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Volumn 29, Issue 6, 2010, Pages 1033-1044

Regulation of clathrin adaptor function in endocytosis: Novel role for the SAM domain

Author keywords

Adaptor; Clathrin; Endocytosis; SAM domain; Sla1

Indexed keywords

CLATHRIN;

EID: 77949566571     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2010.5     Document Type: Article
Times cited : (37)

References (51)
  • 1
    • 0032934806 scopus 로고    scopus 로고
    • Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology
    • Ayscough KR, Eby JJ, Lila T, Dewar H, Kozminski KG, Drubin DG (1999) Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology. Mol Biol Cell 10: 1061-1075
    • (1999) Mol Biol Cell , vol.10 , pp. 1061-1075
    • Ayscough, K.R.1    Eby, J.J.2    Lila, T.3    Dewar, H.4    Kozminski, K.G.5    Drubin, D.G.6
  • 3
    • 33745764441 scopus 로고    scopus 로고
    • Molecular structures of coat and coat-associated proteins: Function follows form
    • Brett TJ, Traub LM (2006) Molecular structures of coat and coat-associated proteins: function follows form. Curr Opin Cell Biol 18: 395-406
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 395-406
    • Brett, T.J.1    Traub, L.M.2
  • 5
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner SD, Schmid SL (2003) Regulated portals of entry into the cell. Nature 422: 37-44
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 6
    • 0035166326 scopus 로고    scopus 로고
    • Yeast Gga coat proteins function with clathrin in Golgi to endosome transport
    • Costaguta G, Stefan CJ, Bensen ES, Emr SD, Payne GS (2001) Yeast Gga coat proteins function with clathrin in Golgi to endosome transport. Mol Biol Cell 12: 1885-1896
    • (2001) Mol Biol Cell , vol.12 , pp. 1885-1896
    • Costaguta, G.1    Stefan, C.J.2    Bensen, E.S.3    Emr, S.D.4    Payne, G.S.5
  • 8
    • 0035425192 scopus 로고    scopus 로고
    • Clathrin-binding proteins: Got a motif? Join the network!
    • Dell'Angelica EC (2001) Clathrin-binding proteins: got a motif? Join the network!. Trends Cell Biol 11: 315-318
    • (2001) Trends Cell Biol , vol.11 , pp. 315-318
    • Dell'Angelica, E.C.1
  • 12
    • 1842588760 scopus 로고    scopus 로고
    • Characterization of BLOC-2, a complex containing the Hermansky-Pudlak syndrome proteins HPS3, HPS5 and HPS6
    • Di Pietro SM, Falcon-Perez JM, Dell'Angelica EC (2004) Characterization of BLOC-2, a complex containing the Hermansky-Pudlak syndrome proteins HPS3, HPS5 and HPS6. T r a ffi c 5: 276-283
    • (2004) Traffic , vol.5 , pp. 276-283
    • Di Pietro, S.M.1    Falcon-Perez, J.M.2    Dell'Angelica, E.C.3
  • 14
    • 0035800840 scopus 로고    scopus 로고
    • Interaction of two structurally distinct sequence types with the clathrin terminal domain beta-propeller
    • Drake MT, Traub LM (2001) Interaction of two structurally distinct sequence types with the clathrin terminal domain beta-propeller. J Biol Chem 276: 28700-28709
    • (2001) J Biol Chem , vol.276 , pp. 28700-28709
    • Drake, M.T.1    Traub, L.M.2
  • 16
    • 30844453760 scopus 로고    scopus 로고
    • Life of a clathrin coat: Insights from clathrin and AP structures
    • Edeling MA, Smith C, Owen D (2006) Life of a clathrin coat: insights from clathrin and AP structures. Nat Rev Mol Cell Biol 7: 32-44
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 32-44
    • Edeling, M.A.1    Smith, C.2    Owen, D.3
  • 17
    • 34247615569 scopus 로고    scopus 로고
    • Bidirectional Eph-ephrin signaling during axon guidance
    • Egea J, Klein R (2007) Bidirectional Eph-ephrin signaling during axon guidance. Trends Cell Biol 17: 230-238
    • (2007) Trends Cell Biol , vol.17 , pp. 230-238
    • Egea, J.1    Klein, R.2
  • 18
    • 0037008731 scopus 로고    scopus 로고
    • BLOC-1, a novel complex containing the pallidin and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules
    • Falcon-Perez JM, Starcevic M, Gautam R, Dell'Angelica EC (2002) BLOC-1, a novel complex containing the pallidin and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules. J Biol Chem 277: 28191-28199
    • (2002) J Biol Chem , vol.277 , pp. 28191-28199
    • Falcon-Perez, J.M.1    Starcevic, M.2    Gautam, R.3    Dell'Angelica, E.C.4
  • 19
    • 0033545203 scopus 로고    scopus 로고
    • Coronin promotes the rapid assembly and cross-linking of actin filaments and may link the actin and microtubule cytoskeletons in yeast
    • Goode BL, Wong JJ, Butty AC, Peter M, McCormack AL, Yates JR, Drubin DG, Barnes G (1999) Coronin promotes the rapid assembly and cross-linking of actin filaments and may link the actin and microtubule cytoskeletons in yeast. J Cell Biol 144: 83-98
    • (1999) J Cell Biol , vol.144 , pp. 83-98
    • Goode, B.L.1    Wong, J.J.2    Butty, A.C.3    Peter, M.4    McCormack, A.L.5    Yates, J.R.6    Drubin, D.G.7    Barnes, G.8
  • 20
    • 0038159267 scopus 로고    scopus 로고
    • An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast
    • Gourlay CW, Dewar H, Warren DT, Costa R, Satish N, Ayscough KR (2003) An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast. J Cell Sci 11 6 (Pt 12): 2551-2564
    • (2003) J Cell Sci , vol.11 , Issue.6 PART 12 , pp. 2551-2564
    • Gourlay, C.W.1    Dewar, H.2    Warren, D.T.3    Costa, R.4    Satish, N.5    Ayscough, K.R.6
  • 22
    • 0037092043 scopus 로고    scopus 로고
    • Sla1p serves as the targeting signal recognition factor for NPFX(1, 2)D-mediated endocytosis
    • Howard JP, Hutton JL, Olson JM, Payne GS (2002) Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis. J Cell Biol 157: 315-326
    • (2002) J Cell Biol , vol.157 , pp. 315-326
    • Howard, J.P.1    Hutton, J.L.2    Olson, J.M.3    Payne, G.S.4
  • 23
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H, Fukuda Y, Murata K, Kimura A (1983) Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153: 163-168
    • (1983) J Bacteriol , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 24
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • Kaksonen M, Sun Y, Drubin DG (2003) A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115: 475-487
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 25
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin-and actin-mediated endocytosis machinery
    • Kaksonen M, Toret CP, Drubin DG (2005) A modular design for the clathrin-and actin-mediated endocytosis machinery. Cell 123: 305-320
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 28
    • 0036704540 scopus 로고    scopus 로고
    • Clathrin-protein interactions
    • Lafer EM (2002) Clathrin-protein interactions. Traffic 3: 513-520
    • (2002) Traffic , vol.3 , pp. 513-520
    • Lafer, E.M.1
  • 29
    • 20544432791 scopus 로고    scopus 로고
    • Cell wall integrity signaling in Saccharomyces cerevisiae
    • Levin DE (2005) Cell wall integrity signaling in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 69: 262-291
    • (2005) Microbiol Mol Biol Rev , vol.69 , pp. 262-291
    • Levin, D.E.1
  • 30
    • 0031045512 scopus 로고    scopus 로고
    • Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton
    • Li R (1997) Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. J Cell Biol 136: 649-658
    • (1997) J Cell Biol , vol.136 , pp. 649-658
    • Li, R.1
  • 31
    • 34247243351 scopus 로고    scopus 로고
    • Structure of Sla1p homology domain 1 and interaction with the NPFxD endocytic internalization motif
    • Mahadev RK, Di Pietro SM, Olson JM, Piao HL, Payne GS, Overduin M (2007) Structure of Sla1p homology domain 1 and interaction with the NPFxD endocytic internalization motif. EMBO J 26: 1963-1971
    • (2007) EMBO J , vol.26 , pp. 1963-1971
    • Mahadev, R.K.1    Di Pietro, S.M.2    Olson, J.M.3    Piao, H.L.4    Payne, G.S.5    Overduin, M.6
  • 32
    • 33748969492 scopus 로고    scopus 로고
    • Endocytic adaptors: Recruiters, coordinators and regulators
    • Maldonado-Baez L, Wendland B (2006) Endocytic adaptors: recruiters, coordinators and regulators. Trends Cell Biol 16: 505-513
    • (2006) Trends Cell Biol , vol.16 , pp. 505-513
    • Maldonado-Baez, L.1    Wendland, B.2
  • 33
    • 1442335990 scopus 로고    scopus 로고
    • Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller
    • Miele AE, Watson PJ, Evans PR, Traub LM, Owen DJ (2004) Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller. Nat Struct Mol Biol 11: 242-248
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 242-248
    • Miele, A.E.1    Watson, P.J.2    Evans, P.R.3    Traub, L.M.4    Owen, D.J.5
  • 34
    • 0035170896 scopus 로고    scopus 로고
    • Structural requirements for function of yeast GGAs in vacuolar protein sorting, alpha-factor maturation, and interactions with clathrin
    • Mullins C, Bonifacino JS (2001) Structural requirements for function of yeast GGAs in vacuolar protein sorting, alpha-factor maturation, and interactions with clathrin. Mol Cell Biol 21: 7981-7994
    • (2001) Mol Cell Biol , vol.21 , pp. 7981-7994
    • Mullins, C.1    Bonifacino, J.S.2
  • 35
    • 33846053104 scopus 로고    scopus 로고
    • NPFXD-mediated endocy-tosis is required for polarity and function of a yeast cell wall stress sensor
    • Piao HL, Machado IM, Payne GS (2007) NPFXD-mediated endocy-tosis is required for polarity and function of a yeast cell wall stress sensor. Mol Biol Cell 18: 57-65
    • (2007) Mol Biol Cell , vol.18 , pp. 57-65
    • Piao, H.L.1    MacHado, I.M.2    Payne, G.S.3
  • 38
    • 0031746484 scopus 로고    scopus 로고
    • Multiple amphiphysin II splice variants display differential clathrin binding: Identification of two distinct clathrin-binding sites
    • Ramjaun AR, McPherson PS (1998) Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites. J Neurochem 70: 2369-2376
    • (1998) J Neurochem , vol.70 , pp. 2369-2376
    • Ramjaun, A.R.1    McPherson, P.S.2
  • 39
    • 34548176765 scopus 로고    scopus 로고
    • Integrating molecular and network biology to decode endocytosis
    • Schmid EM, McMahon HT (2007) Integrating molecular and network biology to decode endocytosis. Nature 448: 883-888
    • (2007) Nature , vol.448 , pp. 883-888
    • Schmid, E.M.1    McMahon, H.T.2
  • 40
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski RS, Hieter P (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 41
    • 0034625338 scopus 로고    scopus 로고
    • Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites
    • Slepnev VI, Ochoa GC, Butler MH, De Camilli P (2000) Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites. J Biol Chem 275: 17583-17589
    • (2000) J Biol Chem , vol.275 , pp. 17583-17589
    • Slepnev, V.I.1    Ochoa, G.C.2    Butler, M.H.3    De Camilli, P.4
  • 42
    • 0033622305 scopus 로고    scopus 로고
    • Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis
    • Tang HY, Xu J, Cai M (2000) Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis. Mol Cell Biol 20: 12-25
    • (2000) Mol Cell Biol , vol.20 , pp. 12-25
    • Tang, H.Y.1    Xu, J.2    Cai, M.3
  • 43
    • 0033967923 scopus 로고    scopus 로고
    • Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin
    • Ter Haar E, Harrison SC, Kirchhausen T (2000) Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin. Proc Natl Acad Sci USA 97: 1096-1100
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1096-1100
    • Ter Haar, E.1    Harrison, S.C.2    Kirchhausen, T.3
  • 44
    • 20544465126 scopus 로고    scopus 로고
    • Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane
    • Traub LM (2005) Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane. Biochim Biophys Acta 1744: 415-437
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 415-437
    • Traub, L.M.1
  • 45
    • 34547969807 scopus 로고    scopus 로고
    • Endocytosis: Clathrin-mediated membrane budding
    • Ungewickell EJ, Hinrichsen L (2007) Endocytosis: clathrin-mediated membrane budding. Curr Opin Cell Biol 19: 417-425
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 417-425
    • Ungewickell, E.J.1    Hinrichsen, L.2
  • 46
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida TA, Emr SD (1995) A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J Cell Biol 128: 779-792
    • (1995) J Cell Biol , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 48
    • 0037089086 scopus 로고    scopus 로고
    • Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics
    • Warren DT, Andrews PD, Gourlay CW, Ayscough KR (2002) Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics. J Cell Sci 11 5 (Pt 8): 1703-1715
    • (2002) J Cell Sci , vol.11 , Issue.5 PART 8 , pp. 1703-1715
    • Warren, D.T.1    Andrews, P.D.2    Gourlay, C.W.3    Ayscough, K.R.4
  • 49
    • 15844419751 scopus 로고    scopus 로고
    • New faces of the familiar clathrin lattice
    • Wilbur JD, Hwang PK, Brodsky FM (2005) New faces of the familiar clathrin lattice. Traffic 6: 346-350
    • (2005) Traffic , vol.6 , pp. 346-350
    • Wilbur, J.D.1    Hwang, P.K.2    Brodsky, F.M.3
  • 50
    • 56149108155 scopus 로고    scopus 로고
    • ARAP1 regulates endocytosis of EGFR
    • Yoon HY, Lee JS, Randazzo PA (2008) ARAP1 regulates endocytosis of EGFR. Traffic 9: 2236-2252
    • (2008) Traffic , vol.9 , pp. 2236-2252
    • Yoon, H.Y.1    Lee, J.S.2    Randazzo, P.A.3
  • 51
    • 34047268925 scopus 로고    scopus 로고
    • Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphati-dylinositol 3-kinase-dependent Rac1 activation
    • Zhuang G, Hunter S, Hwang Y, Chen J (2007) Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphati-dylinositol 3-kinase-dependent Rac1 activation. J Biol Chem 282: 2683-2694
    • (2007) J Biol Chem , vol.282 , pp. 2683-2694
    • Zhuang, G.1    Hunter, S.2    Hwang, Y.3    Chen, J.4


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