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Volumn 12, Issue 6, 2002, Pages 814-821

Endocytosis and vesicle trafficking

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ADAPTIN; AMPHIPHYSIN; BETA2 ADAPTIN; DYNAMIN; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE 15; GAMMA ADAPTIN; GAMMA SYNERGIN; INOSITOL POLYPHOSPHATE; PROTEIN; PROTEIN AAK; PROTEIN AP180; PROTEIN AUXILIN; PROTEIN DAB2; PROTEIN EPSIN; PROTEIN GAK; PROTEIN NUMB; UNCLASSIFIED DRUG;

EID: 0036909262     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(02)00395-0     Document Type: Review
Times cited : (65)

References (39)
  • 2
    • 0034572830 scopus 로고    scopus 로고
    • Three ways to make a vesicle
    • Kirchhausen T. Three ways to make a vesicle. Nat Rev Mol Cell Biol. 1:2000;187-198.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 187-198
    • Kirchhausen, T.1
  • 3
    • 0035805064 scopus 로고    scopus 로고
    • Specificity determinants in phosphoinositide dephosphorylation: Crystal structure of an archetypal inositol polyphosphate 5-phosphatase
    • 2, explains the specificity for cleavage at the 5-position.
    • 2, explains the specificity for cleavage at the 5-position.
    • (2001) Cell , vol.105 , pp. 379-389
    • Tsujishita, Y.1    Guo, S.L.2    Stolz, L.E.3    York, J.D.4    Hurley, J.H.5
  • 4
    • 0035830502 scopus 로고    scopus 로고
    • A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis
    • Mao Y.X., Chen J., Maynard J.A., Zhang B., Quiocho F.A. A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis. Cell. 104:2001;433-440.
    • (2001) Cell , vol.104 , pp. 433-440
    • Mao, Y.X.1    Chen, J.2    Maynard, J.A.3    Zhang, B.4    Quiocho, F.A.5
  • 5
    • 0035135419 scopus 로고    scopus 로고
    • 2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes
    • Two papers [4,5•] describe the structures of the ANTH domain of two proteins of the AP180 family, LAP from Drosophila and rat CALM. Ford et al. [5•] describe complexes with lipid headgroups, showing that the two adjacent phosphates are bound on the tips of lysine sidechains in a most unusual surface binding site. Full-length AP180 stimulates clathrin assembly and forms clathrin buds on lipid monolayers (visualised by electron microscopy), which become more invaginated in the presence of the AP2 adaptor complex.
    • 2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes. Science. 291:2001;1051-1055. Two papers [4,5•] describe the structures of the ANTH domain of two proteins of the AP180 family, LAP from Drosophila and rat CALM. Ford et al. [5•] describe complexes with lipid headgroups, showing that the two adjacent phosphates are bound on the tips of lysine sidechains in a most unusual surface binding site. Full-length AP180 stimulates clathrin assembly and forms clathrin buds on lipid monolayers (visualised by electron microscopy), which become more invaginated in the presence of the AP2 adaptor complex.
    • (2001) Science , vol.291 , pp. 1051-1055
    • Ford, M.G.J.1    Pearse, B.M.F.2    Higgins, M.K.3    Vallis, Y.4    Owen, D.J.5    Gibson, A.6    Hopkins, C.R.7    Evans, P.R.8    McMahon, H.T.9
  • 6
    • 0037179662 scopus 로고    scopus 로고
    • Curvature of clathrin-coated pits driven by epsin
    • 3 shows that the ligand binds in a deep cleft formed by the folding of N-terminal residues that are disordered in the unligated structure [9] into a new α helix, including residues previously identified to bind the ligand [10]. This creates an exposed hydrophobic ridge on the helix. Mutations in this hydrophobic ridge show that it is essential both for the formation of lipid tubules by the ENTH domain and for the epsin-stimulated assembly of clathrin on lipid monolayers.
    • 3 shows that the ligand binds in a deep cleft formed by the folding of N-terminal residues that are disordered in the unligated structure [9] into a new α helix, including residues previously identified to bind the ligand [10]. This creates an exposed hydrophobic ridge on the helix. Mutations in this hydrophobic ridge show that it is essential both for the formation of lipid tubules by the ENTH domain and for the epsin-stimulated assembly of clathrin on lipid monolayers.
    • (2002) Nature , vol.419 , pp. 361-366
    • Ford, M.G.1    Mills, I.G.2    Peter, B.J.3    Vallis, Y.4    Praefke, G.J.K.5    Evans, P.R.6    McMahon, H.T.7
  • 7
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic AP2 complex
    • 6 binds between two molecules in the crystal, identifying two physiological binding sites on the α- and μ2-adaptin subunits.
    • 6 binds between two molecules in the crystal, identifying two physiological binding sites on the α- and μ2-adaptin subunits.
    • (2002) Cell , vol.109 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 8
    • 0037157830 scopus 로고    scopus 로고
    • A phosphatidylinositol (4,5)-bisphosphate binding site within μ2-adaptin regulates clathrin-mediated endocytosis
    • Rohde G., Wenzel D., Haucke V. A phosphatidylinositol (4,5)-bisphosphate binding site within μ2-adaptin regulates clathrin-mediated endocytosis. J Cell Biol. 158:2002;209-214.
    • (2002) J Cell Biol , vol.158 , pp. 209-214
    • Rohde, G.1    Wenzel, D.2    Haucke, V.3
  • 10
    • 0035134328 scopus 로고    scopus 로고
    • Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis
    • Itoh T., Koshiba S., Kigawa T., Kikuchi A., Yokoyama S., Takenawa T. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science. 291:2001;1047-1051.
    • (2001) Science , vol.291 , pp. 1047-1051
    • Itoh, T.1    Koshiba, S.2    Kigawa, T.3    Kikuchi, A.4    Yokoyama, S.5    Takenawa, T.6
  • 11
    • 0035977098 scopus 로고    scopus 로고
    • Recognizing phosphatidylinositol 3-phosphate
    • Misra S., Miller G.J., Hurley J.H. Recognizing phosphatidylinositol 3-phosphate. Cell. 107:2001;559-562.
    • (2001) Cell , vol.107 , pp. 559-562
    • Misra, S.1    Miller, G.J.2    Hurley, J.H.3
  • 12
    • 0033612372 scopus 로고    scopus 로고
    • Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p
    • Misra S., Hurley J.H. Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Cell. 97:1999;657-666.
    • (1999) Cell , vol.97 , pp. 657-666
    • Misra, S.1    Hurley, J.H.2
  • 13
    • 0034681262 scopus 로고    scopus 로고
    • Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction
    • Mao Y.X., Nickitenko A., Duan X.Q., Lloyd T.E., Wu M.N., Bellen H., Quiocho F.A. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell. 100:2000;447-456.
    • (2000) Cell , vol.100 , pp. 447-456
    • Mao, Y.X.1    Nickitenko, A.2    Duan, X.Q.3    Lloyd, T.E.4    Wu, M.N.5    Bellen, H.6    Quiocho, F.A.7
  • 14
    • 0035793903 scopus 로고    scopus 로고
    • Structural mechanism of endosome docking by the FYVE domain
    • Kutateladze T., Overduin M. Structural mechanism of endosome docking by the FYVE domain. Science. 291:2001;1793-1796.
    • (2001) Science , vol.291 , pp. 1793-1796
    • Kutateladze, T.1    Overduin, M.2
  • 17
    • 0034687118 scopus 로고    scopus 로고
    • Structure of the VHS domain of human Tom1 (target of myb1): Insights into interactions with proteins and membranes
    • Misra S., Beach B.M., Hurley J.H. Structure of the VHS domain of human Tom1 (target of myb1): Insights into interactions with proteins and membranes. Biochemistry. 39:2000;11282-11290.
    • (2000) Biochemistry , vol.39 , pp. 11282-11290
    • Misra, S.1    Beach, B.M.2    Hurley, J.H.3
  • 19
    • 0037148787 scopus 로고    scopus 로고
    • Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains
    • Two papers [18,19••] show details of the binding and recognition of xDxxLL signal peptides to the VHS domains of GGA1 and GGA3.
    • Misra S., Puertollano R., Kato Y., Bonifacino J.S., Hurley J.H. Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains. Nature. 415:2002;933-937. Two papers [18,19••] show details of the binding and recognition of xDxxLL signal peptides to the VHS domains of GGA1 and GGA3.
    • (2002) Nature , vol.415 , pp. 933-937
    • Misra, S.1    Puertollano, R.2    Kato, Y.3    Bonifacino, J.S.4    Hurley, J.H.5
  • 20
    • 0036295109 scopus 로고    scopus 로고
    • Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism
    • Signal binding to GGA VHS domains is modulated but not completely determined by phosphorylation of a serine residue before the aspartic acid in the recognition motif S(P)DxxLL, which binds to a positively charged patch on the protein.
    • Kato Y., Misra S., Puertollano R., Hurley J.H., Bonifacino J.S. Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism. Nat Struct Biol. 9:2002;532-536. Signal binding to GGA VHS domains is modulated but not completely determined by phosphorylation of a serine residue before the aspartic acid in the recognition motif S(P)DxxLL, which binds to a positively charged patch on the protein.
    • (2002) Nat Struct Biol , vol.9 , pp. 532-536
    • Kato, Y.1    Misra, S.2    Puertollano, R.3    Hurley, J.H.4    Bonifacino, J.S.5
  • 21
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen D.J., Evans P.R. A structural explanation for the recognition of tyrosine-based endocytotic signals. Science. 282:1998;1327-1332.
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 22
    • 0035102330 scopus 로고    scopus 로고
    • A third specificity-determining site in μ2 adaptin for sequences upstream of YxxΦ sorting motifs
    • Owen D.J., Setiadi H., Evans P.R., McEver P.P., Green S.A. A third specificity-determining site in μ2 adaptin for sequences upstream of YxxΦ sorting motifs. Traffic. 2:2001;105-110.
    • (2001) Traffic , vol.2 , pp. 105-110
    • Owen, D.J.1    Setiadi, H.2    Evans, P.R.3    McEver, P.P.4    Green, S.A.5
  • 24
    • 0033000498 scopus 로고    scopus 로고
    • A structural explanation for the binding of multiple ligands by the α-adaptin appendage domain
    • Owen D.J., Vallis Y., Noble M.E., Hunter J.B., Dafforn T.R., Evans P.R., McMahon H.T. A structural explanation for the binding of multiple ligands by the α-adaptin appendage domain. Cell. 97:1999;805-815.
    • (1999) Cell , vol.97 , pp. 805-815
    • Owen, D.J.1    Vallis, Y.2    Noble, M.E.3    Hunter, J.B.4    Dafforn, T.R.5    Evans, P.R.6    McMahon, H.T.7
  • 25
    • 0033529768 scopus 로고    scopus 로고
    • Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly
    • Traub L.M., Downs M.A., Westrich J.L., Fremont D.H. Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly. Proc Natl Acad Sci USA. 96:1999;8907-8912.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8907-8912
    • Traub, L.M.1    Downs, M.A.2    Westrich, J.L.3    Fremont, D.H.4
  • 26
    • 0034663990 scopus 로고    scopus 로고
    • The structure and function of the β2-adaptin appendage domain
    • Owen D.J., Vallis Y., Pearse B.M.F., McMahon H.T., Evans P.R. The structure and function of the β2-adaptin appendage domain. EMBO J. 19:2000;4216-4227.
    • (2000) EMBO J , vol.19 , pp. 4216-4227
    • Owen, D.J.1    Vallis, Y.2    Pearse, B.M.F.3    McMahon, H.T.4    Evans, P.R.5
  • 27
    • 0036278105 scopus 로고    scopus 로고
    • Accessory protein recruitment motifs in clathrin-mediated endocytosis
    • Crystal structures of peptide complexes of the 'appendage' domain of α-adaptin show two modes of binding into the previously identified hydrophobic site (see [24,25]).
    • Brett T.J., Traub L.M., Fremont D.H. Accessory protein recruitment motifs in clathrin-mediated endocytosis. Structure. 10:2002;797-809. Crystal structures of peptide complexes of the 'appendage' domain of α-adaptin show two modes of binding into the previously identified hydrophobic site (see [24,25]).
    • (2002) Structure , vol.10 , pp. 797-809
    • Brett, T.J.1    Traub, L.M.2    Fremont, D.H.3
  • 29
    • 0036049039 scopus 로고    scopus 로고
    • γ-Adaptin appendage domain: Structure and binding site for Eps15 and γ-synergin
    • Kent H.M., McMahon H.T., Evans P.R., Benmerah A., Owen D.J. γ-Adaptin appendage domain: structure and binding site for Eps15 and γ-synergin. Structure. 10:2002;1-20.
    • (2002) Structure , vol.10 , pp. 1-20
    • Kent, H.M.1    McMahon, H.T.2    Evans, P.R.3    Benmerah, A.4    Owen, D.J.5
  • 30
    • 0037018156 scopus 로고    scopus 로고
    • Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals
    • Ricotta D., Conner S., Schmid S., von Figura K., Honing S. Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals. J Cell Biol. 156:2002;791-795.
    • (2002) J Cell Biol , vol.156 , pp. 791-795
    • Ricotta, D.1    Conner, S.2    Schmid, S.3    Von Figura, K.4    Honing, S.5
  • 31
    • 0035503309 scopus 로고    scopus 로고
    • Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms
    • Niemann H.H., Knetsch M.L.W., Scherer A., Manstein D.J., Kull F.J. Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms. EMBO J. 20:2001;5813-5821.
    • (2001) EMBO J , vol.20 , pp. 5813-5821
    • Niemann, H.H.1    Knetsch, M.L.W.2    Scherer, A.3    Manstein, D.J.4    Kull, F.J.5
  • 32
    • 0034598734 scopus 로고    scopus 로고
    • Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
    • Prakash B., Praefcke G.J.K., Renault L., Wittinghofer A., Herrmann C. Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature. 403:2000;567-571.
    • (2000) Nature , vol.403 , pp. 567-571
    • Prakash, B.1    Praefcke, G.J.K.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 33
    • 0034784987 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of dynamin in the constricted state
    • Zhang P.J., Hinshaw J.E. Three-dimensional reconstruction of dynamin in the constricted state. Nat Cell Biol. 3:2001;922-926.
    • (2001) Nat Cell Biol , vol.3 , pp. 922-926
    • Zhang, P.J.1    Hinshaw, J.E.2
  • 35
    • 0037062410 scopus 로고    scopus 로고
    • Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif
    • Doray B., Bruns K., Ghosh P., Kornfeld S.A. Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif. Proc Natl Acad Sci USA. 99:2002;8072-8077.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8072-8077
    • Doray, B.1    Bruns, K.2    Ghosh, P.3    Kornfeld, S.A.4
  • 36
    • 0037041026 scopus 로고    scopus 로고
    • Unusual structural organization of the endocytic proteins AP180 and epsin 1
    • For both epsin and AP180, no region of the protein apart from the N-terminal ENTH/ANTH domain shows evidence of any folded structure, by hydrodynamics or circular dichroism. This extended region (∼400 residues for epsin and ∼600 for AP180) contains a succession of binding sites for other endocytosis components, notably clathrin and AP2.
    • Kalthoff C., Alves J., Urbanke C., Knorr R., Ungewickell E.J. Unusual structural organization of the endocytic proteins AP180 and epsin 1. J Biol Chem. 277:2002;8209-8216. For both epsin and AP180, no region of the protein apart from the N-terminal ENTH/ANTH domain shows evidence of any folded structure, by hydrodynamics or circular dichroism. This extended region (∼400 residues for epsin and ∼600 for AP180) contains a succession of binding sites for other endocytosis components, notably clathrin and AP2.
    • (2002) J Biol Chem , vol.277 , pp. 8209-8216
    • Kalthoff, C.1    Alves, J.2    Urbanke, C.3    Knorr, R.4    Ungewickell, E.J.5
  • 37
    • 0033967923 scopus 로고    scopus 로고
    • Peptide-in-groove interactions link target proteins to the β-propeller of clathrin
    • ter Haar E., Harrison S.C., Kirchhausen T. Peptide-in-groove interactions link target proteins to the β-propeller of clathrin. Proc Natl Acad Sci USA. 97:2000;1096-1100.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1096-1100
    • Ter Haar, E.1    Harrison, S.C.2    Kirchhausen, T.3
  • 38
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 39
    • 0037136560 scopus 로고    scopus 로고
    • Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat
    • The crystal structures of the Sec23/Sec24 complex and the Sec23/Sar1 complex (with the GTP analogue GMPPNP) provide a detailed model of the Sec23/24/Sar1/GTP complex. Sec23 is an activating protein (GAP) for Sar1 and inserts an arginine sidechain into its active site.
    • Bi X.P., Corpina R.A., Goldberg J. Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature. 419:2002;271-277. The crystal structures of the Sec23/Sec24 complex and the Sec23/Sar1 complex (with the GTP analogue GMPPNP) provide a detailed model of the Sec23/24/Sar1/GTP complex. Sec23 is an activating protein (GAP) for Sar1 and inserts an arginine sidechain into its active site.
    • (2002) Nature , vol.419 , pp. 271-277
    • Bi, X.P.1    Corpina, R.A.2    Goldberg, J.3


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