메뉴 건너뛰기




Volumn 14, Issue 9, 2013, Pages 987-996

Hsc70-induced changes in clathrin-auxilin cage structure suggest a role for clathrin light chains in cage disassembly

Author keywords

3D structure; Cryo electron microscopy (cryo EM); Endocytosis; Molecular chaperone; Vesicle uncoating

Indexed keywords


EID: 85027935265     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12085     Document Type: Article
Times cited : (23)

References (57)
  • 1
    • 30844453760 scopus 로고    scopus 로고
    • Life of a clathrin coat: insights from clathrin and AP structures
    • Edeling M, Smith C, Owen D. Life of a clathrin coat: insights from clathrin and AP structures. Nat Rev Mol Cell Biol 2006;7:32-44.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 32-44
    • Edeling, M.1    Smith, C.2    Owen, D.3
  • 3
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: an integrated process
    • Schmid SL. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu Rev Biochem 1997;66:511-548.
    • (1997) Annu Rev Biochem , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 4
    • 0030986955 scopus 로고    scopus 로고
    • Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets
    • Barouch W, Prasad K, Greene LE, Eisenberg E. Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets. Biochemistry 1997;36:4303-4308.
    • (1997) Biochemistry , vol.36 , pp. 4303-4308
    • Barouch, W.1    Prasad, K.2    Greene, L.E.3    Eisenberg, E.4
  • 5
    • 0029846829 scopus 로고    scopus 로고
    • Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin
    • Holstein SE, Ungewickell H, Ungewickell E. Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin. J Cell Biol 1996;135:925-937.
    • (1996) J Cell Biol , vol.135 , pp. 925-937
    • Holstein, S.E.1    Ungewickell, H.2    Ungewickell, E.3
  • 6
    • 0025077286 scopus 로고
    • Predominance of clathrin light chain LCb correlates with the presence of a regulated secretory pathway
    • Acton SL, Brodsky FM. Predominance of clathrin light chain LCb correlates with the presence of a regulated secretory pathway. J Cell Biol 1990;111:1419-1426.
    • (1990) J Cell Biol , vol.111 , pp. 1419-1426
    • Acton, S.L.1    Brodsky, F.M.2
  • 9
    • 0030957964 scopus 로고    scopus 로고
    • A novel structural model for regulation of clathrin function
    • Pishvaee B,Munn A, Payne GS. 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
  • 10
    • 0348013276 scopus 로고    scopus 로고
    • Contribution of cysteines to clathrin trimerization domain stability and mapping of light chain binding
    • Ybe JA, Ruppel N, Mishra S, VanHaaften E. Contribution of cysteines to clathrin trimerization domain stability and mapping of light chain binding. Traffic 2003;4:850-856.
    • (2003) Traffic , vol.4 , pp. 850-856
    • Ybe, J.A.1    Ruppel, N.2    Mishra, S.3    VanHaaften, E.4
  • 13
    • 76349117689 scopus 로고    scopus 로고
    • Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly
    • Xing Y, Böcking T, Wolf M, Grigorieff N, Kirchhausen T, Harrison SC. Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly. EMBO J 2010;29:655-665.
    • (2010) EMBO J , vol.29 , pp. 655-665
    • Xing, Y.1    Böcking, T.2    Wolf, M.3    Grigorieff, N.4    Kirchhausen, T.5    Harrison, S.C.6
  • 14
    • 38749145560 scopus 로고    scopus 로고
    • A motif in the clathrin heavy chain required for the Hsc70/auxilin uncoating reaction
    • Rapoport I, Boll W, Yu A, Bocking T, Kirchhausen T. A motif in the clathrin heavy chain required for the Hsc70/auxilin uncoating reaction. Mol Biol Cell 2008;19:405-413.
    • (2008) Mol Biol Cell , vol.19 , pp. 405-413
    • Rapoport, I.1    Boll, W.2    Yu, A.3    Bocking, T.4    Kirchhausen, T.5
  • 15
    • 79955557478 scopus 로고    scopus 로고
    • A sequential mechanism for clathrin cage disassembly by 70-kDa heat-shock cognate protein (Hsc70) and auxilin
    • Rothnie A, Clarke AR, Kuzmic P, Cameron A, Smith CJ. A sequential mechanism for clathrin cage disassembly by 70-kDa heat-shock cognate protein (Hsc70) and auxilin. Proc Natl Acad Sci USA 2011;108:6927-6932.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 6927-6932
    • Rothnie, A.1    Clarke, A.R.2    Kuzmic, P.3    Cameron, A.4    Smith, C.J.5
  • 17
    • 0032167614 scopus 로고    scopus 로고
    • Clathrin coats at 21 angstrom resolution: a cellular assembly designed to recycle multiple membrane receptors
    • Smith C, Grigorieff N, Pearse B. Clathrin coats at 21 angstrom resolution: a cellular assembly designed to recycle multiple membrane receptors. EMBO J 1998;17:4943-4953.
    • (1998) EMBO J , vol.17 , pp. 4943-4953
    • Smith, C.1    Grigorieff, N.2    Pearse, B.3
  • 19
    • 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 SC, Kirchhausen T. Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating. Nature 2004;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
  • 20
    • 44649169371 scopus 로고    scopus 로고
    • Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation
    • Chang YW, Sun YJ, Wang C, Hsiao CD. Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation. J Biol Chem 2008;283:15502-15511.
    • (2008) J Biol Chem , vol.283 , pp. 15502-15511
    • Chang, Y.W.1    Sun, Y.J.2    Wang, C.3    Hsiao, C.D.4
  • 22
    • 27944436648 scopus 로고    scopus 로고
    • Structural basis of interdomain communication in the Hsc70 chaperone
    • Jiang J, Prasad K, Lafer EM, Sousa R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol Cell 2005;20:513-524.
    • (2005) Mol Cell , vol.20 , pp. 513-524
    • Jiang, J.1    Prasad, K.2    Lafer, E.M.3    Sousa, R.4
  • 24
    • 79952359360 scopus 로고    scopus 로고
    • Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70- driven clathrin uncoating
    • Böcking T, Aguet F, Harrison SC, Kirchhausen T. Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70- driven clathrin uncoating. Nat Struct Mol Biol 2011;18:295-301.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 295-301
    • Böcking, T.1    Aguet, F.2    Harrison, S.C.3    Kirchhausen, T.4
  • 25
    • 77956306571 scopus 로고    scopus 로고
    • Structure of the PTEN-like region of auxilin, a detector of clathrin-coated vesicle budding
    • Guan R, Dai H, Han D, Harrison SC, Kirchhausen T. Structure of the PTEN-like region of auxilin, a detector of clathrin-coated vesicle budding. Structure 2010;18:1191-1198.
    • (2010) Structure , vol.18 , pp. 1191-1198
    • Guan, R.1    Dai, H.2    Han, D.3    Harrison, S.C.4    Kirchhausen, T.5
  • 26
    • 0021206453 scopus 로고
    • A role for clathrin light chains in the recognition of clathrin cages by 'uncoating ATPase'
    • Schmid SL, Braell WA, Schlossman DM, Rothman JE. A role for clathrin light chains in the recognition of clathrin cages by 'uncoating ATPase'. Nature 1984;311:228-231.
    • (1984) Nature , vol.311 , pp. 228-231
    • Schmid, S.L.1    Braell, W.A.2    Schlossman, D.M.3    Rothman, J.E.4
  • 28
    • 0037147292 scopus 로고    scopus 로고
    • Identification of domain required for catalytic activity of auxilin in supporting clathrin uncoating by Hsc70
    • Ma Y, Greener T, Pacold ME, Kaushal S, Greene LE, Eisenberg E. Identification of domain required for catalytic activity of auxilin in supporting clathrin uncoating by Hsc70. J Biol Chem 2002;277:49267-49274.
    • (2002) J Biol Chem , vol.277 , pp. 49267-49274
    • Ma, Y.1    Greener, T.2    Pacold, M.E.3    Kaushal, S.4    Greene, L.E.5    Eisenberg, E.6
  • 29
    • 0035965299 scopus 로고    scopus 로고
    • Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor complex
    • Scheele U, Kalthoff C, Ungewickell E. Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor complex. J Biol Chem 2001;276:36131-36138.
    • (2001) J Biol Chem , vol.276 , pp. 36131-36138
    • Scheele, U.1    Kalthoff, C.2    Ungewickell, E.3
  • 30
    • 0022410258 scopus 로고
    • Two classes of binding sites for uncoating protein in clathrin triskelions
    • Schmid SL, Rothman JE. Two classes of binding sites for uncoating protein in clathrin triskelions. J Biol Chem 1985;260:10050-10056.
    • (1985) J Biol Chem , vol.260 , pp. 10050-10056
    • Schmid, S.L.1    Rothman, J.E.2
  • 31
    • 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
  • 34
    • 67749099404 scopus 로고    scopus 로고
    • Endocytic accessory proteins are functionally distinguished by their differential effects on the maturation of clathrin-coated pits
    • Mettlen M, Stoeber M, Loerke D, Antonescu CN, Danuser G, Schmid SL. Endocytic accessory proteins are functionally distinguished by their differential effects on the maturation of clathrin-coated pits. Mol Biol Cell 2009;20:3251-3260.
    • (2009) Mol Biol Cell , vol.20 , pp. 3251-3260
    • Mettlen, M.1    Stoeber, M.2    Loerke, D.3    Antonescu, C.N.4    Danuser, G.5    Schmid, S.L.6
  • 35
    • 77955263413 scopus 로고    scopus 로고
    • A comparison of GFP-tagged clathrin light chains with fluorochromated light chains in vivo and in vitro
    • Hoffmann A, Dannhauser PN, Groos S, Hinrichsen L, Curth U, Ungewickell EJ. A comparison of GFP-tagged clathrin light chains with fluorochromated light chains in vivo and in vitro. Traffic 2010;11:1129-1140.
    • (2010) Traffic , vol.11 , pp. 1129-1140
    • Hoffmann, A.1    Dannhauser, P.N.2    Groos, S.3    Hinrichsen, L.4    Curth, U.5    Ungewickell, E.J.6
  • 36
    • 0032473362 scopus 로고    scopus 로고
    • Clathrin self-assembly is regulated by three light-chain residues controlling the formation of critical salt bridges
    • Ybe JA, Greene B, Liu SH, Pley U, Parham P, Brodsky FM. 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
  • 37
    • 80053356578 scopus 로고    scopus 로고
    • Clathrin light chain directs endocytosis by influencing the binding of the yeast Hip1R homologue, Sla2, to F-actin
    • Boettner DR, Friesen H, Andrews B, Lemmon SK. Clathrin light chain directs endocytosis by influencing the binding of the yeast Hip1R homologue, Sla2, to F-actin. Mol Biol Cell 2011;22:3699-3714.
    • (2011) Mol Biol Cell , vol.22 , pp. 3699-3714
    • Boettner, D.R.1    Friesen, H.2    Andrews, B.3    Lemmon, S.K.4
  • 38
    • 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 JD, Chen CY, Manalo V, Hwang PK, Fletterick RJ, Brodsky FM. 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
  • 39
    • 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 CY, Brodsky FM. 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
  • 40
    • 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,MetzlerM, Lemaire JF, Philie J, Gan L, Hayden MR, McPherson PS. 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
  • 41
    • 0021760620 scopus 로고
    • Identification of a protein kinase as an intrinsic component of rat liver coated vesicles
    • Campbell C, Squicciarini J, Shia M, Pilch PF, Fine RE. Identification of a protein kinase as an intrinsic component of rat liver coated vesicles. Biochemistry 1984;23:4420-4426.
    • (1984) Biochemistry , vol.23 , pp. 4420-4426
    • Campbell, C.1    Squicciarini, J.2    Shia, M.3    Pilch, P.F.4    Fine, R.E.5
  • 42
    • 0021487739 scopus 로고
    • Purification and properties of 100-kd proteins from coated vesicles and their reconstitution with clathrin
    • Pearse BM, Robinson MS. Purification and properties of 100-kd proteins from coated vesicles and their reconstitution with clathrin. EMBO J 1984;3:1951-1957.
    • (1984) EMBO J , vol.3 , pp. 1951-1957
    • Pearse, B.M.1    Robinson, M.S.2
  • 43
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1
    • Höhfeld J, Jentsch S. GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J 1997;16:6209-6216.
    • (1997) EMBO J , vol.16 , pp. 6209-6216
    • Höhfeld, J.1    Jentsch, S.2
  • 44
    • 0023316845 scopus 로고
    • Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells
    • Sorger PK, Pelham HR. Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells. EMBO J 1987;6:993-998.
    • (1987) EMBO J , vol.6 , pp. 993-998
    • Sorger, P.K.1    Pelham, H.R.2
  • 45
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: purification of an uncoating ATPase
    • Schlossman DM, Schmid SL, Braell WA, Rothman JE. An enzyme that removes clathrin coats: purification of an uncoating ATPase. J Cell Biol 1984;99:723-733.
    • (1984) J Cell Biol , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.E.4
  • 46
    • 0025231301 scopus 로고
    • Dissociation of clathrin from coated vesicles by the uncoating ATPase
    • Greene LE, Eisenberg E. Dissociation of clathrin from coated vesicles by the uncoating ATPase. J Biol Chem 1990; 265:6682-6687.
    • (1990) J Biol Chem , vol.265 , pp. 6682-6687
    • Greene, L.E.1    Eisenberg, E.2
  • 47
    • 0021092725 scopus 로고
    • Clathrin heavy chain, light chain interactions
    • Winkler FK, Stanley KK. Clathrin heavy chain, light chain interactions. EMBO J 1983;2:1393-1400.
    • (1983) EMBO J , vol.2 , pp. 1393-1400
    • Winkler, F.K.1    Stanley, K.K.2
  • 48
    • 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, Ladjadj M, Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 1996;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.5    Ladjadj, M.6    Leith, A.7
  • 49
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice
    • Grigorieff N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice. J Mol Biol 1998;277: 1033-1046.
    • (1998) J Mol Biol , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 50
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: high-resolution refinement of single particle structures
    • Grigorieff N. FREALIGN: high-resolution refinement of single particle structures. J Struct Biol 2007;157:117-125.
    • (2007) J Struct Biol , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 51
    • 0033776245 scopus 로고    scopus 로고
    • Docking structures of domains into maps from cryoelectron microscopy using local correlation
    • Roseman AM. Docking structures of domains into maps from cryoelectron microscopy using local correlation. Acta Crystallogr D Biol Crystallogr 2000;56(Pt 10):1332-1340.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , Issue.PART 10 , pp. 1332-1340
    • Roseman, A.M.1
  • 52
    • 0037375602 scopus 로고    scopus 로고
    • Particle finding in electron micrographs using a fast local correlation algorithm
    • Roseman AM. Particle finding in electron micrographs using a fast local correlation algorithm. Ultramicroscopy 2003;94(3-4):225-236.
    • (2003) Ultramicroscopy , vol.94 , Issue.3-4 , pp. 225-236
    • Roseman, A.M.1
  • 53
    • 3242887696 scopus 로고    scopus 로고
    • SCit: web tools for protein side chain conformation analysis
    • Web Server issue
    • Gautier R, Camproux AC, Tuffé ry P. SCit: web tools for protein side chain conformation analysis. Nucleic Acids Res 2004;32(Web Server issue):W508-W511.
    • (2004) Nucleic Acids Res , vol.32
    • Gautier, R.1    Camproux, A.C.2    Tufféry, P.3
  • 54
    • 33747819887 scopus 로고    scopus 로고
    • SABBAC: online Structural Alphabetbased protein BackBone reconstruction from Alpha-Carbon trace
    • Web Server issue
    • Maupetit J, Gautier R, Tuffé ry P. SABBAC: online Structural Alphabetbased protein BackBone reconstruction from Alpha-Carbon trace. Nucleic Acids Res 2006;34(Web Server issue):W147-W151.
    • (2006) Nucleic Acids Res , vol.34
    • Maupetit, J.1    Gautier, R.2    Tufféry, P.3
  • 55
    • 0023374114 scopus 로고
    • Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy
    • Milligan RA, Flicker PF. Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy. J Cell Biol 1987;105:29-39.
    • (1987) J Cell Biol , vol.105 , pp. 29-39
    • Milligan, R.A.1    Flicker, P.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.