메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Lysosome sorting of β-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLUCOSYLCERAMIDASE; CERAMIDE; GLUCOSYLCERAMIDASE; HISTIDINE; LIMP 2 PROTEIN; MEMBRANE PROTEIN; SOMATOMEDIN B RECEPTOR; UNCLASSIFIED DRUG; LYSOSOME ASSOCIATED MEMBRANE PROTEIN; SCARB2 PROTEIN, HUMAN; SCAVENGER RECEPTOR;

EID: 84904469837     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5321     Document Type: Article
Times cited : (77)

References (50)
  • 1
    • 0028911434 scopus 로고
    • The cd36, cla-1 (cd36l1), and limpii (cd36l2) gene family: Cellular distribution, chromosomal location, and genetic evolution
    • Calvo, D., Dopazo, J. & Vega, M. A. The CD36, CLA-1 (CD36L1), and LIMPII (CD36L2) gene family: Cellular distribution, chromosomal location, and genetic evolution. Genomics 25, 100-106 (1995
    • (1995) Genomics , vol.25 , pp. 100-106
    • Calvo, D.1    Dopazo, J.2    Vega, M.A.3
  • 2
    • 0026653801 scopus 로고
    • Isolation and sequencing of a cDNA clone encoding the 85 kDa human lysosomal sialoglycoprotein (hLGP85) in human metastatic pancreas islet tumor cells
    • Fujita, H. et al. Isolation and sequencing of a cDNA clone encoding the 85 kDa human lysosomal sialoglycoprotein (hLGP85) in human metastatic pancreas islet tumor cells. Biochem. Biophys. Res. Commun. 184, 604-611 (1992
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 604-611
    • Fujita, H.1
  • 3
    • 61849164561 scopus 로고    scopus 로고
    • Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry
    • Chen, R. et al. Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J. Proteome. Res. 8, 651-661 (2009
    • (2009) J. Proteome. Res. , vol.8 , pp. 651-661
    • Chen, R.1
  • 4
    • 40849144062 scopus 로고    scopus 로고
    • Array-based gene discovery with three unrelated subjects shows SCARB2/LIMP-2 deficiency causes myoclonus epilepsy and glomerulosclerosis
    • Berkovic, S. F. et al. Array-based gene discovery with three unrelated subjects shows SCARB2/LIMP-2 deficiency causes myoclonus epilepsy and glomerulosclerosis. Am. J. Hum. Genet. 82, 673-684 (2008
    • (2008) Am. J. Hum. Genet. , vol.82 , pp. 673-684
    • Berkovic, S.F.1
  • 5
    • 82955232423 scopus 로고    scopus 로고
    • Clinical and neurophysiologic features of progressive myoclonus epilepsy without renal failure caused by SCARB2 mutations
    • Rubboli, G. et al. Clinical and neurophysiologic features of progressive myoclonus epilepsy without renal failure caused by SCARB2 mutations. Epilepsia 52, 2356-2363 (2011
    • (2011) Epilepsia , vol.52 , pp. 2356-2363
    • Rubboli, G.1
  • 6
    • 0034833822 scopus 로고    scopus 로고
    • CD36: A class B scavenger receptor involved in angiogenesis, atherosclerosis, inflammation, and lipid metabolism
    • DOI 10.1172/JCI200114006
    • Febbraio, M., Hajjar, D. P. & Silverstein, R. L. CD36: A class B scavenger receptor involved in angiogenesis, atherosclerosis, inflammation, and lipid metabolism. J. Clin. Invest. 108, 785-791 (2001 (Pubitemid 32880285)
    • (2001) Journal of Clinical Investigation , vol.108 , Issue.6 , pp. 785-791
    • Febbraio, M.1    Hajjar, D.P.2    Silverstein, R.L.3
  • 7
    • 84883158032 scopus 로고    scopus 로고
    • Scavenger receptors in homeostasis and immunity
    • Canton, J., Neculai, D. & Grinstein, S. Scavenger receptors in homeostasis and immunity. Nat. Rev. Immunol. 13, 621-634 (2013
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 621-634
    • Canton, J.1    Neculai, D.2    Grinstein, S.3
  • 8
    • 67650446350 scopus 로고    scopus 로고
    • Scavenger receptor B2 is a cellular receptor for enterovirus 71
    • Yamayoshi, S. et al. Scavenger receptor B2 is a cellular receptor for enterovirus 71. Nat. Med. 15, 798-801 (2009
    • (2009) Nat. Med. , vol.15 , pp. 798-801
    • Yamayoshi, S.1
  • 9
    • 84889609917 scopus 로고    scopus 로고
    • Structure of limp-2 provides functional insights with implications for sr-bi and cd36
    • Neculai, D. et al. Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36. Nature 504, 172-176 (2013
    • (2013) Nature , vol.504 , pp. 172-176
    • Neculai, D.1
  • 11
    • 17644422131 scopus 로고    scopus 로고
    • Gaucher disease: Pathological mechanisms and modern management
    • DOI 10.1111/j.1365-2141.2004.05351.x
    • Jmoudiak, M. & Futerman, A. H. Gaucher disease: Pathological mechanisms and modern management. Br. J. Haematol. 129, 178-188 (2005 (Pubitemid 40562438)
    • (2005) British Journal of Haematology , vol.129 , Issue.2 , pp. 178-188
    • Jmoudiak, M.1    Futerman, A.H.2
  • 12
    • 0039109678 scopus 로고    scopus 로고
    • A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3
    • DOI 10.1093/emboj/17.5.1304
    • Honing, S., Sandoval, I. V. & von Figura, K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J. 17, 1304-1314 (1998 (Pubitemid 28105510)
    • (1998) EMBO Journal , vol.17 , Issue.5 , pp. 1304-1314
    • Honing, S.1    Sandoval, I.2    Von Figura, K.3
  • 13
    • 70349882101 scopus 로고    scopus 로고
    • Carbohydrate recognition by the mannose-6-phosphate receptors
    • Kim, J. J., Olson, L. J. & Dahms, N. M. Carbohydrate recognition by the mannose-6-phosphate receptors. Curr. Opin. Struct. Biol. 19, 534-542 (2009
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 534-542
    • Kim, J.J.1    Olson, L.J.2    Dahms, N.M.3
  • 14
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • DOI 10.1073/pnas.212519299
    • Reeves, P. J., Callewaert, N., Contreras, R. & Khorana, H. G. Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl Acad. Sci. USA 99, 13419-13424 (2002 (Pubitemid 35215396)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.21 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 15
    • 0030780140 scopus 로고    scopus 로고
    • Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase
    • Tikkanen, R., Peltola, M., Oinonen, C., Rouvinen, J. & Peltonen, L. Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase. EMBO J. 16, 6684-6693 (1997 (Pubitemid 27503481)
    • (1997) EMBO Journal , vol.16 , Issue.22 , pp. 6684-6693
    • Tikkanen, R.1    Peltola, M.2    Oinonen, C.3    Rouvinen, J.4    Peltonen, L.5
  • 16
    • 84858698808 scopus 로고    scopus 로고
    • Mannose-6-phosphate pathway: A review on its role in lysosomal function and dysfunction
    • Coutinho, M. F., Prata, M. J. & Alves, S. Mannose-6-phosphate pathway: A review on its role in lysosomal function and dysfunction. Mol. Genet. Metab. 105, 542-550 (2012
    • (2012) Mol. Genet. Metab. , vol.105 , pp. 542-550
    • Coutinho, M.F.1    Prata, M.J.2    Alves, S.3
  • 17
    • 84859848908 scopus 로고    scopus 로고
    • FRET microscopy in the living cell: Different approaches, strengths and weaknesses
    • Padilla-Parra, S. & Tramier, M. FRET microscopy in the living cell: Different approaches, strengths and weaknesses. BioEssays 34, 369-376 (2012
    • (2012) BioEssays , vol.34 , pp. 369-376
    • Padilla-Parra, S.1    Tramier, M.2
  • 18
    • 77953027792 scopus 로고    scopus 로고
    • Modeling spectral tuning in monomeric teal fluorescent protein mTFP1
    • Topol, I., Collins, J. & Nemukhin, A. Modeling spectral tuning in monomeric teal fluorescent protein mTFP1. Biophys. Chem. 149, 78-82 (2010
    • (2010) Biophys. Chem. , vol.149 , pp. 78-82
    • Topol, I.1    Collins, J.2    Nemukhin, A.3
  • 19
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • DOI 10.1038/nbt0102-87
    • Nagai, T. et al. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20, 87-90 (2002 (Pubitemid 34044921)
    • (2002) Nature Biotechnology , vol.20 , Issue.1 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 20
    • 33644764063 scopus 로고    scopus 로고
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes
    • DOI 10.1016/j.cell.2005.12.038, PII S0092867406001231
    • Lakadamyali, M., Rust, M. J. & Zhuang, X. Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. Cell 124, 997-1009 (2006 (Pubitemid 43344239)
    • (2006) Cell , vol.124 , Issue.5 , pp. 997-1009
    • Lakadamyali, M.1    Rust, M.J.2    Zhuang, X.3
  • 21
    • 55549111893 scopus 로고    scopus 로고
    • Quantitative fret analysis by fast acquisition time domain flim at high spatial resolution in living cells
    • Padilla-Parra, S., Auduge, N., Coppey-Moisan, M. & Tramier, M. Quantitative FRET analysis by fast acquisition time domain FLIM at high spatial resolution in living cells. Biophys. J. 95, 2976-2988 (2008
    • (2008) Biophys. J. , vol.95 , pp. 2976-2988
    • Padilla-Parra, S.1    Auduge, N.2    Coppey-Moisan, M.3    Tramier, M.4
  • 22
    • 71749083025 scopus 로고    scopus 로고
    • Dynamic interaction of amphiphysin with N-WASP regulates actin assembly
    • Yamada, H. et al. Dynamic interaction of amphiphysin with N-WASP regulates actin assembly. J. Biol. Chem. 284, 34244-34256 (2009
    • (2009) J. Biol. Chem. , vol.284 , pp. 34244-34256
    • Yamada, H.1
  • 23
    • 77950360086 scopus 로고    scopus 로고
    • Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta- glucocerebrosidase
    • Blanz, J. et al. Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta-glucocerebrosidase. Hum. Mol. Genet. 19, 563-572 (2010
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 563-572
    • Blanz, J.1
  • 25
    • 84891352709 scopus 로고    scopus 로고
    • Action myoclonus renal failure syndrome: Diagnostic applications of activity-based probes and lipid analysis
    • Gaspar, P. et al. Action myoclonus renal failure syndrome: Diagnostic applications of activity-based probes and lipid analysis. J. Lipid Res. 55, 138-145 (2013
    • (2013) J. Lipid Res. , vol.55 , pp. 138-145
    • Gaspar, P.1
  • 27
    • 84863871382 scopus 로고    scopus 로고
    • A critical histidine residue within LIMP-2 mediates pH sensitive binding to its ligand beta-glucocerebrosidase
    • Zachos, C., Blanz, J., Saftig, P. & Schwake, M. A critical histidine residue within LIMP-2 mediates pH sensitive binding to its ligand beta-glucocerebrosidase. Traffic 13, 1113-1123 (2012
    • (2012) Traffic , vol.13 , pp. 1113-1123
    • Zachos, C.1    Blanz, J.2    Saftig, P.3    Schwake, M.4
  • 28
    • 84863116544 scopus 로고    scopus 로고
    • Molecular determinants of enterovirus 71 viral entry: Cleft around GLN-172 on VP1 protein interacts with variable region on scavenge receptor B 2
    • Chen, P. et al. Molecular determinants of enterovirus 71 viral entry: Cleft around GLN-172 on VP1 protein interacts with variable region on scavenge receptor B 2. J. Biol. Chem. 287, 6406-6420 (2012
    • (2012) J. Biol. Chem. , vol.287 , pp. 6406-6420
    • Chen, P.1
  • 29
    • 84861316194 scopus 로고    scopus 로고
    • A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71
    • Wang, X. et al. A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71. Nat. Struct. Mol. Biol. 19, 424-429 (2012
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 424-429
    • Wang, X.1
  • 30
    • 84885907969 scopus 로고    scopus 로고
    • Picornavirus uncoating intermediate captured in atomic detail
    • Ren, J. et al. Picornavirus uncoating intermediate captured in atomic detail. Nat. Commun. 4, 1929 (2013
    • (2013) Nat. Commun. , vol.4 , Issue.1929
    • Ren, J.1
  • 31
    • 84861409583 scopus 로고    scopus 로고
    • The glycan-binding properties of the cationindependent mannose 6-phosphate receptor are evolutionary conserved in vertebrates
    • Castonguay, A. C. et al. The glycan-binding properties of the cationindependent mannose 6-phosphate receptor are evolutionary conserved in vertebrates. Glycobiology 22, 983-996 (2012
    • (2012) Glycobiology , vol.22 , pp. 983-996
    • Castonguay, A.C.1
  • 33
    • 0027443394 scopus 로고
    • Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts
    • Glickman, J. N. & Kornfeld, S. Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts. J. Cell. Biol. 123, 99-108 (1993 (Pubitemid 23284866)
    • (1993) Journal of Cell Biology , vol.123 , Issue.1 , pp. 99-108
    • Glickman, J.N.1    Kornfeld, S.2
  • 34
    • 79959935033 scopus 로고    scopus 로고
    • Automation of large scale transient protein expression in mammalian cells
    • Zhao, Y. et al. Automation of large scale transient protein expression in mammalian cells. J. Struct. Biol. 175, 209-215 (2011
    • (2011) J. Struct. Biol. , vol.175 , pp. 209-215
    • Zhao, Y.1
  • 35
    • 80051613693 scopus 로고    scopus 로고
    • A comparison of exogenous promoter activity at the ROSA26 locus using a PhiiC31 integrase mediated cassette exchange approach in mouse ES cells
    • Chen, C. M., Krohn, J., Bhattacharya, S. & Davies, B. A comparison of exogenous promoter activity at the ROSA26 locus using a PhiiC31 integrase mediated cassette exchange approach in mouse ES cells. PloS ONE 6, e23376 (2011
    • (2011) PloS ONE , vol.6
    • Chen, C.M.1    Krohn, J.2    Bhattacharya, S.3    Davies, B.4
  • 36
    • 84898436061 scopus 로고    scopus 로고
    • Structural insights into the inhibition of Wnt signaling by cancer antigen 5T4/Wnt-activated inhibitory factor
    • Zhao, Y., Malinauskas, T., Harlos, K. & Jones, E. Y. Structural insights into the inhibition of Wnt signaling by cancer antigen 5T4/Wnt-activated inhibitory factor, Structure 22, 612-620 (2014
    • (2014) Structure , vol.22 , pp. 612-620
    • Zhao, Y.1    Malinauskas, T.2    Harlos, K.3    Jones, E.Y.4
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
  • 44
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • DOI 10.1107/S0907444906029799
    • Aricescu, A. R., Lu, W. & Jones, E. Y. A time-and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr. D Biol. Crystallogr. 62, 1243-1250 (2006 (Pubitemid 44526216)
    • (2006) Acta Crystallographica Section D: Biological Crystallography , vol.62 , Issue.10 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 46
    • 79953718772 scopus 로고    scopus 로고
    • A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis
    • Taylor, M. J., Perrais, D. & Merrifield, C. J. A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis. PLoS Biol 9, e1000604 (2011
    • (2011) PLoS Biol , vol.9
    • Taylor, M.J.1    Perrais, D.2    Merrifield, C.J.3
  • 47
    • 0142090026 scopus 로고    scopus 로고
    • Low-intensity two-dimensional imaging of fluorescence lifetimes in living cells
    • Emiliani, V. et al. Low-intensity two-dimensional imaging of fluorescence lifetimes in living cells. Appl. Phys. Lett. 83, 2471-2473 (2003
    • (2003) Appl. Phys. Lett. , vol.83 , pp. 2471-2473
    • Emiliani, V.1
  • 48
    • 70449135167 scopus 로고    scopus 로고
    • Quantitative comparison of different fluorescent protein couples for fast fret-flim acquisition
    • Padilla-Parra, S. et al. Quantitative comparison of different fluorescent protein couples for fast FRET-FLIM acquisition. Biophys. J. 97, 2368-2376 (2009
    • (2009) Biophys. J. , vol.97 , pp. 2368-2376
    • Padilla-Parra, S.1
  • 49
    • 33845751079 scopus 로고    scopus 로고
    • Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: Structural characterization and applications in fluorescence imaging
    • DOI 10.1042/BJ20060874
    • Ai, H. W., Henderson, J. N., Remington, S. J. & Campbell, R. E. Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: Structural characterization and applications in fluorescence imaging. Biochem. J. 400, 531-540 (2006 (Pubitemid 44974465)
    • (2006) Biochemical Journal , vol.400 , Issue.3 , pp. 531-540
    • Ai, H.-W.1    Henderson, J.N.2    Remington, S.J.3    Campbell, R.E.4
  • 50
    • 84880413281 scopus 로고    scopus 로고
    • 827Spatiotemporal quantification of FRET in living cells by fast time-domain FLIM: A comparative study of non-fitting methods
    • Leray, A., Padilla-Parra, S., Roul, J., Heliot, L. & Tramier, M. 827Spatiotemporal quantification of FRET in living cells by fast time-domain FLIM: A comparative study of non-fitting methods. PloS ONE 8, e69335 (2013).
    • (2013) PloS ONE , vol.8
    • Leray, A.1    Padilla-Parra, S.2    Roul, J.3    Heliot, L.4    Tramier, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.