메뉴 건너뛰기




Volumn 6, Issue 9, 2014, Pages

Unconventional functions for clathrin, ESCRTs, and other endocytic regulators in the cytoskeleton, cell cycle, nucleus, and beyond: Links to human disease

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN; ESCRT PROTEIN; GLUCOSE;

EID: 84905478139     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a017004     Document Type: Article
Times cited : (18)

References (126)
  • 1
    • 0020462085 scopus 로고
    • Initial events during phagocytosis by macrophages viewed from outside and inside the cell: Membrane-particle interactions and clathrin
    • Aggeler J., Werb Z. 1982. Initial events during phagocytosis by macrophages viewed from outside and inside the cell: Membrane-particle interactions and clathrin. J Cell Biol 94: 613-623.
    • (1982) J Cell Biol , vol.94 , pp. 613-623
    • Aggeler, J.1    Werb, Z.2
  • 2
    • 68249085870 scopus 로고    scopus 로고
    • Differential requirements for actin during yeast and mammalian endocytosis
    • Aghamohammadzadeh S., Ayscough KR. 2009. Differential requirements for actin during yeast and mammalian endocytosis. Nat Cell Biol 11: 1039-1042.
    • (2009) Nat Cell Biol , vol.11 , pp. 1039-1042
    • Aghamohammadzadeh, S.1    Ayscough, K.R.2
  • 3
    • 0023020763 scopus 로고
    • Purification and properties of a new clathrin assembly protein
    • Ahle S., Ungewickell E. 1986. Purification and properties of a new clathrin assembly protein. EMBO J 5: 3143-3149.
    • (1986) EMBO J , vol.5 , pp. 3143-3149
    • Ahle, S.1    Ungewickell, E.2
  • 4
    • 84903765792 scopus 로고    scopus 로고
    • Reciprocal regulation of endocytosis and metabolism
    • doi: 10.1101/cshperspect.a016964
    • Antonescu CN, McGraw TE, Klip A. 2014. Reciprocal regulation of endocytosis and metabolism. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a016964.
    • (2014) Cold Spring Harb Perspect Biol
    • Antonescu, C.N.1    McGraw, T.E.2    Klip, A.3
  • 5
    • 33745768614 scopus 로고    scopus 로고
    • The novel CALM interactor CATS influences the subcellular localization of the leukemogenic fusion protein CALM/AF10
    • Archangelo L.F., Glasner J, Krause A, Bohlander SK. 2006. The novel CALM interactor CATS influences the subcellular localization of the leukemogenic fusion protein CALM/AF10. Oncogene 25: 4099-4109.
    • (2006) Oncogene , vol.25 , pp. 4099-4109
    • Archangelo, L.F.1    Glasner, J.2    Krause, A.3    Bohlander, S.K.4
  • 6
    • 65549107435 scopus 로고    scopus 로고
    • Cerebellar neurons possess a vesicular compartment structurally and functionally similar to Glut4-storage vesicles from peripheral insulin-sensitive tissues
    • Bakirtzi K., Belfort G, Lopez-Coviella I, Kuruppu D, Cao L, Abel E.D., Brownell AL, Kandror KV. 2009. Cerebellar neurons possess a vesicular compartment structurally and functionally similar to Glut4-storage vesicles from peripheral insulin-sensitive tissues. J Neurosci 29: 5193-5201.
    • (2009) J Neurosci , vol.29 , pp. 5193-5201
    • Bakirtzi, K.1    Belfort, G.2    Lopez-Coviella, I.3    Kuruppu, D.4    Cao, L.5    Abel, E.D.6    Brownell, A.L.7    Kandror, K.V.8
  • 8
    • 1942445085 scopus 로고    scopus 로고
    • Endocytosis: Signaling from endocytic membranes to the nucleus
    • Benmerah A. 2004. Endocytosis: Signaling from endocytic membranes to the nucleus. Curr Biol 14: R314-R316.
    • (2004) Curr Biol , vol.14
    • Benmerah, A.1
  • 9
    • 0036696444 scopus 로고    scopus 로고
    • The endocytic protein α-adaptin is required for Numbmediated asymmetric cell division in Drosophila
    • Berdnik D., Torok T, Gonzalez-Gaitan M, Knoblich JA. 2002. The endocytic protein α-adaptin is required for Numbmediated asymmetric cell division in Drosophila. Dev Cell 3: 221-231.
    • (2002) Dev Cell , vol.3 , pp. 221-231
    • Berdnik, D.1    Torok, T.2    Gonzalez-Gaitan, M.3    Knoblich, J.A.4
  • 10
    • 84897654475 scopus 로고    scopus 로고
    • Endocytosis and signaling during development
    • doi: 10.1101/cshperspect.a017020
    • Bökel C, Brand M. 2014. Endocytosis and signaling during development. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a017020.
    • (2014) Cold Spring Harb Perspect Biol
    • Bökel, C.1    Brand, M.2
  • 13
    • 79952281843 scopus 로고    scopus 로고
    • A TACC3/ chTOG/clathrin complex stabilises kinetochore fibres by inter-microtubule bridging
    • Booth D.G., Hood FE, Prior IA, Royle SJ. 2011. A TACC3/ chTOG/clathrin complex stabilises kinetochore fibres by inter-microtubule bridging. EMBO J 30: 906-919.
    • (2011) EMBO J , vol.30 , pp. 906-919
    • Booth, D.G.1    Hood, F.E.2    Prior, I.A.3    Royle, S.J.4
  • 14
    • 80052432601 scopus 로고    scopus 로고
    • Actin dynamics counteract membrane tension during clathrin-mediated endocytosis
    • Boulant S., Kural C, Zeeh JC, Ubelmann F, Kirchhausen T. 2011. Actin dynamics counteract membrane tension during clathrin-mediated endocytosis. Nat Cell Biol 13: 1124-1131.
    • (2011) Nat Cell Biol , vol.13 , pp. 1124-1131
    • Boulant, S.1    Kural, C.2    Zeeh, J.C.3    Ubelmann, F.4    Kirchhausen, T.5
  • 15
    • 0036278105 scopus 로고    scopus 로고
    • Accessory protein recruitment motifs in clathrin-mediated endocytosis
    • Brett T.J., Traub LM, Fremont DH. 2002. Accessory protein recruitment motifs in clathrin-mediated endocytosis. Structure 10: 797-809.
    • (2002) Structure , vol.10 , pp. 797-809
    • Brett, T.J.1    Traub, L.M.2    Fremont, D.H.3
  • 17
    • 84870212873 scopus 로고    scopus 로고
    • Diversity of clathrin function:New tricks for an old protein
    • Brodsky F.M. 2012. Diversity of clathrin function:New tricks for an old protein. Annu Rev Cell Dev Biol 28: 309-336.
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 309-336
    • Brodsky, F.M.1
  • 18
    • 0036270751 scopus 로고    scopus 로고
    • Regulated transport of the glucose transporter GLUT4
    • Bryant N.J., Govers R, James DE. 2002. Regulated transport of the glucose transporter GLUT4. Nat Rev Mol Cell Biol 3: 267-277.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 267-277
    • Bryant, N.J.1    Govers, R.2    James, D.E.3
  • 20
    • 84859630113 scopus 로고    scopus 로고
    • ESCRT-III governs the Aurora B-mediated abscission checkpoint through CHMP4C
    • Carlton J.G., Caballe A, Agromayor M, Kloc M, Martin-Serrano J. 2012. ESCRT-III governs the Aurora B-mediated abscission checkpoint through CHMP4C. Science 336: 220-225.
    • (2012) Science , vol.336 , pp. 220-225
    • Carlton, J.G.1    Caballe, A.2    Agromayor, M.3    Kloc, M.4    Martin-Serrano, J.5
  • 21
    • 1642464712 scopus 로고    scopus 로고
    • TOGp, the human homolog of XMAP215/Dis1, is required for centrosome integrity, spindle pole organization, and bipolar spindle assembly
    • Cassimeris L., Morabito J. 2004. TOGp, the human homolog of XMAP215/Dis1, is required for centrosome integrity, spindle pole organization, and bipolar spindle assembly. Mol Biol Cell 15: 1580-1590.
    • (2004) Mol Biol Cell , vol.15 , pp. 1580-1590
    • Cassimeris, L.1    Morabito, J.2
  • 22
    • 34247129671 scopus 로고    scopus 로고
    • Downregulation of CD4 by human immunodeficiency virus type 1Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor
    • Chaudhuri R., Lindwasser OW, Smith WJ, Hurley JH, Bonifacino JS. 2007. Downregulation of CD4 by human immunodeficiency virus type 1Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor. J Virol 81: 3877-3890.
    • (2007) J Virol , vol.81 , pp. 3877-3890
    • Chaudhuri, R.1    Lindwasser, O.W.2    Smith, W.J.3    Hurley, J.H.4    Bonifacino, J.S.5
  • 23
    • 84858126301 scopus 로고    scopus 로고
    • Aurora A kinase activity is required for localization of TACC3/ch-TOG/clathrin inter-microtubule bridges
    • Cheeseman L.P., Booth DG, Hood FE, Prior IA, Royle SJ. 2011. Aurora A kinase activity is required for localization of TACC3/ch-TOG/clathrin inter-microtubule bridges. Commun Integr Biol 4: 409-412.
    • (2011) Commun Integr Biol , vol.4 , pp. 409-412
    • Cheeseman, L.P.1    Booth, D.G.2    Hood, F.E.3    Prior, I.A.4    Royle, S.J.5
  • 26
    • 12644297393 scopus 로고    scopus 로고
    • The light chain subunit is required for clathrin function in Saccharomyces cerevisiae
    • Chu D.S., Pishvaee B, Payne GS. 1996. The light chain subunit is required for clathrin function in Saccharomyces cerevisiae. J Biol Chem 271: 33123-33130.
    • (1996) J Biol Chem , vol.271 , pp. 33123-33130
    • Chu, D.S.1    Pishvaee, B.2    Payne, G.S.3
  • 29
    • 84899743971 scopus 로고    scopus 로고
    • Endocytosis of viruses and bacteria
    • doi: 10.1101/ cshperspect.a016972
    • Cossart P, Helenius A. 2014. Endocytosis of viruses and bacteria. Cold Spring Harb Perspect Biol doi: 10.1101/ cshperspect.a016972.
    • (2014) Cold Spring Harb Perspect Biol
    • Cossart, P.1    Helenius, A.2
  • 30
    • 1842631478 scopus 로고    scopus 로고
    • T cell receptor engagement leads to phosphorylation of clathrin heavy chain during receptor internalization
    • Crotzer V.L., Mabardy AS, Weiss A, Brodsky FM. 2004. T cell receptor engagement leads to phosphorylation of clathrin heavy chain during receptor internalization. J Exp Med 199: 981-991.
    • (2004) J Exp Med , vol.199 , pp. 981-991
    • Crotzer, V.L.1    Mabardy, A.S.2    Weiss, A.3    Brodsky, F.M.4
  • 32
    • 18344401500 scopus 로고    scopus 로고
    • MLL and CALM are fused to AF10 in morphologically distinct subsets of acute leukemia with translocation t(10;11): Both rearrangements are associated with a poor prognosis
    • Dreyling M.H., Schrader K, Fonatsch C, Schlegelberger B, Haase D., Schoch C, Ludwig W, Loffler H, Buchner T, Wormann B., et al. 1998. MLL and CALM are fused to AF10 in morphologically distinct subsets of acute leukemia with translocation t(10;11): Both rearrangements are associated with a poor prognosis. Blood 91: 4662-4667.
    • (1998) Blood , vol.91 , pp. 4662-4667
    • Dreyling, M.H.1    Schrader, K.2    Fonatsch, C.3    Schlegelberger, B.4    Haase, D.5    Schoch, C.6    Ludwig, W.7    Loffler, H.8    Buchner, T.9    Wormann, B.10
  • 33
    • 84905479255 scopus 로고    scopus 로고
    • Cargo sorting in the endocytic pathway: A key regulator of cell polarity and tissue dynamics
    • doi: 10.1101/cshperspect.a016899
    • Eaton S, Martin-Belmonte F. 2014. Cargo sorting in the endocytic pathway: A key regulator of cell polarity and tissue dynamics. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a016899.
    • (2014) Cold Spring Harb Perspect Biol
    • Eaton, S.1    Martin-Belmonte, F.2
  • 34
    • 33745177802 scopus 로고    scopus 로고
    • Requirement of clathrin heavy chain for p53-mediated transcription
    • Enari M., Ohmori K, Kitabayashi I, Taya Y. 2006. Requirement of clathrin heavy chain for p53-mediated transcription. Genes Dev 20: 1087-1099.
    • (2006) Genes Dev , vol.20 , pp. 1087-1099
    • Enari, M.1    Ohmori, K.2    Kitabayashi, I.3    Taya, Y.4
  • 35
    • 0033611051 scopus 로고    scopus 로고
    • An actin-binding protein of the Sla2/huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles
    • Engqvist-Goldstein A.E., Kessels MM, Chopra VS, Hayden MR, Drubin DG. 1999. An actin-binding protein of the Sla2/huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles. J Cell Biol 147: 1503-1518.
    • (1999) J Cell Biol , vol.147 , pp. 1503-1518
    • Engqvist-Goldstein, A.E.1    Kessels, M.M.2    Chopra, V.S.3    Hayden, M.R.4    Drubin, D.G.5
  • 36
    • 0035904239 scopus 로고    scopus 로고
    • The actin-binding protein Hip1R associates with clathrin during early stages of endocytosis and promotes clathrin assembly in vitro
    • Engqvist-Goldstein A.E., Warren RA, Kessels MM, Keen JH, Heuser J., Drubin DG. 2001. The actin-binding protein Hip1R associates with clathrin during early stages of endocytosis and promotes clathrin assembly in vitro. J Cell Biol 154: 1209-1223.
    • (2001) J Cell Biol , vol.154 , pp. 1209-1223
    • Engqvist-Goldstein, A.E.1    Warren, R.A.2    Kessels, M.M.3    Keen, J.H.4    Heuser, J.5    Drubin, D.G.6
  • 37
    • 75749142337 scopus 로고    scopus 로고
    • The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step
    • Esk C., Chen CY, Johannes L, Brodsky FM. 2010. The clathrin heavy chain isoform CHC22 functions in a novel endosomal sorting step. J Cell Biol 188: 131-144.
    • (2010) J Cell Biol , vol.188 , pp. 131-144
    • Esk, C.1    Chen, C.Y.2    Johannes, L.3    Brodsky, F.M.4
  • 38
    • 84866596927 scopus 로고    scopus 로고
    • Replacement of charged and polar residues in the coiled-coiled interface of huntingtin-interacting protein 1 (HIP1) causes aggregation and cell death
    • Fontaine S.N., Bauer SP, Lin X, Poorfarahani S, Ybe JA. 2012. Replacement of charged and polar residues in the coiled-coiled interface of huntingtin-interacting protein 1 (HIP1) causes aggregation and cell death. FEBS Lett 586: 3030-3036.
    • (2012) FEBS Lett , vol.586 , pp. 3030-3036
    • Fontaine, S.N.1    Bauer, S.P.2    Lin, X.3    Poorfarahani, S.4    Ybe, J.A.5
  • 42
    • 0035114361 scopus 로고    scopus 로고
    • Cytokinesis failure in clathrin-minus cells is caused by cleavage furrow instability
    • Gerald N.J., Damer CK, O'Halloran TJ, De Lozanne A. 2001. Cytokinesis failure in clathrin-minus cells is caused by cleavage furrow instability. Cell Motil Cytoskeleton 48: 213-223.
    • (2001) Cell Motil Cytoskeleton , vol.48 , pp. 213-223
    • Gerald, N.J.1    Damer, C.K.2    O'Halloran, T.J.3    De Lozanne, A.4
  • 44
    • 84870436293 scopus 로고    scopus 로고
    • ESCRT-II's involvement in HIV-1 genomic RNA trafficking and assembly
    • Ghoujal B., Milev MP, Ajamian L, Abel K, Mouland AJ. 2012. ESCRT-II's involvement in HIV-1 genomic RNA trafficking and assembly. Biol Cell 104: 706-721.
    • (2012) Biol Cell , vol.104 , pp. 706-721
    • Ghoujal, B.1    Milev, M.P.2    Ajamian, L.3    Abel, K.4    Mouland, A.J.5
  • 45
    • 84897621664 scopus 로고    scopus 로고
    • The role of endocytosis during morphogenetic signaling
    • doi: 10.1101/cshperspect.a016881
    • Gonzalez-Gaitan M, Jülicher F. 2014. The role of endocytosis during morphogenetic signaling. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a016881.
    • (2014) Cold Spring Harb Perspect Biol
    • Gonzalez-Gaitan, M.1    Jülicher, F.2
  • 47
    • 0030199973 scopus 로고    scopus 로고
    • Control of daughter cell fates during asymmetric division: Interaction of Numb and Notch
    • Guo M., Jan LY, Jan YN. 1996. Control of daughter cell fates during asymmetric division: Interaction of Numb and Notch. Neuron 17: 27-41.
    • (1996) Neuron , vol.17 , pp. 27-41
    • Guo, M.1    Jan, L.Y.2    Jan, Y.N.3
  • 51
    • 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 KK, Stefan CJ, Blumer K, Lemmon S.K. 1997. Novel functions of clathrin light chains: Clathrin heavy chain trimerization is defective in light chain-deficient yeast. J Cell Sci 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
  • 52
    • 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. 2004. Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference. J Biol Chem 279: 16657-16661.
    • (2004) J Biol Chem , vol.279 , pp. 16657-16661
    • Huang, F.1    Khvorova, A.2    Marshall, W.3    Sorkin, A.4
  • 54
    • 1642587778 scopus 로고    scopus 로고
    • HIP1: Trafficking roles and regulation of tumorigenesis
    • Hyun T.S., Ross TS. 2004. HIP1: Trafficking roles and regulation of tumorigenesis. Trends Mol Med 10: 194-199.
    • (2004) Trends Mol Med , vol.10 , pp. 194-199
    • Hyun, T.S.1    Ross, T.S.2
  • 56
    • 20444420188 scopus 로고    scopus 로고
    • Cytokinesis in higher plants
    • Jurgens G. 2005. Cytokinesis in higher plants. Annu Rev Plant Biol 56: 281-299.
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 281-299
    • Jurgens, G.1
  • 59
    • 61349119882 scopus 로고    scopus 로고
    • The preprophase band is a localized center of clathrin-mediated endocytosis in late prophase cells of the onion cotyledon epidermis
    • Karahara I., Suda J, Tahara H, Yokota E, Shimmen T, Misaki K, Yonemura S, Staehelin LA, Mineyuki Y. 2009. The preprophase band is a localized center of clathrin-mediated endocytosis in late prophase cells of the onion cotyledon epidermis. Plant J 57: 819-831.
    • (2009) Plant J , vol.57 , pp. 819-831
    • Karahara, I.1    Suda, J.2    Tahara, H.3    Yokota, E.4    Shimmen, T.5    Misaki, K.6    Yonemura, S.7    Staehelin, L.A.8    Mineyuki, Y.9
  • 61
    • 84899704909 scopus 로고    scopus 로고
    • Molecular structure, function and dynamics of clathrin-mediated membrane traffic
    • doi: 10.1101/cshperspect.a016725
    • Kirchhausen T, Owen D, Harrison SC. 2014. Molecular structure, function and dynamics of clathrin-mediated membrane traffic. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a016725.
    • (2014) Cold Spring Harb Perspect Biol
    • Kirchhausen, T.1    Owen, D.2    Harrison, S.C.3
  • 65
    • 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 JF, Philie J, Gan L, Hayden MR, McPherson PS. 2005. Huntingtin interacting protein 1 (HIP1) regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain. J Biol Chem 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
  • 66
    • 0035863193 scopus 로고    scopus 로고
    • A novel clathrin homolog that codistributes with cytoskeletal components functions in the trans-Golgi network
    • Liu S.H., Towler MC, Chen E, Chen CY, Song W, Apodaca G, Brodsky F.M. 2001. A novel clathrin homolog that codistributes with cytoskeletal components functions in the trans-Golgi network. EMBO J 20: 272-284.
    • (2001) EMBO J , vol.20 , pp. 272-284
    • Liu, S.H.1    Towler, M.C.2    Chen, E.3    Chen, C.Y.4    Song, W.5    Apodaca, G.6    Brodsky, F.M.7
  • 68
    • 69449086077 scopus 로고    scopus 로고
    • No strings attached: The ESCRTmachinery in viral budding and cytokinesis
    • McDonald B, Martin-Serrano J. 2009. No strings attached: The ESCRTmachinery in viral budding and cytokinesis. J Cell Sci 122: 2167-2177.
    • (2009) J Cell Sci , vol.122 , pp. 2167-2177
    • McDonald, B.1    Martin-Serrano, J.2
  • 69
    • 84875602814 scopus 로고    scopus 로고
    • Clathrin is not required for SNX-BAR-retromer-mediated carrier formation
    • McGough IJ, Cullen PJ. 2013. Clathrin is not required for SNX-BAR-retromer-mediated carrier formation. J Cell Sci 126: 45-52.
    • (2013) J Cell Sci , vol.126 , pp. 45-52
    • McGough, I.J.1    Cullen, P.J.2
  • 70
    • 79751508874 scopus 로고    scopus 로고
    • Life is a highway: Membrane trafficking during cytokinesis
    • McKay HF, Burgess DR. 2011. "Life is a highway": Membrane trafficking during cytokinesis. Traffic 12: 247-251.
    • (2011) Traffic , vol.12 , pp. 247-251
    • McKay, H.F.1    Burgess, D.R.2
  • 73
    • 84891657465 scopus 로고    scopus 로고
    • Endocytic accessory factors and regulation of clathrin-mediated endocytosis
    • doi: 10.1101/cshper spect.a016733
    • Merrifield CJ, Kaksonen M. 2014. Endocytic accessory factors and regulation of clathrin-mediated endocytosis. Cold Spring Harb Perspect Biol doi: 10.1101/cshper spect.a016733.
    • (2014) Cold Spring Harb Perspect Biol
    • Merrifield, C.J.1    Kaksonen, M.2
  • 75
    • 22944481528 scopus 로고    scopus 로고
    • Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors
    • Mills I.G., Gaughan L, Robson C, Ross T, McCracken S, Kelly J, Neal DE. 2005. Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors. J Cell Biol 170: 191-200.
    • (2005) J Cell Biol , vol.170 , pp. 191-200
    • Mills, I.G.1    Gaughan, L.2    Robson, C.3    Ross, T.4    McCracken, S.5    Kelly, J.6    Neal, D.E.7
  • 76
    • 0035824673 scopus 로고    scopus 로고
    • Clathrin-and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins
    • Mishra S.K., Agostinelli NR, Brett TJ, Mizukami I, Ross TS, Traub L.M. 2001. Clathrin-and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins. J Biol Chem 276: 46230-46236.
    • (2001) J Biol Chem , vol.276 , pp. 46230-46236
    • Mishra, S.K.1    Agostinelli, N.R.2    Brett, T.J.3    Mizukami, I.4    Ross, T.S.5    Traub, L.M.6
  • 77
    • 84885035853 scopus 로고    scopus 로고
    • Presynaptic membrane retrieval and endosome biology: Defining molecularly heterogeneous synaptic vesicles
    • Morgan JR, Comstra HS, Cohen M, Faundez V. 2013. Presynaptic membrane retrieval and endosome biology: Defining molecularly heterogeneous synaptic vesicles. Cold Spring Harb Perspect Biol 5: a016915.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • Morgan, J.R.1    Comstra, H.S.2    Cohen, M.3    Faundez, V.4
  • 78
    • 84859593755 scopus 로고    scopus 로고
    • Differential requirements of mammalian ESCRTs in multivesicular body formation, virus budding and cell division
    • Morita E. 2012. Differential requirements of mammalian ESCRTs in multivesicular body formation, virus budding and cell division. FEBS J 279: 1399-1406.
    • (2012) FEBS J , vol.279 , pp. 1399-1406
    • Morita, E.1
  • 79
    • 84860706719 scopus 로고    scopus 로고
    • CALM/AF10-positive leukemias show upregulation of genes involved in chromatin assembly and DNA repair processes and of genes adjacent to the breakpoint at 10p12
    • Mulaw M.A., Krause A, Deshpande AJ, Krause LF, Rouhi A, La Starza R, Borkhardt A, Buske C, Mecucci C, Ludwig WD, et al. 2012. CALM/AF10-positive leukemias show upregulation of genes involved in chromatin assembly and DNA repair processes and of genes adjacent to the breakpoint at 10p12. Leukemia 26: 1012-1019.
    • (2012) Leukemia , vol.26 , pp. 1012-1019
    • Mulaw, M.A.1    Krause, A.2    Deshpande, A.J.3    Krause, L.F.4    Rouhi, A.5    La Starza, R.6    Borkhardt, A.7    Buske, C.8    Mecucci, C.9    Ludwig, W.D.10
  • 80
    • 0033027052 scopus 로고    scopus 로고
    • Consistent detection of CALM-AF10 chimaeric transcripts in haematological malignancies with t(10;11)(p13;q14) and identification of novel transcripts
    • Narita M., Shimizu K, Hayashi Y, Taki T, Taniwaki M, Hosoda F, Kobayashi H, Nakamura H, Sadamori N, Ohnishi H, et al. 1999. Consistent detection of CALM-AF10 chimaeric transcripts in haematological malignancies with t(10;11)(p13;q14) and identification of novel transcripts. Br J Haematol 105: 928-937.
    • (1999) Br J Haematol , vol.105 , pp. 928-937
    • Narita, M.1    Shimizu, K.2    Hayashi, Y.3    Taki, T.4    Taniwaki, M.5    Hosoda, F.6    Kobayashi, H.7    Nakamura, H.8    Sadamori, N.9    Ohnishi, H.10
  • 81
    • 37549017337 scopus 로고    scopus 로고
    • Crystal structure at 2.8 Å of huntingtin-interacting protein 1 (HIP1) coiled-coil domain reveals a charged surface suitable for HIP1 protein interactor (HIPPI)
    • Niu Q., Ybe JA. 2008. Crystal structure at 2.8 Å of huntingtin-interacting protein 1 (HIP1) coiled-coil domain reveals a charged surface suitable for HIP1 protein interactor (HIPPI). J Mol Biol 375: 1197-1205.
    • (2008) J Mol Biol , vol.375 , pp. 1197-1205
    • Niu, Q.1    Ybe, J.A.2
  • 82
    • 41649120555 scopus 로고    scopus 로고
    • Monomeric but not trimeric clathrin heavy chain regulates p53-mediated transcription
    • Ohmori K., Endo Y, Yoshida Y, Ohata H, Taya Y, Enari M. 2008. Monomeric but not trimeric clathrin heavy chain regulates p53-mediated transcription. Oncogene 27: 2215-2227.
    • (2008) Oncogene , vol.27 , pp. 2215-2227
    • Ohmori, K.1    Endo, Y.2    Yoshida, Y.3    Ohata, H.4    Taya, Y.5    Enari, M.6
  • 84
    • 0016834909 scopus 로고
    • Coated vesicles from pig brain: Purification and biochemical characterization
    • Pearse B.M.F. 1975. Coated vesicles from pig brain: Purification and biochemical characterization. J Mol Biol 97: 93-98.
    • (1975) J Mol Biol , vol.97 , pp. 93-98
    • Pearse, B.M.F.1
  • 88
    • 75749110614 scopus 로고    scopus 로고
    • Mechanics of cytokinesis in eukaryotes
    • Pollard T.D. 2010. Mechanics of cytokinesis in eukaryotes. Curr Opin Cell Biol 22: 50-56.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 50-56
    • Pollard, T.D.1
  • 92
    • 0034780505 scopus 로고    scopus 로고
    • Huntingtin interacting protein 1 is a clathrin coat binding protein required for differentiation of late spermatogenic progenitors
    • Rao D.S., Chang JC, Kumar PD, Mizukami I, Smithson GM, Bradley S.V., Parlow AF, Ross TS. 2001. Huntingtin interacting protein 1 is a clathrin coat binding protein required for differentiation of late spermatogenic progenitors. Mol Cell Biol 21: 7796-7806.
    • (2001) Mol Cell Biol , vol.21 , pp. 7796-7806
    • Rao, D.S.1    Chang, J.C.2    Kumar, P.D.3    Mizukami, I.4    Smithson, G.M.5    Bradley, S.V.6    Parlow, A.F.7    Ross, T.S.8
  • 93
    • 67650540827 scopus 로고    scopus 로고
    • Endosomal adaptor proteins APPL1 and APPL2 are novel activators of β-catenin/ TCF-mediated transcription
    • Rashid S., Pilecka I, Torun A, Olchowik M, Bielinska B, Miaczynska M. 2009. Endosomal adaptor proteins APPL1 and APPL2 are novel activators of β-catenin/ TCF-mediated transcription. J Biol Chem 284: 18115-18128.
    • (2009) J Biol Chem , vol.284 , pp. 18115-18128
    • Rashid, S.1    Pilecka, I.2    Torun, A.3    Olchowik, M.4    Bielinska, B.5    Miaczynska, M.6
  • 94
    • 10344258588 scopus 로고    scopus 로고
    • HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail
    • Roeth J.F., Williams M, Kasper MR, Filzen TM, Collins KL. 2004. HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail. J Cell Biol 167: 903-913.
    • (2004) J Cell Biol , vol.167 , pp. 903-913
    • Roeth, J.F.1    Williams, M.2    Kasper, M.R.3    Filzen, T.M.4    Collins, K.L.5
  • 95
    • 0031864246 scopus 로고    scopus 로고
    • Fusion of huntingtin interacting protein 1 to platelet-derived growth factor β receptor (PDGFβR) in chronic myelomonocytic leukemia with t(5;7)(q33;q11.2)
    • Ross T.S., Bernard OA, Berger R, Gilliland DG. 1998. Fusion of huntingtin interacting protein 1 to platelet-derived growth factor β receptor (PDGFβR) in chronic myelomonocytic leukemia with t(5;7)(q33;q11.2). Blood 91: 4419-4426.
    • (1998) Blood , vol.91 , pp. 4419-4426
    • Ross, T.S.1    Bernard, O.A.2    Berger, R.3    Gilliland, D.G.4
  • 96
    • 84858143588 scopus 로고    scopus 로고
    • The role of clathrin in mitotic spindle organisation
    • Royle S.J. 2012. The role of clathrin in mitotic spindle organisation. J Cell Sci 125: 19-28.
    • (2012) J Cell Sci , vol.125 , pp. 19-28
    • Royle, S.J.1
  • 97
    • 17844394685 scopus 로고    scopus 로고
    • Clathrin is required for the function of the mitotic spindle
    • Royle S.J., Bright NA, Lagnado L. 2005. Clathrin is required for the function of the mitotic spindle. Nature 434: 1152-1157.
    • (2005) Nature , vol.434 , pp. 1152-1157
    • Royle, S.J.1    Bright, N.A.2    Lagnado, L.3
  • 98
    • 70349764506 scopus 로고    scopus 로고
    • Distinct dynamics of endocytic clathrin-coated pits and coated plaques
    • Saffarian S., Cocucci E, Kirchhausen T. 2009. Distinct dynamics of endocytic clathrin-coated pits and coated plaques. PLoS Biol 7: e1000191.
    • (2009) PLoS Biol , vol.7
    • Saffarian, S.1    Cocucci, E.2    Kirchhausen, T.3
  • 100
    • 75749096347 scopus 로고    scopus 로고
    • The endocytic matrix
    • Scita G., Di Fiore PP. 2010. The endocytic matrix. Nature 463: 464-473.
    • (2010) Nature , vol.463 , pp. 464-473
    • Scita, G.1    Di Fiore, P.P.2
  • 101
    • 84873263347 scopus 로고    scopus 로고
    • Clathrin-mediated endocytic proteins are involved in regulating mitotic progression and completion
    • Smith C.M., Chircop M. 2012. Clathrin-mediated endocytic proteins are involved in regulating mitotic progression and completion. Traffic 13: 1628-1641.
    • (2012) Traffic , vol.13 , pp. 1628-1641
    • Smith, C.M.1    Chircop, M.2
  • 102
    • 33845397660 scopus 로고    scopus 로고
    • The monomeric clathrin assembly protein, AP180, regulates contractile vacuole size in Dictyostelium discoideum
    • Stavrou I., O'Halloran TJ. 2006. The monomeric clathrin assembly protein, AP180, regulates contractile vacuole size in Dictyostelium discoideum. Mol Biol Cell 17: 5381-5389.
    • (2006) Mol Biol Cell , vol.17 , pp. 5381-5389
    • Stavrou, I.1    O'Halloran, T.J.2
  • 103
    • 0036800489 scopus 로고    scopus 로고
    • Lipid rafts unite signaling cascades with clathrin to regulate BCR internalization
    • Stoddart A., Dykstra ML, Brown BK, Song W, Pierce SK, Brodsky F.M. 2002. Lipid rafts unite signaling cascades with clathrin to regulate BCR internalization. Immunity 17: 451-462.
    • (2002) Immunity , vol.17 , pp. 451-462
    • Stoddart, A.1    Dykstra, M.L.2    Brown, B.K.3    Song, W.4    Pierce, S.K.5    Brodsky, F.M.6
  • 105
    • 33847775787 scopus 로고    scopus 로고
    • Clathrin is involved in organization of mitotic spindle and phragmoplast as well as in endocytosis in tobacco cell cultures
    • Tahara H., Yokota E, Igarashi H, Orii H, Yao M, Sonobe S, Hashimoto T., Hussey PJ, Shimmen T. 2007. Clathrin is involved in organization of mitotic spindle and phragmoplast as well as in endocytosis in tobacco cell cultures. Protoplasma 230: 1-11.
    • (2007) Protoplasma , vol.230 , pp. 1-11
    • Tahara, H.1    Yokota, E.2    Igarashi, H.3    Orii, H.4    Yao, M.5    Sonobe, S.6    Hashimoto, T.7    Hussey, P.J.8    Shimmen, T.9
  • 106
    • 0032807691 scopus 로고    scopus 로고
    • Clathrin assembly lymphoid myeloid leukemia (CALM) protein: Localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic
    • Tebar F., Bohlander SK, Sorkin A. 1999. Clathrin assembly lymphoid myeloid leukemia (CALM) protein: Localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic. Mol Biol Cell 10: 2687-2702.
    • (1999) Mol Biol Cell , vol.10 , pp. 2687-2702
    • Tebar, F.1    Bohlander, S.K.2    Sorkin, A.3
  • 107
    • 84889050260 scopus 로고    scopus 로고
    • MHCclass II antigen presentation by dendritic cells regulated through endosomal sorting
    • ten Broeke T, Wubbolts R, Stoorvogel W. 2013. MHCclass II antigen presentation by dendritic cells regulated through endosomal sorting. Cold Spring Harb Perspect Biol 5: a016873.
    • (2013) Cold Spring Harb Perspect Biol , vol.5
    • ten Broeke, T.1    Wubbolts, R.2    Stoorvogel, W.3
  • 108
    • 3042806469 scopus 로고    scopus 로고
    • Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration
    • Towler M.C., Gleeson PA, Hoshino S, Rahkila P, Manalo V, Ohkoshi N., Ordahl C, Parton RG, Brodsky FM. 2004. Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration. Mol Biol Cell 15: 3181-3195.
    • (2004) Mol Biol Cell , vol.15 , pp. 3181-3195
    • Towler, M.C.1    Gleeson, P.A.2    Hoshino, S.3    Rahkila, P.4    Manalo, V.5    Ohkoshi, N.6    Ordahl, C.7    Parton, R.G.8    Brodsky, F.M.9
  • 112
    • 0348013274 scopus 로고    scopus 로고
    • Compromise of clathrin function and membrane association by clathrin light chain deletion
    • Wang J., Virta VC, Riddelle-Spencer K, O'Halloran TJ. 2003. Compromise of clathrin function and membrane association by clathrin light chain deletion. Traffic 4: 891-901.
    • (2003) Traffic , vol.4 , pp. 891-901
    • Wang, J.1    Virta, V.C.2    Riddelle-Spencer, K.3    O'Halloran, T.J.4
  • 114
    • 33645112128 scopus 로고    scopus 로고
    • Dynamics of membrane clathrin-coated structures during cytokinesis
    • Warner A.K., Keen JH, Wang YL. 2006. Dynamics of membrane clathrin-coated structures during cytokinesis. Traffic 7: 205-215.
    • (2006) Traffic , vol.7 , pp. 205-215
    • Warner, A.K.1    Keen, J.H.2    Wang, Y.L.3
  • 115
    • 34248229690 scopus 로고    scopus 로고
    • More than one door-Budding of enveloped viruses through cellular membranes
    • Welsch S., Muller B, Krausslich HG. 2007. More than one door-Budding of enveloped viruses through cellular membranes. FEBS Lett 581: 2089-2097.
    • (2007) FEBS Lett , vol.581 , pp. 2089-2097
    • Welsch, S.1    Muller, B.2    Krausslich, H.G.3
  • 116
    • 77649119002 scopus 로고    scopus 로고
    • Accommodation of structural rearrangements in the huntingtin-interacting protein 1 coiled-coil domain
    • Wilbur J.D., Hwang PK, Brodsky FM, Fletterick RJ. 2010a. Accommodation of structural rearrangements in the huntingtin-interacting protein 1 coiled-coil domain. Acta Crystallogr D Biol Crystallogr 66: 314-318.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 314-318
    • Wilbur, J.D.1    Hwang, P.K.2    Brodsky, F.M.3    Fletterick, R.J.4
  • 118
    • 0033525759 scopus 로고    scopus 로고
    • EGF receptor signaling stimulates SRC kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake
    • Wilde A., Beattie EC, Lem L, Riethof DA, Liu SH, Mobley WC, Soriano P, Brodsky FM. 1999. EGF receptor signaling stimulates SRC kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake. Cell 96: 677-687.
    • (1999) Cell , vol.96 , pp. 677-687
    • Wilde, A.1    Beattie, E.C.2    Lem, L.3    Riethof, D.A.4    Liu, S.H.5    Mobley, W.C.6    Soriano, P.7    Brodsky, F.M.8
  • 120
    • 52949115363 scopus 로고    scopus 로고
    • Linking cell cycle to asymmetric division: Aurora-A phosphorylates the Par complex to regulate Numb localization
    • Wirtz-Peitz F., Nishimura T, Knoblich JA. 2008. Linking cell cycle to asymmetric division: Aurora-A phosphorylates the Par complex to regulate Numb localization. Cell 135: 161-173.
    • (2008) Cell , vol.135 , pp. 161-173
    • Wirtz-Peitz, F.1    Nishimura, T.2    Knoblich, J.A.3
  • 121
    • 0348013276 scopus 로고    scopus 로고
    • Contribution of cysteines to clathrin trimerization domain stability and mapping of light chain binding
    • Ybe J.A., Ruppel N, Mishra S, Van Haaften E. 2003. Contribution of cysteines to clathrin trimerization domain stability and mapping of light chain binding. Traffic 4: 850-856.
    • (2003) Traffic , vol.4 , pp. 850-856
    • Ybe, J.A.1    Ruppel, N.2    Mishra, S.3    Van Haaften, E.4
  • 122
    • 33847041161 scopus 로고    scopus 로고
    • Crystal structure at 2.8 Å of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding
    • Ybe J.A., Mishra S, Helms S, Nix J. 2007a. Crystal structure at 2.8 Å of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding. J Mol Biol 367: 8-15.
    • (2007) J Mol Biol , vol.367 , pp. 8-15
    • Ybe, J.A.1    Mishra, S.2    Helms, S.3    Nix, J.4
  • 123
    • 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 DA, Drazer MW, Clegg ME. 2007b. Light chain C-terminal region reinforces the stability of clathrin heavy chain trimers. Traffic 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
  • 124
    • 77950999602 scopus 로고    scopus 로고
    • Two distantly spaced basic patches in the flexible domain of huntingtin-interacting protein 1 (HIP1) are essential for the binding of clathrin light chain
    • Ybe J.A., Clegg ME, Illingworth M, Gonzalez C, Niu Q. 2009. Two distantly spaced basic patches in the flexible domain of huntingtin-interacting protein 1 (HIP1) are essential for the binding of clathrin light chain. Res Lett Biochem 2009: 256124.
    • (2009) Res Lett Biochem , vol.2009 , pp. 256124
    • Ybe, J.A.1    Clegg, M.E.2    Illingworth, M.3    Gonzalez, C.4    Niu, Q.5
  • 125
    • 84872100799 scopus 로고    scopus 로고
    • Nuclear localization of clathrin involves a labile helix outside the trimerization domain
    • Ybe J.A., Fontaine SN, Stone T, Nix J, Lin X, Mishra S. 2013. Nuclear localization of clathrin involves a labile helix outside the trimerization domain. FEBS Lett 587: 142-149.
    • (2013) FEBS Lett , vol.587 , pp. 142-149
    • Ybe, J.A.1    Fontaine, S.N.2    Stone, T.3    Nix, J.4    Lin, X.5    Mishra, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.