메뉴 건너뛰기




Volumn 18, Issue 5, 2010, Pages 854-861

Conformation switching of clathrin light chain regulates clathrin lattice assembly

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN HEAVY CHAIN; CLATHRIN LIGHT CHAIN;

EID: 77952907625     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.devcel.2010.03.012     Document Type: Article
Times cited : (64)

References (35)
  • 2
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger A.T. Version 1.2 of the Crystallography and NMR system. Nat. Protoc. 2007, 2:2728-2733.
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 4
    • 14044275140 scopus 로고    scopus 로고
    • Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo
    • Chen C.Y., Brodsky F.M. Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo. J. Biol. Chem. 2005, 280:6109-6117.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6109-6117
    • Chen, C.Y.1    Brodsky, F.M.2
  • 5
    • 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., Brodsky F.M. Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans. EMBO J. 2002, 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
  • 6
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • DeLaBarre B., Brunger A.T. Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. Nat. Struct. Biol. 2003, 10:856-863.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 856-863
    • DeLaBarre, B.1    Brunger, A.T.2
  • 7
    • 33746414364 scopus 로고    scopus 로고
    • Considerations for the refinement of low-resolution crystal structures
    • DeLaBarre B., Brunger A.T. Considerations for the refinement of low-resolution crystal structures. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:923-932.
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 923-932
    • DeLaBarre, B.1    Brunger, A.T.2
  • 10
    • 23444442876 scopus 로고    scopus 로고
    • Non-stoichiometric relationship between clathrin heavy and light chains revealed by quantitative comparative proteomics of clathrin-coated vesicles from brain and liver
    • Girard M., Allaire P.D., McPherson P.S., Blondeau F. Non-stoichiometric relationship between clathrin heavy and light chains revealed by quantitative comparative proteomics of clathrin-coated vesicles from brain and liver. Mol. Cell. Proteomics 2005, 4:1145-1154.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1145-1154
    • Girard, M.1    Allaire, P.D.2    McPherson, P.S.3    Blondeau, F.4
  • 11
    • 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., Brodsky F.M. Complete reconstitution of clathrin basket formation with recombinant protein fragments: adaptor control of clathrin self-assembly. Traffic 2000, 1:69-75.
    • (2000) Traffic , vol.1 , pp. 69-75
    • Greene, B.1    Liu, S.H.2    Wilde, A.3    Brodsky, F.M.4
  • 12
    • 0023945674 scopus 로고
    • Identification of the phosphorylation sites of clathrin light chain LCb
    • Hill B.L., Drickamer K., Brodsky F.M., Parham P. Identification of the phosphorylation sites of clathrin light chain LCb. J. Biol. Chem. 1988, 263:5499-5501.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5499-5501
    • Hill, B.L.1    Drickamer, K.2    Brodsky, F.M.3    Parham, P.4
  • 13
    • 1942469322 scopus 로고    scopus 로고
    • Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference
    • Huang F., Khvorova A., Marshall W., Sorkin A. Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference. J. Biol. Chem. 2004, 279:16657-16661.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16657-16661
    • Huang, F.1    Khvorova, A.2    Marshall, W.3    Sorkin, A.4
  • 14
    • 0030975677 scopus 로고    scopus 로고
    • Novel functions of clathrin light chains: clathrin heavy chain trimerization is defective in light chain-deficient yeast
    • Huang K.M., Gullberg L., Nelson K.K., Stefan C.J., Blumer K., Lemmon S.K. Novel functions of clathrin light chains: clathrin heavy chain trimerization is defective in light chain-deficient yeast. J. Cell Sci. 1997, 110:899-910.
    • (1997) J. Cell Sci. , vol.110 , pp. 899-910
    • Huang, K.M.1    Gullberg, L.2    Nelson, K.K.3    Stefan, C.J.4    Blumer, K.5    Lemmon, S.K.6
  • 16
    • 0027195836 scopus 로고
    • Immunoelectron microscopic evidence for the extended conformation of light chains in clathrin trimers
    • Kirchhausen T., Toyoda T. Immunoelectron microscopic evidence for the extended conformation of light chains in clathrin trimers. J. Biol. Chem. 1993, 268:10268-10273.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10268-10273
    • Kirchhausen, T.1    Toyoda, T.2
  • 17
    • 14044265129 scopus 로고    scopus 로고
    • Huntingtin interacting protein 1 (HIP1) regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain
    • Legendre-Guillemin V., Metzler M., Lemaire J.F., Philie J., Gan L., Hayden M.R., McPherson P.S. Huntingtin interacting protein 1 (HIP1) regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain. J. Biol. Chem. 2005, 280:6101-6108.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6101-6108
    • Legendre-Guillemin, V.1    Metzler, M.2    Lemaire, J.F.3    Philie, J.4    Gan, L.5    Hayden, M.R.6    McPherson, P.S.7
  • 18
    • 0028858382 scopus 로고
    • Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs
    • Liu S.H., Wong M.L., Craik C.S., Brodsky F.M. Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs. Cell 1995, 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
  • 21
    • 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., Pearse B.M. Functional organization of clathrin in coats: combining electron cryomicroscopy and X-ray crystallography. Mol. Cell 1999, 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
  • 22
    • 0026503136 scopus 로고
    • Folding and trimerization of clathrin subunits at the triskelion hub
    • Näthke I.S., Heuser J., Lupas A., Stock J., Turck C.W., Brodsky F.M. Folding and trimerization of clathrin subunits at the triskelion hub. Cell 1992, 68:899-910.
    • (1992) Cell , vol.68 , pp. 899-910
    • Näthke, I.S.1    Heuser, J.2    Lupas, A.3    Stock, J.4    Turck, C.W.5    Brodsky, F.M.6
  • 23
    • 0030957964 scopus 로고    scopus 로고
    • A novel structural model for regulation of clathrin function
    • Pishvaee B., Munn A., Payne G.S. A novel structural model for regulation of clathrin function. EMBO J. 1997, 16:2227-2239.
    • (1997) EMBO J. , vol.16 , pp. 2227-2239
    • Pishvaee, B.1    Munn, A.2    Payne, G.S.3
  • 26
    • 0021092754 scopus 로고
    • Biochemical and immunological studies on clathrin light chains and their binding sites on clathrin triskelions
    • Ungewickell E. Biochemical and immunological studies on clathrin light chains and their binding sites on clathrin triskelions. EMBO J. 1983, 2:1401-1408.
    • (1983) EMBO J. , vol.2 , pp. 1401-1408
    • Ungewickell, E.1
  • 27
    • 0025900858 scopus 로고
    • Bovine brain clathrin light chains impede heavy chain assembly in vitro
    • Ungewickell E., Ungewickell H. Bovine brain clathrin light chains impede heavy chain assembly in vitro. J. Biol. Chem. 1991, 266:12710-12714.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12710-12714
    • Ungewickell, E.1    Ungewickell, H.2
  • 28
  • 30
    • 0141642033 scopus 로고    scopus 로고
    • Clathrin self-assembly involves coordinated weak interactions favorable for cellular regulation
    • Wakeham D.E., Chen C.Y., Greene B., Hwang P.K., Brodsky F.M. Clathrin self-assembly involves coordinated weak interactions favorable for cellular regulation. EMBO J. 2003, 22:4980-4990.
    • (2003) EMBO J. , vol.22 , pp. 4980-4990
    • Wakeham, D.E.1    Chen, C.Y.2    Greene, B.3    Hwang, P.K.4    Brodsky, F.M.5
  • 31
    • 33745043237 scopus 로고    scopus 로고
    • Clathrin light chain: importance of the conserved carboxy terminal domain to function in living cells
    • Wang J., Wang Y., O'Halloran T.J. Clathrin light chain: importance of the conserved carboxy terminal domain to function in living cells. Traffic 2006, 7:824-832.
    • (2006) Traffic , vol.7 , pp. 824-832
    • Wang, J.1    Wang, Y.2    O'Halloran, T.J.3
  • 32
    • 57749099198 scopus 로고    scopus 로고
    • Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R (Hip1-related protein) is regulated by clathrin light chain
    • Wilbur J.D., Chen C.Y., Manalo V., Hwang P.K., Fletterick R.J., Brodsky F.M. Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R (Hip1-related protein) is regulated by clathrin light chain. J. Biol. Chem. 2008, 283:32870-32879.
    • (2008) J. Biol. Chem. , vol.283 , pp. 32870-32879
    • Wilbur, J.D.1    Chen, C.Y.2    Manalo, V.3    Hwang, P.K.4    Fletterick, R.J.5    Brodsky, F.M.6
  • 33
    • 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., Brodsky F.M. Clathrin self-assembly is regulated by three light-chain residues controlling the formation of critical salt bridges. EMBO J. 1998, 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
  • 35
    • 34447519196 scopus 로고    scopus 로고
    • Light chain C-terminal region reinforces the stability of clathrin heavy chain trimers
    • Ybe J.A., Perez-Miller S., Niu Q., Coates D.A., Drazer M.W., Clegg M.E. Light chain C-terminal region reinforces the stability of clathrin heavy chain trimers. Traffic 2007, 8:1101-1110.
    • (2007) Traffic , vol.8 , pp. 1101-1110
    • Ybe, J.A.1    Perez-Miller, S.2    Niu, Q.3    Coates, D.A.4    Drazer, M.W.5    Clegg, M.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.