메뉴 건너뛰기




Volumn 501, Issue 7465, 2013, Pages 116-120

Vesicular and non-vesicular transport feed distinct glycosylation pathways in the Golgi

(21)  D'Angelo, Giovanni a,b   Uemura, Takefumi c   Chuang, Chia Chen d   Polishchuk, Elena a   Santoro, Michele a   Ohvo Rekilä, Henna e   Sato, Takashi c   Di Tullio, Giuseppe f   Varriale, Antonio b   D'Auria, Sabato b   Daniele, Tiziana f   Capuani, Fabrizio a   Johannes, Ludger g,h   Mattjus, Peter e   Monti, Maria i   Pucci, Piero i   Williams, Roger L j   Burke, John E j   Platt, Frances M d   Harada, Akihiro c,k   more..

h CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; FAPP2 PROTEIN; GLYCOSPHINGOLIPID; GUANINE NUCLEOTIDE BINDING PROTEIN; PHOSPHATIDYLCHOLINE; UNCLASSIFIED DRUG;

EID: 84883742330     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12423     Document Type: Article
Times cited : (131)

References (30)
  • 1
    • 34548498611 scopus 로고    scopus 로고
    • Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide
    • D'Angelo, G. et al. Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide. Nature 449, 62-67 (2007)
    • (2007) Nature , vol.449 , pp. 62-67
    • D'Angelo, G.1
  • 2
    • 40849119996 scopus 로고    scopus 로고
    • Structure and function of glycosphingolipids and sphingolipids: Recollections and future trends
    • Hakomori, S. I. Structure and function of glycosphingolipids and sphingolipids: recollections and future trends. Biochim. Biophys. Acta 1780, 325-346 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 325-346
    • Hakomori, S.I.1
  • 3
    • 0026552908 scopus 로고
    • Glucosylceramide is synthesized at the cytosolic surface of various Golgi subfractions
    • Jeckel, D., Karrenbauer, A., Burger, K. N., van Meer, G. & Wieland, F. Glucosylceramide is synthesized at the cytosolic surface of various Golgi subfractions. J. Cell Biol. 117, 259-267 (1992).
    • (1992) J. Cell Biol. , vol.117 , pp. 259-267
    • Jeckel, D.1    Karrenbauer, A.2    Burger, K.N.3    Van Meer, G.4    Wieland, F.5
  • 4
    • 0025993036 scopus 로고
    • Determinationofthe intracellular sites and topology of glucosylceramide synthesis in rat liver
    • Futerman, A. H. & Pagano, R. E. Determinationofthe intracellular sites and topology of glucosylceramide synthesis in rat liver. Biochem. J. 280, 295-302 (1991).
    • (1991) Biochem. J. , vol.280 , pp. 295-302
    • Futerman, A.H.1    Pagano, R.E.2
  • 5
    • 38549152194 scopus 로고    scopus 로고
    • Principles of bioactive lipid signalling: Lessons from sphingolipids
    • Hannun, Y. A. & Obeid, L. M. Principles of bioactive lipid signalling: lessons from sphingolipids. Nature Rev. Mol. Cell Biol. 9, 139-150 (2008).
    • (2008) Nature Rev. Mol. Cell Biol. , vol.9 , pp. 139-150
    • Hannun, Y.A.1    Obeid, L.M.2
  • 6
    • 35348991132 scopus 로고    scopus 로고
    • Pre-and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis
    • Halter, D. et al. Pre-and post-Golgi translocation of glucosylceramide in glycosphingolipid synthesis. J. Cell Biol. 179, 101-115 (2007).
    • (2007) J. Cell Biol. , vol.179 , pp. 101-115
    • Halter, D.1
  • 7
    • 79954988198 scopus 로고    scopus 로고
    • Cellular and molecular biology of glycosphingolipid glycosylation
    • Maccioni, H. J., Quiroga, R. & Ferrari, M. L. Cellular and molecular biology of glycosphingolipid glycosylation. J. Neurochem. 117, 589-602 (2011).
    • (2011) J. Neurochem. , vol.117 , pp. 589-602
    • MacCioni, H.J.1    Quiroga, R.2    Ferrari, M.L.3
  • 8
    • 0022508584 scopus 로고
    • Pathogenesisof shigella diarrhea. XI. Isolationof ashigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide
    • Jacewicz, M., Clausen, H., Nudelman, E., Donohue-Rolfe, A. & Keusch, G. T. Pathogenesisof shigella diarrhea. XI. Isolationof ashigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide. J. Exp. Med. 163, 1391-1404 (1986).
    • (1986) J. Exp. Med. , vol.163 , pp. 1391-1404
    • Jacewicz, M.1    Clausen, H.2    Nudelman, E.3    Donohue-Rolfe, A.4    Keusch, G.T.5
  • 10
    • 62449248428 scopus 로고    scopus 로고
    • Shiga toxin2targets the murine renal collecting duct epithelium
    • Psotka, M. A. et al. Shiga toxin2targets the murine renal collecting duct epithelium. Infect. Immun. 77, 959-969 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 959-969
    • Psotka, M.A.1
  • 11
    • 33744519950 scopus 로고    scopus 로고
    • Targeted disruption of Gb3/CD77 synthase gene resulted in the complete deletion of globo-series glycosphingolipids and loss of sensitivity to verotoxins
    • Okuda, T. et al. Targeted disruption of Gb3/CD77 synthase gene resulted in the complete deletion of globo-series glycosphingolipids and loss of sensitivity to verotoxins. J. Biol. Chem. 281, 10230-10235 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 10230-10235
    • Okuda, T.1
  • 13
    • 0025103773 scopus 로고
    • Compartmentation of the Golgi complex: Brefeldin-A distinguishes trans-Golgi cisternae from the trans-Golgi network
    • Chege, N. W. & Pfeffer, S. R. Compartmentation of the Golgi complex: brefeldin-A distinguishes trans-Golgi cisternae from the trans-Golgi network. J. Cell Biol. 111, 893-899 (1990).
    • (1990) J. Cell Biol. , vol.111 , pp. 893-899
    • Chege, N.W.1    Pfeffer, S.R.2
  • 14
    • 2342556630 scopus 로고    scopus 로고
    • FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns (4) P
    • Godi, A. et al. FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns (4) P. Nature Cell Biol. 6, 393-404 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 393-404
    • Godi, A.1
  • 15
    • 78149271035 scopus 로고    scopus 로고
    • Transmembrane BAX inhibitor motif containing (TMBIM) family proteins perturbs a trans-Golgi network enzyme, Gb3 synthase, and reducesGb3 biosynthesis
    • Yamaji, T., Nishikawa, K. & Hanada, K. Transmembrane BAX inhibitor motif containing (TMBIM) family proteins perturbs a trans-Golgi network enzyme, Gb3 synthase, and reducesGb3 biosynthesis. J. Biol. Chem. 285, 35505-35518 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 35505-35518
    • Yamaji, T.1    Nishikawa, K.2    Hanada, K.3
  • 16
    • 70349976317 scopus 로고    scopus 로고
    • 2a controls the formation of inter-cisternal continuities involved in intra-Golgi transport
    • 2a controls the formation of inter-cisternal continuities involved in intra-Golgi transport. PLoS Biol. 7, e1000194 (2009).
    • (2009) PLoS Biol. , vol.7
    • San Pietro, E.1
  • 18
    • 79956320991 scopus 로고    scopus 로고
    • Molecularbasisofphosphatidylinositol 4-phosphate andARF1GTPase recognition by the FAPP1 pleckstrin homology (PH) domain
    • He, J. et al. Molecularbasisofphosphatidylinositol 4-phosphate andARF1GTPase recognition by the FAPP1 pleckstrin homology (PH) domain. J. Biol. Chem. 286, 18650-18657 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 18650-18657
    • He, J.1
  • 19
    • 47649123929 scopus 로고    scopus 로고
    • The multiple roles of PtdIns (4) P-not just the precursor of PtdIns (4, 5) P2
    • D'Angelo, G., Vicinanza, M., Di Campli, A. & De Matteis, M. A. The multiple roles of PtdIns (4) P-not just the precursor of PtdIns (4, 5) P2. J. Cell Sci. 121, 1955-1963 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 1955-1963
    • D'Angelo, G.1    Vicinanza, M.2    Di Campli, A.3    De Matteis, M.A.4
  • 20
    • 84870654359 scopus 로고    scopus 로고
    • The glycolipid transfer protein (GLTP) domain of phosphoinositol 4-phosphate adaptor protein-2 (FAPP2): Structure drives preference for simple neutral glycosphingolipids
    • Kamlekar, R. K. et al. The glycolipid transfer protein (GLTP) domain of phosphoinositol 4-phosphate adaptor protein-2 (FAPP2): structure drives preference for simple neutral glycosphingolipids. Biochim. Biophys. Acta 1831, 417-427 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1831 , pp. 417-427
    • Kamlekar, R.K.1
  • 21
    • 1842868694 scopus 로고    scopus 로고
    • Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes
    • Yan, X., Watson, J., Ho, P. S. & Deinzer, M. L. Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes. Mol. Cell. Proteomics 3, 10-23 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 10-23
    • Yan, X.1    Watson, J.2    Ho, P.S.3    Deinzer, M.L.4
  • 22
    • 34447519003 scopus 로고    scopus 로고
    • The Rab8 GTPase regulates apical protein localization in intestinal cells
    • Sato, T. et al. The Rab8 GTPase regulates apical protein localization in intestinal cells. Nature 448, 366-369 (2007).
    • (2007) Nature , vol.448 , pp. 366-369
    • Sato, T.1
  • 23
    • 71749114199 scopus 로고    scopus 로고
    • GRASP65 and GRASP55 sequentially promote the transport of C-terminal valine-bearing cargos to and through the Golgi complex
    • D'Angelo, G. et al. GRASP65 and GRASP55 sequentially promote the transport of C-terminal valine-bearing cargos to and through the Golgi complex. J. Biol. Chem. 284, 34849-34860 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 34849-34860
    • D'Angelo, G.1
  • 24
    • 67649391259 scopus 로고    scopus 로고
    • Glycolipid acquisition by human glycolipid transfer protein dramatically alters intrinsic tryptophan fluorescence: Insights into glycolipid binding affinity
    • Zhai, X. et al. Glycolipid acquisition by human glycolipid transfer protein dramatically alters intrinsic tryptophan fluorescence: insights into glycolipid binding affinity. J. Biol. Chem. 284, 13620-13628 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 13620-13628
    • Zhai, X.1
  • 25
    • 78649784768 scopus 로고    scopus 로고
    • Monitoring glycolipid transfer protein activity and membrane interaction with the surface plasmon resonance technique
    • Ohvo-Rekilä, H. & Mattjus, P. Monitoring glycolipid transfer protein activity and membrane interaction with the surface plasmon resonance technique. Biochim. Biophys. Acta 1808, 47-54 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 47-54
    • Ohvo-Rekilä, H.1    Mattjus, P.2
  • 26
    • 84866544615 scopus 로고    scopus 로고
    • Oncogenic mutations mimic and enhance dynamic events in the natural activation of phosphoinositide 3-kinase p110alpha (PIK3CA)
    • Burke, J. E., Perisic, O., Masson, G. R., Vadas, O. & Williams, R. L. Oncogenic mutations mimic and enhance dynamic events in the natural activation of phosphoinositide 3-kinase p110alpha (PIK3CA). Proc. Natl Acad. Sci. USA 109, 15259-15264 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 15259-15264
    • Burke, J.E.1    Perisic, O.2    Masson, G.R.3    Vadas, O.4    Williams, R.L.5
  • 27
    • 0037209194 scopus 로고    scopus 로고
    • Shiga toxin B-subunit as a tool to study retrograde transport
    • Mallard, F. & Johannes, L. Shiga toxin B-subunit as a tool to study retrograde transport. Methods Mol. Med. 73, 209-220 (2003).
    • (2003) Methods Mol. Med. , vol.73 , pp. 209-220
    • Mallard, F.1    Johannes, L.2
  • 28
    • 42749084800 scopus 로고    scopus 로고
    • Neuron-specific recombination by Cre recombinase inserted into the murine tau locus
    • Muramatsu, K. et al. Neuron-specific recombination by Cre recombinase inserted into the murine tau locus. Biochem. Biophys. Res. Commun. 370, 419-423 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.370 , pp. 419-423
    • Muramatsu, K.1
  • 29
    • 41749105334 scopus 로고    scopus 로고
    • Neuron-specific and inducible recombination by Cre recombinase in the mouse
    • Hashimoto, Y. et al. Neuron-specific and inducible recombination by Cre recombinase in the mouse. Neuroreport 19, 621-624 (2008).
    • (2008) Neuroreport , vol.19 , pp. 621-624
    • Hashimoto, Y.1
  • 30
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S. & Cordelieres, F. P. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224, 213-232 (2006).
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.