. 560-583
    • Heuser, J.1
  • 14
    • 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
  • 15
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., and Cowan, S.W. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3
  • 16
    • 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
  • 17
    • 0021683933 scopus 로고
    • Structural domains of clathrin heavy chains
    • Kirchhausen, T., and Harrison, S.C. (1984). Structural domains of clathrin heavy chains. J. Cell Biol. 99, 1725-1734.
    • (1984) J. Cell Biol. , vol.99 , pp. 1725-1734
    • Kirchhausen, T.1    Harrison, S.C.2
  • 18
    • 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, 10268-1027 3.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10268-10273
    • Kirchhausen, T.1    Toyoda, T.2
  • 23
    • 0030794182 scopus 로고    scopus 로고
    • Linking cargo to vesicle formation - Receptor tail interactions with coat proteins
    • Kirchhausen, T., Bonifacino, J.S., and Riezman, H. (1997). Linking cargo to vesicle formation - Receptor tail interactions with coat proteins. Curr. Opin. Cell Biol. 9, 488-495.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 488-495
    • Kirchhausen, T.1    Bonifacino, J.S.2    Riezman, H.3
  • 24
    • 0030967614 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus
    • Krupnick, J.G., Goodman, O.B., Jr., Keen, J.H., and Benovic, J.L. (1997). Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus. J. Biol. Chem. 272, 15011-15016.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15011-15016
    • Krupnick, J.G.1    Goodman O.B., Jr.2    Keen, J.H.3    Benovic, J.L.4
  • 26
    • 0026007817 scopus 로고
    • Sequence of the clathrin heavy chain from Saccharomyces cerevisiae and requirement of the COOH terminus for clathrin function
    • Lemmon, S.K., Pellicena Palle, A., Conley, K., and Freund, C.L. (1991). Sequence of the clathrin heavy chain from Saccharomyces cerevisiae and requirement of the COOH terminus for clathrin function. J. Cell Biol. 112, 65-80.
    • (1991) J. Cell Biol. , vol.112 , pp. 65-80
    • Lemmon, S.K.1    Pellicena Palle, A.2    Conley, K.3    Freund, C.L.4
  • 27
    • 0025949426 scopus 로고
    • Light-chain-independent binding of adaptors, AP180, and auxilin to clathrin
    • Lindner, R., and Ungewickell, E. (1991). Light-chain-independent binding of adaptors, AP180, and auxilin to clathrin. Biochemistry 30, 9097-9101.
    • (1991) Biochemistry , vol.30 , pp. 9097-9101
    • Lindner, R.1    Ungewickell, E.2
  • 28
    • 0028858382 scopus 로고
    • Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs
    • Liu, S.-H., Wong, M.L., Craik, C.S., and Brodsky, F.M. (1995). Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs. Cell 83, 257-267.
    • (1995) Cell , vol.83 , pp. 257-267
    • Liu, S.-H.1    Wong, M.L.2    Craik, C.S.3    Brodsky, F.M.4
  • 29
    • 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
  • 31
    • 0021487739 scopus 로고
    • Purification and properties of 100-kd proteins from coated vesicles and their reconstitution with clathrin
    • Pearse, B.M., and Robinson, M.S. (1984). Purification and properties of 100-kd proteins from coated vesicles and their reconstitution with clathrin. EMBO J. 3, 1951-1957.
    • (1984) EMBO J. , vol.3 , pp. 1951-1957
    • Pearse, B.M.1    Robinson, M.S.2
  • 32
    • 0025258892 scopus 로고
    • Clathrin, adaptors, and sorting
    • Pearse, B., and Robinson, M. (1990). Clathrin, adaptors, and sorting. Annu. Rev. Cell Biol. 6, 151-171.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 151-171
    • Pearse, B.1    Robinson, M.2
  • 33
    • 0018651717 scopus 로고
    • Yolk transport in the ovarian follicle of the hen (Gallus domesticus): Lipoprotein-like particles at the periphery of the oocyte in the rapid growth phase
    • Perry, M.M., and Gilbert, A.B. (1979). Yolk transport in the ovarian follicle of the hen (Gallus domesticus): Lipoprotein-like particles at the periphery of the oocyte in the rapid growth phase. J. Cell Sci. 39, 257-272.
    • (1979) J. Cell Sci. , vol.39 , pp. 257-272
    • Perry, M.M.1    Gilbert, A.B.2
  • 34
    • 0032515135 scopus 로고    scopus 로고
    • Clathrin coats - Threads laid bare
    • Pishvaee, B., and Payne, G.S. (1998). Clathrin coats - Threads laid bare. Cell 95, 443-446.
    • (1998) Cell , vol.95 , pp. 443-446
    • Pishvaee, B.1    Payne, G.S.2
  • 35
    • 0030957964 scopus 로고    scopus 로고
    • A novel structural model for regulation of clathrin function
    • Pishvaee, B., Munn, A., and Payne, G.S. (1997). A novel structural model for regulation of clathrin function. EMBO J. 16, 2227-2239.
    • (1997) EMBO J. , vol.16 , pp. 2227-2239
    • Pishvaee, B.1    Munn, A.2    Payne, G.S.3
  • 36
    • 0023228992 scopus 로고
    • 100-kD coated vesicle proteins: Molecular heterogeneity and intracellular distribution studied with monoclonal antibodies
    • Robinson, M.S. (1987). 100-kD coated vesicle proteins: Molecular heterogeneity and intracellular distribution studied with monoclonal antibodies. J. Cell Biol. 104, 887-895.
    • (1987) J. Cell Biol. , vol.104 , pp. 887-895
    • Robinson, M.S.1
  • 37
    • 0031106614 scopus 로고    scopus 로고
    • Coats and vesicle budding
    • Robinson, M.S. (1997). Coats and vesicle budding. Trends Cell Biol. 7, 99-102.
    • (1997) Trends Cell Biol. , vol.7 , pp. 99-102
    • Robinson, M.S.1
  • 38
    • 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, 3661-366 8.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3661-3668
    • Scarmato, P.1    Kirchhausen, T.2
  • 39
    • 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
  • 40
    • 0032167614 scopus 로고    scopus 로고
    • Clathrin coats at 21 Å resolution: A cellular assembly designed to recycle multiple membrane receptors
    • Smith, C.J., Grigorieff, N., and Pearse, B.M. (1998). Clathrin coats at 21 Å resolution: A cellular assembly designed to recycle multiple membrane receptors. EMBO J. 17, 4943-495 3.
    • (1998) EMBO J. , vol.17 , pp. 4943-4953
    • Smith, C.J.1    Grigorieff, N.2    Pearse, B.M.3
  • 41
    • 0022971519 scopus 로고
    • Clathrin cubes: An extreme variant of the normal cage
    • Sorger, P.K., Crowther, R.A., Finch, J.T., and Pearse, B.M. (1986). Clathrin cubes: An extreme variant of the normal cage. J. Cell Biol. 103, 1213-1219.
    • (1986) J. Cell Biol. , vol.103 , pp. 1213-1219
    • Sorger, P.K.1    Crowther, R.A.2    Finch, J.T.3    Pearse, B.M.4
  • 42
    • 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
  • 43
    • 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. 8, 1401-1408.
    • (1983) EMBO J. , vol.8 , pp. 1401-1408
    • Ungewickell, E.1
  • 44
    • 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
  • 45
    • 0025900858 scopus 로고
    • Bovine brain clathrin light chains impede heavy chain assembly in vitro
    • Ungewickell, E., and Ungewickell, H. (1991). Bovine brain clathrin light chains impede heavy chain assembly in vitro. J. Biol. Chem. 266, 12710-12714.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12710-12714
    • Ungewickell, E.1    Ungewickell, H.2
  • 46
    • 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. (1986a). 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
  • 47
    • 0022684837 scopus 로고
    • Three-dimensional structure of clathrin cages in ice
    • Vigers, G.P., Crowther, R.A., and Pearse, B.M. (1986b). 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
  • 49
    • 0031214092 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated endocytosis by the amphiphysin SH3 domain
    • Wigge, P., Vallis, Y., and McMahon, H.T. (1997). Inhibition of receptor-mediated endocytosis by the amphiphysin SH3 domain. Curr. Biol. 7, 554-560.
    • (1997) Curr. Biol. , vol.7 , pp. 554-560
    • Wigge, P.1    Vallis, Y.2    McMahon, H.T.3
  • 50
    • 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
  • 51
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.