메뉴 건너뛰기




Volumn 123, Issue 3, 2010, Pages 460-471

Functional characterization of protein-sorting machineries at the trans-Golgi network in Drosophila melanogaster

Author keywords

AP 1; CIMPR; Clathrin; GGA; Lerp; Lysosome

Indexed keywords

ADAPTOR PROTEIN; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; CLATHRIN; DROSOPHILA PROTEIN; GUANOSINE TRIPHOSPHATASE; LYSOSOMAL ENZYME RECEPTOR PROTEIN; LYSOSOME ENZYME; MANNOSE 6 PHOSPHATE; UNCLASSIFIED DRUG;

EID: 76649090601     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.055103     Document Type: Article
Times cited : (28)

References (53)
  • 1
    • 2342420937 scopus 로고    scopus 로고
    • GGA1 interacts with the adaptor protein AP-1 through a WNSF sequence in its hinge region
    • Bai, H., Doray, B. and Kornfeld, S. (2004). GGA1 interacts with the adaptor protein AP-1 through a WNSF sequence in its hinge region. J. Biol. Chem. 279, 17411-17417.
    • (2004) J. Biol. Chem , vol.279 , pp. 17411-17417
    • Bai, H.1    Doray, B.2    Kornfeld, S.3
  • 2
    • 0034735540 scopus 로고    scopus 로고
    • A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins
    • Black, M. W. and Pelham, H. R. (2000). A selective transport route from Golgi to late endosomes that requires the yeast GGA proteins. J. Cell Biol. 151, 587-600.
    • (2000) J. Cell Biol , vol.151 , pp. 587-600
    • Black, M.W.1    Pelham, H.R.2
  • 3
    • 0035158494 scopus 로고    scopus 로고
    • Adaptins: The final recount
    • Boehm, M. and Bonifacino, J. S. (2001). Adaptins: the final recount. Mol. Biol. Cell 12, 2907-2920.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2907-2920
    • Boehm, M.1    Bonifacino, J.S.2
  • 4
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: Adaptors on the move
    • Bonifacino, J. S. (2004). The GGA proteins: adaptors on the move. Nat. Rev. Mol. Cell. Biol. 5, 23-32.
    • (2004) Nat. Rev. Mol. Cell. Biol , vol.5 , pp. 23-32
    • Bonifacino, J.S.1
  • 6
    • 34247129671 scopus 로고    scopus 로고
    • Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor
    • Chaudhuri, R., Lindwasser, O. W., Smith, W. J., Hurley, J. H. and Bonifacino, J. S. (2007). Downregulation of CD4 by human immunodeficiency virus type 1 Nef 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
  • 7
    • 0035166326 scopus 로고    scopus 로고
    • Yeast Gga coat proteins function with clathrin in Golgi to endosome transport
    • Costaguta, G., Stefan, C. J., Bensen, E. S., Emr, S. D. and Payne, G. S. (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
  • 9
    • 69949152537 scopus 로고    scopus 로고
    • Gga2 mediates sequential ubiquitin-independent and ubiquitin-dependent steps in the trafficking of ARN1 from the trans-Golgi network to the vacuole
    • Deng, Y., Guo, Y., Watson, H., Au, W. C., Shakoury-Elizeh, M., Basrai, M. A., Bonifacino, J. S. and Philpott, C. C. (2009). Gga2 mediates sequential ubiquitin-independent and ubiquitin-dependent steps in the trafficking of ARN1 from the trans-Golgi network to the vacuole. J. Biol. Chem. 284, 23830-23841.
    • (2009) J. Biol. Chem , vol.284 , pp. 23830-23841
    • Deng, Y.1    Guo, Y.2    Watson, H.3    Au, W.C.4    Shakoury-Elizeh, M.5    Basrai, M.A.6    Bonifacino, J.S.7    Philpott, C.C.8
  • 10
    • 16844380274 scopus 로고    scopus 로고
    • The novel Drosophila lysosomal enzyme receptor protein mediates lysosomal sorting in mammalian cells and binds mammalian and Drosophila GGA adaptors
    • Dennes, A., Cromme, C., Suresh, K., Kumar, N. S., Eble, J. A., Hahnenkamp, A. and Pohlmann, R. (2005). The novel Drosophila lysosomal enzyme receptor protein mediates lysosomal sorting in mammalian cells and binds mammalian and Drosophila GGA adaptors. J. Biol. Chem. 280, 12849-12857.
    • (2005) J. Biol. Chem , vol.280 , pp. 12849-12857
    • Dennes, A.1    Cromme, C.2    Suresh, K.3    Kumar, N.S.4    Eble, J.A.5    Hahnenkamp, A.6    Pohlmann, R.7
  • 11
    • 0037166331 scopus 로고    scopus 로고
    • Interaction of the cation-dependent mannose 6-phosphate receptor with GGA proteins
    • Doray, B., Bruns, K., Ghosh, P. and Kornfeld, S. (2002a). Interaction of the cation-dependent mannose 6-phosphate receptor with GGA proteins. J. Biol. Chem. 277, 18477-18482.
    • (2002) J. Biol. Chem , vol.277 , pp. 18477-18482
    • Doray, B.1    Bruns, K.2    Ghosh, P.3    Kornfeld, S.4
  • 12
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • Doray, B., Ghosh, P., Griffith, J., Geuze, H. J. and Kornfeld, S. (2002b). Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science 297, 1700-1703.
    • (2002) Science , vol.297 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.J.4    Kornfeld, S.5
  • 13
    • 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. and Kornfeld, S. A. (2002c). Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif. Proc. Natl. Acad. Sci. USA 99, 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
  • 14
    • 33745601971 scopus 로고    scopus 로고
    • Laa1p, a conserved AP-1 accessory protein important for AP-1 localization in yeast
    • Fernandez, G. E. and Payne, G. S. (2006). Laa1p, a conserved AP-1 accessory protein important for AP-1 localization in yeast. Mol. Biol. Cell 17, 3304-3317.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3304-3317
    • Fernandez, G.E.1    Payne, G.S.2
  • 15
    • 2542449272 scopus 로고    scopus 로고
    • The cytoplasmic tail of the cation-independent mannose 6-phosphate receptor contains four binding sites for AP-1
    • Ghosh, P. and Kornfeld, S. (2004). The cytoplasmic tail of the cation-independent mannose 6-phosphate receptor contains four binding sites for AP-1. Arch. Biochem. Biophys. 426, 225-230.
    • (2004) Arch. Biochem. Biophys , vol.426 , pp. 225-230
    • Ghosh, P.1    Kornfeld, S.2
  • 16
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: New twists in the tale
    • Ghosh, P., Dahms, N. M. and Kornfeld, S. (2003a). Mannose 6-phosphate receptors: new twists in the tale. Nat. Rev. Mol. Cell. Biol. 4, 202-212.
    • (2003) Nat. Rev. Mol. Cell. Biol , vol.4 , pp. 202-212
    • Ghosh, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 17
    • 0344304559 scopus 로고    scopus 로고
    • Mammalian GGAs act together to sort mannose 6-phosphate receptors
    • Ghosh, P., Griffith, J., Geuze, H. J. and Kornfeld, S. (2003b). Mammalian GGAs act together to sort mannose 6-phosphate receptors. J. Cell Biol. 163, 755-766.
    • (2003) J. Cell Biol , vol.163 , pp. 755-766
    • Ghosh, P.1    Griffith, J.2    Geuze, H.J.3    Kornfeld, S.4
  • 20
    • 0034599537 scopus 로고    scopus 로고
    • A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome
    • Hirst, J., Lui, W. W., Bright, N. A., Totty, N., Seaman, M. N. and Robinson, M. S. (2000). A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome. J. Cell Biol. 149, 67-80.
    • (2000) J. Cell Biol , vol.149 , pp. 67-80
    • Hirst, J.1    Lui, W.W.2    Bright, N.A.3    Totty, N.4    Seaman, M.N.5    Robinson, M.S.6
  • 21
    • 0035192658 scopus 로고    scopus 로고
    • GGAs: Roles of the different domains and comparison with AP-1 and clathrin
    • Hirst, J., Lindsay, M. R. and Robinson, M. S. (2001). GGAs: roles of the different domains and comparison with AP-1 and clathrin. Mol. Biol. Cell 12, 3573-3588.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3573-3588
    • Hirst, J.1    Lindsay, M.R.2    Robinson, M.S.3
  • 23
    • 70350626560 scopus 로고    scopus 로고
    • Spatial and functional relationship of GGAs and AP-1 in Drosophila and HeLa cells
    • Hirst, J., Motley, A., Harasaki, K., Peak Chew, S. Y. and Robinson, M. S. (2009). Spatial and functional relationship of GGAs and AP-1 in Drosophila and HeLa cells. Traffic 10, 1696-1710.
    • (2009) Traffic , vol.10 , pp. 1696-1710
    • Hirst, J.1    Motley, A.2    Harasaki, K.3    Peak Chew, S.Y.4    Robinson, M.S.5
  • 24
    • 24344478722 scopus 로고    scopus 로고
    • Epidermal growth factor-dependent phosphorylation of the GGA3 adaptor protein regulates its recruitment to membranes
    • Kametaka, S., Mattera, R. and Bonifacino, J. S. (2005). Epidermal growth factor-dependent phosphorylation of the GGA3 adaptor protein regulates its recruitment to membranes. Mol. Cell. Biol. 25, 7988-8000.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 7988-8000
    • Kametaka, S.1    Mattera, R.2    Bonifacino, J.S.3
  • 25
    • 34547758367 scopus 로고    scopus 로고
    • Canonical interaction of cyclin G associated kinase with adaptor protein 1 regulates lysosomal enzyme sorting
    • Kametaka, S., Moriyama, K., Burgos, P. V., Eisenberg, E., Greene, L. E., Mattera, R. and Bonifacino, J. S. (2007). Canonical interaction of cyclin G associated kinase with adaptor protein 1 regulates lysosomal enzyme sorting. Mol. Biol. Cell 18, 2991-3001.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2991-3001
    • Kametaka, S.1    Moriyama, K.2    Burgos, P.V.3    Eisenberg, E.4    Greene, L.E.5    Mattera, R.6    Bonifacino, J.S.7
  • 26
    • 0036295109 scopus 로고    scopus 로고
    • Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism
    • Kato, Y., Misra, S., Puertollano, R., Hurley, J. H. and Bonifacino, J. S. (2002). Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism. Nat. Struct. Biol. 9, 532-536.
    • (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
  • 27
    • 0042672956 scopus 로고    scopus 로고
    • A novel role for dp115 in the organization of tER sites in Drosophila
    • Kondylis, V. and Rabouille, C. (2003). A novel role for dp115 in the organization of tER sites in Drosophila. J. Cell Biol. 162, 185-198.
    • (2003) J. Cell Biol , vol.162 , pp. 185-198
    • Kondylis, V.1    Rabouille, C.2
  • 28
    • 0035167943 scopus 로고    scopus 로고
    • Biogenesis of Golgi stacks in imaginal discs of Drosophila melanogaster
    • Kondylis, V., Goulding, S. E., Dunne, J. C. and Rabouille, C. (2001). Biogenesis of Golgi stacks in imaginal discs of Drosophila melanogaster. Mol. Biol. Cell 12, 2308-2327.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2308-2327
    • Kondylis, V.1    Goulding, S.E.2    Dunne, J.C.3    Rabouille, C.4
  • 29
    • 24344453350 scopus 로고    scopus 로고
    • dGRASP localization and function in the early exocytic pathway in Drosophila S2 cells
    • Kondylis, V., Spoorendonk, K. M. and Rabouille, C. (2005). dGRASP localization and function in the early exocytic pathway in Drosophila S2 cells. Mol. Biol. Cell 16, 4061-4072.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4061-4072
    • Kondylis, V.1    Spoorendonk, K.M.2    Rabouille, C.3
  • 30
    • 65649128660 scopus 로고    scopus 로고
    • K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway
    • Lauwers, E., Jacob, C. and André, B. (2009). K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J. Cell Biol. 185, 493-502.
    • (2009) J. Cell Biol , vol.185 , pp. 493-502
    • Lauwers, E.1    Jacob, C.2    André, B.3
  • 32
    • 34548482956 scopus 로고    scopus 로고
    • The trans-Golgi network accessory protein p56 promotes long-range movement of GGA/clathrin-containing transport carriers and lysosomal enzyme sorting
    • Mardones, G. A., Burgos, P. V., Brooks, D. A., Parkinson-Lawrence, E., Mattera, R. and Bonifacino, J. S. (2007). The trans-Golgi network accessory protein p56 promotes long-range movement of GGA/clathrin-containing transport carriers and lysosomal enzyme sorting. Mol. Biol. Cell 18, 3486-3501.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3486-3501
    • Mardones, G.A.1    Burgos, P.V.2    Brooks, D.A.3    Parkinson-Lawrence, E.4    Mattera, R.5    Bonifacino, J.S.6
  • 34
    • 0037413690 scopus 로고    scopus 로고
    • Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex
    • Mattera, R., Arighi, C. N., Lodge, R., Zerial, M. and Bonifacino, J. S. (2003). Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex. EMBO J. 22, 78-88.
    • (2003) EMBO J , vol.22 , pp. 78-88
    • Mattera, R.1    Arighi, C.N.2    Lodge, R.3    Zerial, M.4    Bonifacino, J.S.5
  • 35
    • 3843118843 scopus 로고    scopus 로고
    • The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites
    • Mattera, R., Puertollano, R., Smith, W. J. and Bonifacino, J. S. (2004). The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites. J. Biol. Chem. 279, 31409-31418.
    • (2004) J. Biol. Chem , vol.279 , pp. 31409-31418
    • Mattera, R.1    Puertollano, R.2    Smith, W.J.3    Bonifacino, J.S.4
  • 36
    • 0042991385 scopus 로고    scopus 로고
    • Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3
    • Miller, G. J., Mattera, R., Bonifacino, J. S. and Hurley, J. H. (2003). Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3. Nat. Struct. Biol. 10, 599-606.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 599-606
    • Miller, G.J.1    Mattera, R.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 37
    • 0037148787 scopus 로고    scopus 로고
    • Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains
    • Misra, S., Puertollano, R., Kato, Y., Bonifacino, J. S. and Hurley, J. H. (2002). Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains. Nature. 415, 933-937.
    • (2002) Nature , vol.415 , pp. 933-937
    • Misra, S.1    Puertollano, R.2    Kato, Y.3    Bonifacino, J.S.4    Hurley, J.H.5
  • 40
    • 0032572560 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes
    • Ooi, C. E., Dell'Angelica, E. C. and Bonifacino, J. S. (1998). ADP-ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes. J. Cell Biol. 142, 391-402.
    • (1998) J. Cell Biol , vol.142 , pp. 391-402
    • Ooi, C.E.1    Dell'Angelica, E.C.2    Bonifacino, J.S.3
  • 46
    • 1842556279 scopus 로고    scopus 로고
    • Adaptable adaptors for coated vesicles
    • Robinson, M. S. (2004). Adaptable adaptors for coated vesicles. Trends. Cell Biol. 14, 167-174.
    • (2004) Trends. Cell Biol , vol.14 , pp. 167-174
    • Robinson, M.S.1
  • 47
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl, R. H. and Gietz, R. D. (1989). High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16, 339-346.
    • (1989) Curr. Genet , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 48
    • 0015328565 scopus 로고
    • Cell lines derived from late embryonic stages of Drosophila melanogaster
    • Schneider, I. (1972). Cell lines derived from late embryonic stages of Drosophila melanogaster. J. Embryol. Exp. Morphol. 27, 353-365.
    • (1972) J. Embryol. Exp. Morphol , vol.27 , pp. 353-365
    • Schneider, I.1
  • 51
    • 0035958856 scopus 로고    scopus 로고
    • Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains
    • Takatsu, H., Katoh, Y., Shiba, Y. and Nakayama, K. (2001). Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J. Biol. Chem. 276, 28541-28545.
    • (2001) J. Biol. Chem , vol.276 , pp. 28541-28545
    • Takatsu, H.1    Katoh, Y.2    Shiba, Y.3    Nakayama, K.4
  • 52
    • 34347382638 scopus 로고    scopus 로고
    • PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal
    • Wang, J., Sun, H. Q., Macia, E., Kirchhausen, T., Watson, H., Bonifacino, J. S. and Yin, H. L. (2007). PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal. Mol. Biol. Cell 18, 2646-2655.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2646-2655
    • Wang, J.1    Sun, H.Q.2    Macia, E.3    Kirchhausen, T.4    Watson, H.5    Bonifacino, J.S.6    Yin, H.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.