메뉴 건너뛰기




Volumn 13, Issue 1, 2012, Pages

Evolutionary analysis of the ENTH/ANTH/VHS protein superfamily reveals a coevolution between membrane trafficking and metabolism

Author keywords

Comparative genomic; Cytokinesis; Eukaryotic evolution; Membrane trafficking; Metabolism; Phylogeny

Indexed keywords

ADAPTOR PROTEIN; AP180 AMINO TEMINAL HOMOLOGY PROTEIN; EPSIN AMINO TERMINAL HOMOLOGY PROTEIN; PROTEIN VHS; UNCLASSIFIED DRUG;

EID: 84863114580     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-13-297     Document Type: Article
Times cited : (37)

References (60)
  • 1
    • 67249111424 scopus 로고    scopus 로고
    • Tales of 1001 functions: the multiple roles of membrane trafficking in development
    • 10.1111/j.1600-0854.2009.00931.x, 19570190
    • Furthauer M, Gonzalez-Gaitan M. Tales of 1001 functions: the multiple roles of membrane trafficking in development. Traffic 2009, 10:781-782. 10.1111/j.1600-0854.2009.00931.x, 19570190.
    • (2009) Traffic , vol.10 , pp. 781-782
    • Furthauer, M.1    Gonzalez-Gaitan, M.2
  • 2
    • 34247180015 scopus 로고    scopus 로고
    • The origin of eukaryotes: a reappraisal
    • 10.1038/nrg2071, 17429433
    • de Duve C. The origin of eukaryotes: a reappraisal. Nat Rev Genet 2007, 8:395-403. 10.1038/nrg2071, 17429433.
    • (2007) Nat Rev Genet , vol.8 , pp. 395-403
    • de Duve, C.1
  • 3
    • 77949910116 scopus 로고    scopus 로고
    • Origin of the cell nucleus, mitosis and sex: roles of intracellular coevolution
    • 10.1186/1745-6150-5-7, 2837639, 20132544
    • Cavalier-Smith T. Origin of the cell nucleus, mitosis and sex: roles of intracellular coevolution. Biol Direct 2010, 5:7. 10.1186/1745-6150-5-7, 2837639, 20132544.
    • (2010) Biol Direct , vol.5 , pp. 7
    • Cavalier-Smith, T.1
  • 4
    • 84934443890 scopus 로고    scopus 로고
    • Origin of eukaryotic endomembranes: a critical evaluation of different model scenarios
    • 10.1007/978-0-387-74021-8_3, 17977457
    • Jekely G. Origin of eukaryotic endomembranes: a critical evaluation of different model scenarios. Adv Exp Med Biol 2007, 607:38-51. 10.1007/978-0-387-74021-8_3, 17977457.
    • (2007) Adv Exp Med Biol , vol.607 , pp. 38-51
    • Jekely, G.1
  • 5
    • 74749099537 scopus 로고    scopus 로고
    • The early endosome: a busy sorting station for proteins at the crossroads
    • 2810677, 19924646
    • Jovic M, Sharma M, Rahajeng J, Caplan S. The early endosome: a busy sorting station for proteins at the crossroads. Histol Histopathol 2010, 25:99-112. 2810677, 19924646.
    • (2010) Histol Histopathol , vol.25 , pp. 99-112
    • Jovic, M.1    Sharma, M.2    Rahajeng, J.3    Caplan, S.4
  • 6
    • 33748288113 scopus 로고    scopus 로고
    • BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature
    • 10.1016/j.bbalip.2006.06.015, 16938488
    • Itoh T, De Camilli P. BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim Biophys Acta 2006, 1761:897-912. 10.1016/j.bbalip.2006.06.015, 16938488.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 897-912
    • Itoh, T.1    De Camilli, P.2
  • 7
    • 0034192540 scopus 로고    scopus 로고
    • Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2) + finger protein (PLZF)
    • 10.1083/jcb.149.3.537, 2174850, 10791968
    • Hyman J, Chen H, Di Fiore PP, De Camilli P, Brunger AT. Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2) + finger protein (PLZF). J Cell Biol 2000, 149:537-546. 10.1083/jcb.149.3.537, 2174850, 10791968.
    • (2000) J Cell Biol , vol.149 , pp. 537-546
    • Hyman, J.1    Chen, H.2    Di Fiore, P.P.3    De Camilli, P.4    Brunger, A.T.5
  • 8
    • 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
    • 10.1016/S0092-8674(00)80680-7, 10693761
    • Mao Y, Nickitenko A, Duan X, Lloyd TE, Wu MN, Bellen H, Quiocho FA. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell 2000, 100:447-456. 10.1016/S0092-8674(00)80680-7, 10693761.
    • (2000) Cell , vol.100 , pp. 447-456
    • Mao, Y.1    Nickitenko, A.2    Duan, X.3    Lloyd, T.E.4    Wu, M.N.5    Bellen, H.6    Quiocho, F.A.7
  • 9
    • 0035135419 scopus 로고    scopus 로고
    • Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes
    • 10.1126/science.291.5506.1051, 11161218
    • Ford MG, Pearse BM, Higgins MK, Vallis Y, Owen DJ, Gibson A, Hopkins CR, Evans PR, McMahon HT. Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes. Science 2001, 291:1051-1055. 10.1126/science.291.5506.1051, 11161218.
    • (2001) Science , vol.291 , pp. 1051-1055
    • Ford, M.G.1    Pearse, B.M.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
  • 10
    • 33748969492 scopus 로고    scopus 로고
    • Endocytic adaptors: recruiters, coordinators and regulators
    • 10.1016/j.tcb.2006.08.001, 16935508
    • Maldonado-Baez L, Wendland B. Endocytic adaptors: recruiters, coordinators and regulators. Trends Cell Biol 2006, 16:505-513. 10.1016/j.tcb.2006.08.001, 16935508.
    • (2006) Trends Cell Biol , vol.16 , pp. 505-513
    • Maldonado-Baez, L.1    Wendland, B.2
  • 11
    • 0035369692 scopus 로고    scopus 로고
    • Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor
    • 10.1126/science.1060896, 11387476
    • Zhu Y, Doray B, Poussu A, Lehto VP, Kornfeld S. Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor. Science 2001, 292:1716-1718. 10.1126/science.1060896, 11387476.
    • (2001) Science , vol.292 , pp. 1716-1718
    • Zhu, Y.1    Doray, B.2    Poussu, A.3    Lehto, V.P.4    Kornfeld, S.5
  • 12
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • 10.1038/ncb790, 11988742
    • Shih SC, Katzmann DJ, Schnell JD, Sutanto M, Emr SD, Hicke L. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat Cell Biol 2002, 4:389-393. 10.1038/ncb790, 11988742.
    • (2002) Nat Cell Biol , vol.4 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 14
    • 9444273167 scopus 로고    scopus 로고
    • Components of coated vesicles and nuclear pore complexes share a common molecular architecture
    • 10.1371/journal.pbio.0020380, 524472, 15523559
    • Devos D, Dokudovskaya S, Alber F, Williams R, Chait BT, Sali A, Rout MP. Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biol 2004, 2:e380. 10.1371/journal.pbio.0020380, 524472, 15523559.
    • (2004) PLoS Biol , vol.2
    • Devos, D.1    Dokudovskaya, S.2    Alber, F.3    Williams, R.4    Chait, B.T.5    Sali, A.6    Rout, M.P.7
  • 15
    • 33749005392 scopus 로고    scopus 로고
    • The COPII cage: unifying principles of vesicle coat assembly
    • 10.1038/nrm2025, 16990852
    • Gurkan C, Stagg SM, Lapointe P, Balch WE. The COPII cage: unifying principles of vesicle coat assembly. Nat Rev Mol Cell Biol 2006, 7:727-738. 10.1038/nrm2025, 16990852.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 727-738
    • Gurkan, C.1    Stagg, S.M.2    Lapointe, P.3    Balch, W.E.4
  • 16
    • 49749133839 scopus 로고    scopus 로고
    • SNAREing the basis of multicellularity: consequences of protein family expansion during evolution
    • 10.1093/molbev/msn151, 18621745
    • Kloepper TH, Kienle CN, Fasshauer D. SNAREing the basis of multicellularity: consequences of protein family expansion during evolution. Mol Biol Evol 2008, 25:2055-2068. 10.1093/molbev/msn151, 18621745.
    • (2008) Mol Biol Evol , vol.25 , pp. 2055-2068
    • Kloepper, T.H.1    Kienle, C.N.2    Fasshauer, D.3
  • 17
    • 84934441798 scopus 로고    scopus 로고
    • Reconstructing the evolution of the endocytic system: insights from genomics and molecular cell biology
    • 10.1007/978-0-387-74021-8_7, 17977461
    • Field MC, Gabernet-Castello C, Dacks JB. Reconstructing the evolution of the endocytic system: insights from genomics and molecular cell biology. Adv Exp Med Biol 2007, 607:84-96. 10.1007/978-0-387-74021-8_7, 17977461.
    • (2007) Adv Exp Med Biol , vol.607 , pp. 84-96
    • Field, M.C.1    Gabernet-Castello, C.2    Dacks, J.B.3
  • 18
    • 47149100894 scopus 로고    scopus 로고
    • Evolution of the multivesicular body ESCRT machinery; retention across the eukaryotic lineage
    • 10.1111/j.1600-0854.2008.00797.x, 18637903
    • Leung KF, Dacks JB, Field MC. Evolution of the multivesicular body ESCRT machinery; retention across the eukaryotic lineage. Traffic 2008, 9:1698-1716. 10.1111/j.1600-0854.2008.00797.x, 18637903.
    • (2008) Traffic , vol.9 , pp. 1698-1716
    • Leung, K.F.1    Dacks, J.B.2    Field, M.C.3
  • 19
    • 0037227948 scopus 로고    scopus 로고
    • Yeast epsin-related proteins required for Golgi-endosome traffic define a gamma-adaptin ear-binding motif
    • 10.1038/ncb901, 12483220
    • Duncan MC, Costaguta G, Payne GS. Yeast epsin-related proteins required for Golgi-endosome traffic define a gamma-adaptin ear-binding motif. Nat Cell Biol 2003, 5:77-81. 10.1038/ncb901, 12483220.
    • (2003) Nat Cell Biol , vol.5 , pp. 77-81
    • Duncan, M.C.1    Costaguta, G.2    Payne, G.S.3
  • 20
    • 3042723253 scopus 로고    scopus 로고
    • Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body
    • 10.1091/mbc.E03-11-0793, 452561, 15107463
    • Eugster A, Pecheur EI, Michel F, Winsor B, Letourneur F, Friant S. Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. Mol Biol Cell 2004, 15:3031-3041. 10.1091/mbc.E03-11-0793, 452561, 15107463.
    • (2004) Mol Biol Cell , vol.15 , pp. 3031-3041
    • Eugster, A.1    Pecheur, E.I.2    Michel, F.3    Winsor, B.4    Letourneur, F.5    Friant, S.6
  • 21
    • 33644872913 scopus 로고    scopus 로고
    • Exploring the ESCRTing machinery in eukaryotes
    • 10.1016/j.tplants.2006.01.008, 2865992, 16488176
    • Winter V, Hauser MT. Exploring the ESCRTing machinery in eukaryotes. Trends Plant Sci 2006, 11:115-123. 10.1016/j.tplants.2006.01.008, 2865992, 16488176.
    • (2006) Trends Plant Sci , vol.11 , pp. 115-123
    • Winter, V.1    Hauser, M.T.2
  • 22
    • 58549084391 scopus 로고    scopus 로고
    • Dictyostelium Tom1 participates to an ancestral ESCRT-0 complex
    • 10.1111/j.1600-0854.2008.00855.x, 19054384
    • Blanc C, Charette SJ, Mattei S, Aubry L, Smith EW, Cosson P, Letourneur F. Dictyostelium Tom1 participates to an ancestral ESCRT-0 complex. Traffic 2009, 10:161-171. 10.1111/j.1600-0854.2008.00855.x, 19054384.
    • (2009) Traffic , vol.10 , pp. 161-171
    • Blanc, C.1    Charette, S.J.2    Mattei, S.3    Aubry, L.4    Smith, E.W.5    Cosson, P.6    Letourneur, F.7
  • 23
    • 79951847406 scopus 로고    scopus 로고
    • Multivesicular bodies in the enigmatic amoeboflagellate Breviata anathema and the evolution of ESCRT 0
    • 10.1242/jcs.078436, 3031372, 21266469
    • Herman EK, Walker G, van der Giezen M, Dacks JB. Multivesicular bodies in the enigmatic amoeboflagellate Breviata anathema and the evolution of ESCRT 0. J Cell Sci 2011, 124:613-621. 10.1242/jcs.078436, 3031372, 21266469.
    • (2011) J Cell Sci , vol.124 , pp. 613-621
    • Herman, E.K.1    Walker, G.2    van der Giezen, M.3    Dacks, J.B.4
  • 24
    • 0034687118 scopus 로고    scopus 로고
    • Structure of the VHS domain of human Tom1 (target of myb 1): insights into interactions with proteins and membranes
    • 10.1021/bi0013546, 10985773
    • Misra S, Beach BM, Hurley JH. Structure of the VHS domain of human Tom1 (target of myb 1): insights into interactions with proteins and membranes. Biochemistry 2000, 39:11282-11290. 10.1021/bi0013546, 10985773.
    • (2000) Biochemistry , vol.39 , pp. 11282-11290
    • Misra, S.1    Beach, B.M.2    Hurley, J.H.3
  • 27
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • 10.1073/pnas.94.11.5679, 20838, 9159132
    • McCann RO, Craig SW. The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc Natl Acad Sci U S A 1997, 94:5679-5684. 10.1073/pnas.94.11.5679, 20838, 9159132.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 28
    • 0037025197 scopus 로고    scopus 로고
    • Rooting the eukaryote tree by using a derived gene fusion
    • 10.1126/science.1071196, 12098695
    • Stechmann A, Cavalier-Smith T. Rooting the eukaryote tree by using a derived gene fusion. Science 2002, 297:89-91. 10.1126/science.1071196, 12098695.
    • (2002) Science , vol.297 , pp. 89-91
    • Stechmann, A.1    Cavalier-Smith, T.2
  • 29
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • 10.1083/jcb.200302131, 2172703, 12900395
    • Bache KG, Brech A, Mehlum A, Stenmark H. Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J Cell Biol 2003, 162:435-442. 10.1083/jcb.200302131, 2172703, 12900395.
    • (2003) J Cell Biol , vol.162 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 30
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • 10.1074/jbc.M210843200, 12551915
    • Bache KG, Raiborg C, Mehlum A, Stenmark H. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J Biol Chem 2003, 278:12513-12521. 10.1074/jbc.M210843200, 12551915.
    • (2003) J Biol Chem , vol.278 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 31
    • 70450250211 scopus 로고    scopus 로고
    • Coats of endosomal protein sorting: retromer and ESCRT
    • 10.1016/j.pbi.2009.09.005, 19836992
    • Schellmann S, Pimpl P. Coats of endosomal protein sorting: retromer and ESCRT. Curr Opin Plant Biol 2009, 12:670-676. 10.1016/j.pbi.2009.09.005, 19836992.
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 670-676
    • Schellmann, S.1    Pimpl, P.2
  • 32
    • 79959829850 scopus 로고    scopus 로고
    • Clathrin Mediates Endocytosis and Polar Distribution of PIN Auxin Transporters in Arabidopsis. Plant Cell, Friml J
    • Kitakura S, Vanneste S, Robert S, Lofke C, Teichmann T. Tanaka H 2011, Clathrin Mediates Endocytosis and Polar Distribution of PIN Auxin Transporters in Arabidopsis. Plant Cell, Friml J.
    • (2011) Tanaka H
    • Kitakura, S.1    Vanneste, S.2    Robert, S.3    Lofke, C.4    Teichmann, T.5
  • 33
    • 33749265140 scopus 로고    scopus 로고
    • Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of soluble cargo proteins in plant cells via interactions with clathrin, AP-1, VTI11, and VSR1
    • 10.1105/tpc.105.039123, 1560928, 16905657
    • Song J, Lee MH, Lee GJ, Yoo CM, Hwang I. Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of soluble cargo proteins in plant cells via interactions with clathrin, AP-1, VTI11, and VSR1. Plant Cell 2006, 18:2258-2274. 10.1105/tpc.105.039123, 1560928, 16905657.
    • (2006) Plant Cell , vol.18 , pp. 2258-2274
    • Song, J.1    Lee, M.H.2    Lee, G.J.3    Yoo, C.M.4    Hwang, I.5
  • 34
    • 34249791180 scopus 로고    scopus 로고
    • EpsinR2 interacts with clathrin, adaptor protein-3, AtVTI12, and phosphatidylinositol-3-phosphate. Implications for EpsinR2 function in protein trafficking in plant cells
    • 10.1104/pp.106.095349, 1851837, 17277094
    • Lee GJ, Kim H, Kang H, Jang M, Lee DW, Lee S, Hwang I. EpsinR2 interacts with clathrin, adaptor protein-3, AtVTI12, and phosphatidylinositol-3-phosphate. Implications for EpsinR2 function in protein trafficking in plant cells. Plant Physiol 2007, 143:1561-1575. 10.1104/pp.106.095349, 1851837, 17277094.
    • (2007) Plant Physiol , vol.143 , pp. 1561-1575
    • Lee, G.J.1    Kim, H.2    Kang, H.3    Jang, M.4    Lee, D.W.5    Lee, S.6    Hwang, I.7
  • 35
    • 79960855196 scopus 로고    scopus 로고
    • Comprehensive phylogenetic reconstruction of amoebozoa based on concatenated analyses of SSU-rDNA and actin genes
    • 10.1371/journal.pone.0022780, 3145751, 21829512
    • Lahr DJ, Grant J, Nguyen T, Lin JH, Katz LA. Comprehensive phylogenetic reconstruction of amoebozoa based on concatenated analyses of SSU-rDNA and actin genes. PLoS One 2011, 6:e22780. 10.1371/journal.pone.0022780, 3145751, 21829512.
    • (2011) PLoS One , vol.6
    • Lahr, D.J.1    Grant, J.2    Nguyen, T.3    Lin, J.H.4    Katz, L.A.5
  • 36
    • 77956234143 scopus 로고    scopus 로고
    • Conservation and function of Rab small GTPases in Entamoeba: annotation of E. invadens Rab and its use for the understanding of Entamoeba biology
    • 10.1016/j.exppara.2010.04.014, 20434444
    • Nakada-Tsukui K, Saito-Nakano Y, Husain A, Nozaki T. Conservation and function of Rab small GTPases in Entamoeba: annotation of E. invadens Rab and its use for the understanding of Entamoeba biology. Exp Parasitol 2010, 126:337-347. 10.1016/j.exppara.2010.04.014, 20434444.
    • (2010) Exp Parasitol , vol.126 , pp. 337-347
    • Nakada-Tsukui, K.1    Saito-Nakano, Y.2    Husain, A.3    Nozaki, T.4
  • 38
    • 0036047057 scopus 로고    scopus 로고
    • The GOLD domain, a novel protein module involved in Golgi function and secretion
    • 115225, 12049664
    • Anantharaman V, Aravind L. The GOLD domain, a novel protein module involved in Golgi function and secretion. Genome Biol 2002, 3:research0023. 115225, 12049664.
    • (2002) Genome Biol , vol.3
    • Anantharaman, V.1    Aravind, L.2
  • 39
    • 0242551350 scopus 로고    scopus 로고
    • Small GTPases and the evolution of the eukaryotic cell
    • 10.1002/bies.10353, 14579253
    • Jekely G. Small GTPases and the evolution of the eukaryotic cell. Bioessays 2003, 25:1129-1138. 10.1002/bies.10353, 14579253.
    • (2003) Bioessays , vol.25 , pp. 1129-1138
    • Jekely, G.1
  • 40
    • 34948835726 scopus 로고    scopus 로고
    • Evolution of the eukaryotic membrane-trafficking system: origin, tempo and mode
    • 10.1242/jcs.013250, 17715154
    • Dacks JB, Field MC. Evolution of the eukaryotic membrane-trafficking system: origin, tempo and mode. J Cell Sci 2007, 120:2977-2985. 10.1242/jcs.013250, 17715154.
    • (2007) J Cell Sci , vol.120 , pp. 2977-2985
    • Dacks, J.B.1    Field, M.C.2
  • 41
    • 53149133508 scopus 로고    scopus 로고
    • PtdIns5P regulation through evolution: roles in membrane trafficking?
    • 10.1016/j.tibs.2008.07.002, 18774718
    • Lecompte O, Poch O, Laporte J. PtdIns5P regulation through evolution: roles in membrane trafficking?. Trends Biochem Sci 2008, 33:453-460. 10.1016/j.tibs.2008.07.002, 18774718.
    • (2008) Trends Biochem Sci , vol.33 , pp. 453-460
    • Lecompte, O.1    Poch, O.2    Laporte, J.3
  • 42
    • 84867984219 scopus 로고    scopus 로고
    • The Single ENTH-Domain Protein of Trypanosomes; Endocytic Functions and Evolutionary Relationship with Epsin. Traffic, Field MC
    • Gabernet-Castello C. Dacks JB 2009, The Single ENTH-Domain Protein of Trypanosomes; Endocytic Functions and Evolutionary Relationship with Epsin. Traffic, Field MC.
    • (2009) Dacks JB
    • Gabernet-Castello, C.1
  • 43
    • 77957866592 scopus 로고    scopus 로고
    • Identification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotes
    • 10.1016/j.gene.2010.08.006, 2965036, 20713135
    • Zhang D, Aravind L. Identification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotes. Gene 2010, 469:18-30. 10.1016/j.gene.2010.08.006, 2965036, 20713135.
    • (2010) Gene , vol.469 , pp. 18-30
    • Zhang, D.1    Aravind, L.2
  • 44
    • 77954203830 scopus 로고    scopus 로고
    • UMA and MABP domains throw light on receptor endocytosis and selection of endosomal cargoes
    • 10.1093/bioinformatics/btq235, 2881412, 20448139
    • de Souza RF, Aravind L. UMA and MABP domains throw light on receptor endocytosis and selection of endosomal cargoes. Bioinformatics 2010, 26:1477-1480. 10.1093/bioinformatics/btq235, 2881412, 20448139.
    • (2010) Bioinformatics , vol.26 , pp. 1477-1480
    • de Souza, R.F.1    Aravind, L.2
  • 45
    • 2942610720 scopus 로고    scopus 로고
    • Identification and functional characterization of Arabidopsis AP180, a binding partner of plant alphaC-adaptin
    • 10.1242/jcs.01062, 15054111
    • Barth M, Holstein SE. Identification and functional characterization of Arabidopsis AP180, a binding partner of plant alphaC-adaptin. J Cell Sci 2004, 117:2051-2062. 10.1242/jcs.01062, 15054111.
    • (2004) J Cell Sci , vol.117 , pp. 2051-2062
    • Barth, M.1    Holstein, S.E.2
  • 46
    • 79551637456 scopus 로고    scopus 로고
    • Phosphoinositides regulate clathrin-dependent endocytosis at the tip of pollen tubes in Arabidopsis and tobacco
    • 10.1105/tpc.110.076760, 3027160, 21189293
    • Zhao Y, Yan A, Feijo JA, Furutani M, Takenawa T, Hwang I, Fu Y, Yang Z. Phosphoinositides regulate clathrin-dependent endocytosis at the tip of pollen tubes in Arabidopsis and tobacco. Plant Cell 2010, 22:4031-4044. 10.1105/tpc.110.076760, 3027160, 21189293.
    • (2010) Plant Cell , vol.22 , pp. 4031-4044
    • Zhao, Y.1    Yan, A.2    Feijo, J.A.3    Furutani, M.4    Takenawa, T.5    Hwang, I.6    Fu, Y.7    Yang, Z.8
  • 47
    • 83055194383 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis: the gateway into plant cells
    • 10.1016/j.pbi.2011.08.006, 21945181
    • Chen X, Irani NG, Friml J. Clathrin-mediated endocytosis: the gateway into plant cells. Curr Opin Plant Biol 2011, 14:674-682. 10.1016/j.pbi.2011.08.006, 21945181.
    • (2011) Curr Opin Plant Biol , vol.14 , pp. 674-682
    • Chen, X.1    Irani, N.G.2    Friml, J.3
  • 48
    • 0037148787 scopus 로고    scopus 로고
    • Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains
    • 10.1038/415933a, 11859375
    • Misra S, Puertollano R, Kato Y, Bonifacino JS, Hurley JH. Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains. Nature 2002, 415:933-937. 10.1038/415933a, 11859375.
    • (2002) Nature , vol.415 , pp. 933-937
    • Misra, S.1    Puertollano, R.2    Kato, Y.3    Bonifacino, J.S.4    Hurley, J.H.5
  • 50
    • 53749090788 scopus 로고    scopus 로고
    • The endosomal system of plants: charting new and familiar territories
    • 10.1104/pp.108.120105, 2492610, 18678740
    • Robinson DG, Jiang L, Schumacher K. The endosomal system of plants: charting new and familiar territories. Plant Physiol 2008, 147:1482-1492. 10.1104/pp.108.120105, 2492610, 18678740.
    • (2008) Plant Physiol , vol.147 , pp. 1482-1492
    • Robinson, D.G.1    Jiang, L.2    Schumacher, K.3
  • 51
    • 0346731278 scopus 로고    scopus 로고
    • The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae
    • 1462899, 14704157
    • Baggett JJ, D'Aquino KE, Wendland B. The Sla2p talin domain plays a role in endocytosis in Saccharomyces cerevisiae. Genetics 2003, 165:1661-1674. 1462899, 14704157.
    • (2003) Genetics , vol.165 , pp. 1661-1674
    • Baggett, J.J.1    D'Aquino, K.E.2    Wendland, B.3
  • 52
    • 0242266922 scopus 로고    scopus 로고
    • Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome
    • 10.1083/jcb.200305007, 2173515, 14581452
    • Bilodeau PS, Winistorfer SC, Kearney WR, Robertson AD, Piper RC. Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome. J Cell Biol 2003, 163:237-243. 10.1083/jcb.200305007, 2173515, 14581452.
    • (2003) J Cell Biol , vol.163 , pp. 237-243
    • Bilodeau, P.S.1    Winistorfer, S.C.2    Kearney, W.R.3    Robertson, A.D.4    Piper, R.C.5
  • 53
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • 10.1038/nature07961, 19325624
    • Raiborg C, Stenmark H. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 2009, 458:445-452. 10.1038/nature07961, 19325624.
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 55
    • 0036293634 scopus 로고    scopus 로고
    • Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin
    • 10.1023/A:1011397007366, 12836669
    • Koshiba S, Kigawa T, Kikuchi A, Yokoyama S. Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin. J Struct Funct Genomics 2002, 2:1-8. 10.1023/A:1011397007366, 12836669.
    • (2002) J Struct Funct Genomics , vol.2 , pp. 1-8
    • Koshiba, S.1    Kigawa, T.2    Kikuchi, A.3    Yokoyama, S.4
  • 56
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan an integration platform for the signature-recognition methods in InterPro
    • 10.1093/bioinformatics/17.9.847, 11590104
    • Zdobnov EM, Apweiler R. InterProScan an integration platform for the signature-recognition methods in InterPro. Bioinformatics 2001, 17:847-848. 10.1093/bioinformatics/17.9.847, 11590104.
    • (2001) Bioinformatics , vol.17 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2
  • 57
    • 0030464460 scopus 로고    scopus 로고
    • SEAVIEW and PHYLO_WIN: two graphic tools for sequence alignment and molecular phylogeny
    • Galtier N, Gouy M, Gautier C. SEAVIEW and PHYLO_WIN: two graphic tools for sequence alignment and molecular phylogeny. Comput Appl Biosci 1996, 12:543-548.
    • (1996) Comput Appl Biosci , vol.12 , pp. 543-548
    • Galtier, N.1    Gouy, M.2    Gautier, C.3
  • 58
    • 33845873289 scopus 로고    scopus 로고
    • Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation
    • 10.1093/bioinformatics/btl529, 17050570
    • Letunic I, Bork P. Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation. Bioinformatics 2007, 23:127-128. 10.1093/bioinformatics/btl529, 17050570.
    • (2007) Bioinformatics , vol.23 , pp. 127-128
    • Letunic, I.1    Bork, P.2
  • 59
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • 10.1093/nar/25.17.3389, 146917, 9254694
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25:3389-3402. 10.1093/nar/25.17.3389, 146917, 9254694.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 60
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • 10.1093/bioinformatics/15.4.305, 10320398
    • Gouet P, Courcelle E, Stuart DI, Métoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999, 15:305-8. 10.1093/bioinformatics/15.4.305, 10320398.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    MÃÂtoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.