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Volumn 113, Issue 14, 2016, Pages 3791-3796

Characterization of the complex formed by β-glucocerebrosidase and the lysosomal integral membrane protein type-2

Author keywords

Gaucher's disease; GC activators; LIMP 2; Parkinson's disease; glucocerebrosidase

Indexed keywords

ALPHA SYNUCLEIN; BETA GLUCOSYLCERAMIDASE; GLUCOSYLCERAMIDASE; GLUCOSYLCERAMIDE; LYSOSOMAL INTEGRAL MEMBRANE PROTEIN TYPE 2; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 2; PROTEIN BINDING;

EID: 84962727864     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1514005113     Document Type: Article
Times cited : (46)

References (35)
  • 1
    • 36048935960 scopus 로고    scopus 로고
    • LIMP-2 is a receptor for lysosomal mannose-6-phosphateindependent targeting of beta-glucocerebrosidase
    • Reczek D, et al. (2007) LIMP-2 is a receptor for lysosomal mannose-6-phosphateindependent targeting of beta-glucocerebrosidase. Cell 131(4):770-783.
    • (2007) Cell , vol.131 , Issue.4 , pp. 770-783
    • Reczek, D.1
  • 2
    • 84941599220 scopus 로고    scopus 로고
    • Mannose 6-phosphate-independent lysosomal sorting of LIMP-2
    • Blanz J, et al. (2015) Mannose 6-phosphate-independent Lysosomal Sorting of LIMP-2. Traffic 16(10):1127-1136.
    • (2015) Traffic , vol.16 , Issue.10 , pp. 1127-1136
    • Blanz, J.1
  • 3
    • 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. (2010) 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(4):563-572.
    • (2010) Hum Mol Genet , vol.19 , Issue.4 , pp. 563-572
    • Blanz, J.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 SF, et al. (2008) Array-based gene discovery with three unrelated subjects shows SCARB2/LIMP-2 deficiency causes myoclonus epilepsy and glomerulosclerosis. Am J Hum Genet 82(3):673-684.
    • (2008) Am J Hum Genet , vol.82 , Issue.3 , pp. 673-684
    • Berkovic, S.F.1
  • 5
    • 42949118684 scopus 로고    scopus 로고
    • Gaucher disease: Mutation and polymorphism spectrum in the glucocerebrosidase gene (GBA)
    • Hruska KS, LaMarca ME, Scott CR, Sidransky E (2008) Gaucher disease: Mutation and polymorphism spectrum in the glucocerebrosidase gene (GBA). Hum Mutat 29(5):567-583.
    • (2008) Hum Mutat , vol.29 , Issue.5 , pp. 567-583
    • Hruska, K.S.1    LaMarca, M.E.2    Scott, C.R.3    Sidransky, E.4
  • 6
    • 84878798127 scopus 로고    scopus 로고
    • A multicenter study of glucocerebrosidase mutations in dementia with lewy bodies
    • Nalls MA, et al. (2013) A multicenter study of glucocerebrosidase mutations in dementia with Lewy bodies. JAMA Neurol 70(6):727-735.
    • (2013) JAMA Neurol , vol.70 , Issue.6 , pp. 727-735
    • Nalls, M.A.1
  • 7
    • 80052028927 scopus 로고    scopus 로고
    • Exploring the link between glucocerebrosidase mutations and parkinsonism
    • Westbroek W, Gustafson AM, Sidransky E (2011) Exploring the link between glucocerebrosidase mutations and parkinsonism. Trends Mol Med 17(9):485-493.
    • (2011) Trends Mol Med , vol.17 , Issue.9 , pp. 485-493
    • Westbroek, W.1    Gustafson, A.M.2    Sidransky, E.3
  • 8
    • 84867036900 scopus 로고    scopus 로고
    • Glucocerebrosidase deficiency in substantia nigra of Parkinson disease brains
    • Gegg ME, et al. (2012) Glucocerebrosidase deficiency in substantia nigra of parkinson disease brains. Ann Neurol 72(3):455-463.
    • (2012) Ann Neurol , vol.72 , Issue.3 , pp. 455-463
    • Gegg, M.E.1
  • 9
    • 84908282747 scopus 로고    scopus 로고
    • LIMP-2 expression is critical for β-glucocerebrosidase activity and α-synuclein clearance
    • Rothaug M, et al. (2014) LIMP-2 expression is critical for β-glucocerebrosidase activity and α-synuclein clearance. Proc Natl Acad Sci USA 111(43):15573-15578.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.43 , pp. 15573-15578
    • Rothaug, M.1
  • 10
    • 84908296281 scopus 로고    scopus 로고
    • Genetic analysis implicates APOE, SNCA and suggests lysosomal dysfunction in the etiology of dementia with lewy bodies
    • Bras J, et al. (2014) Genetic analysis implicates APOE, SNCA and suggests lysosomal dysfunction in the etiology of dementia with Lewy bodies. Hum Mol Genet 23(23):6139-6146.
    • (2014) Hum Mol Genet , vol.23 , Issue.23 , pp. 6139-6146
    • Bras, J.1
  • 11
    • 79961083395 scopus 로고    scopus 로고
    • CNS expression of glucocerebrosidase corrects alpha-synuclein pathology and memory in a mouse model of gaucher-related synucleinopathy
    • Sardi SP, et al. (2011) CNS expression of glucocerebrosidase corrects alpha-synuclein pathology and memory in a mouse model of Gaucher-related synucleinopathy. Proc Natl Acad Sci USA 108(29):12101-12106.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.29 , pp. 12101-12106
    • Sardi, S.P.1
  • 12
    • 84874487118 scopus 로고    scopus 로고
    • Augmenting CNS glucocerebrosidase activity as a therapeutic strategy for parkinsonism and other gaucher-related synucleinopathies
    • Sardi SP, et al. (2013) Augmenting CNS glucocerebrosidase activity as a therapeutic strategy for parkinsonism and other Gaucher-related synucleinopathies. Proc Natl Acad Sci USA 110(9):3537-3542.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.9 , pp. 3537-3542
    • Sardi, S.P.1
  • 13
    • 84899818136 scopus 로고    scopus 로고
    • Glucocerebrosidase is shaking up the synucleinopathies
    • Siebert M, Sidransky E, Westbroek W (2014) Glucocerebrosidase is shaking up the synucleinopathies. Brain 137(Pt 5):1304-1322.
    • (2014) Brain , vol.137 , pp. 1304-1322
    • Siebert, M.1    Sidransky, E.2    Westbroek, W.3
  • 14
    • 79960009804 scopus 로고    scopus 로고
    • Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies
    • Mazzulli JR, et al. (2011) Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell 146(1):37-52.
    • (2011) Cell , vol.146 , Issue.1 , pp. 37-52
    • Mazzulli, J.R.1
  • 15
    • 84889609917 scopus 로고    scopus 로고
    • Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36
    • Neculai D, et al. (2013) Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36. Nature 504(7478):172-176.
    • (2013) Nature , vol.504 , Issue.7478 , pp. 172-176
    • Neculai, D.1
  • 16
    • 33845490892 scopus 로고    scopus 로고
    • Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in gaucher disease
    • Brumshtein B, Wormald MR, Silman I, Futerman AH, Sussman JL (2006) Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease. Acta Crystallogr D Biol Crystallogr 62(Pt 12):1458-1465.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 1458-1465
    • Brumshtein, B.1    Wormald, M.R.2    Silman, I.3    Futerman, A.H.4    Sussman, J.L.5
  • 17
    • 0042354624 scopus 로고    scopus 로고
    • X-ray structure of human acid-beta-glucosidase, the defective enzyme in gaucher disease
    • Dvir H, et al. (2003) X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease. EMBO Rep 4(7):704-709.
    • (2003) EMBO Rep , vol.4 , Issue.7 , pp. 704-709
    • Dvir, H.1
  • 18
    • 0031741545 scopus 로고    scopus 로고
    • Mutation analysis of gaucher disease patients from Argentina: High prevalence of the RecNciI mutation
    • Cormand B, et al. (1998) Mutation analysis of Gaucher disease patients from Argentina: High prevalence of the RecNciI mutation. Am J Med Genet 80(4):343-351.
    • (1998) Am J Med Genet , vol.80 , Issue.4 , pp. 343-351
    • Cormand, B.1
  • 19
    • 0026347931 scopus 로고
    • A new glucocerebrosidase-gene missense mutation responsible for neuronopathic gaucher disease in Japanese patients
    • Kawame H, Eto Y (1991) A new glucocerebrosidase-gene missense mutation responsible for neuronopathic Gaucher disease in Japanese patients. Am J Hum Genet 49(6):1378-1380.
    • (1991) Am J Hum Genet , vol.49 , Issue.6 , pp. 1378-1380
    • Kawame, H.1    Eto, Y.2
  • 20
    • 84904469837 scopus 로고    scopus 로고
    • Lysosome sorting of β-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor
    • Zhao Y, Ren J, Padilla-Parra S, Fry EE, Stuart DI (2014) Lysosome sorting of β-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor. Nat Commun 5:4321.
    • (2014) Nat Commun , vol.5 , pp. 4321
    • Zhao, Y.1    Ren, J.2    Padilla-Parra, S.3    Fry, E.E.4    Stuart, D.I.5
  • 21
    • 84942694202 scopus 로고    scopus 로고
    • Extracellular juxtamembrane segment of ADAM17 interacts with membranes and is essential for its shedding activity
    • Düsterhöft S, et al. (2015) Extracellular juxtamembrane segment of ADAM17 interacts with membranes and is essential for its shedding activity. Biochemistry 54(38):5791-5801.
    • (2015) Biochemistry , vol.54 , Issue.38 , pp. 5791-5801
    • Düsterhöft, S.1
  • 22
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel AD, Pabo CO (1988) Cellular uptake of the tat protein from human immunodeficiency virus. Cell 55(6):1189-1193.
    • (1988) Cell , vol.55 , Issue.6 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 23
    • 0032823270 scopus 로고    scopus 로고
    • Import into and degradation of cytosolic proteins by isolated yeast vacuoles
    • Horst M, Knecht EC, Schu PV (1999) Import into and degradation of cytosolic proteins by isolated yeast vacuoles. Mol Biol Cell 10(9):2879-2889.
    • (1999) Mol Biol Cell , vol.10 , Issue.9 , pp. 2879-2889
    • Horst, M.1    Knecht, E.C.2    Schu, P.V.3
  • 24
    • 84958999192 scopus 로고    scopus 로고
    • Alpha-synuclein-induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models
    • Mazzulli JR, Zunke F, Isacson O, Studer L, Krainc D (2016) Alpha-synuclein-induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models. Proc Natl Acad Sci USA 113(7):1931-1936.
    • (2016) Proc Natl Acad Sci USA , vol.113 , Issue.7 , pp. 1931-1936
    • Mazzulli, J.R.1    Zunke, F.2    Isacson, O.3    Studer, L.4    Krainc, D.5
  • 25
    • 33645243798 scopus 로고    scopus 로고
    • Analyses of variant acid beta-glucosidases: Effects of gaucher disease mutations
    • Liou B, et al. (2006) Analyses of variant acid beta-glucosidases: Effects of Gaucher disease mutations. J Biol Chem 281(7):4242-4253.
    • (2006) J Biol Chem , vol.281 , Issue.7 , pp. 4242-4253
    • Liou, B.1
  • 26
    • 0025246148 scopus 로고
    • Analyses of catalytic activity and inhibitor binding of human acid beta-glucosidase by site-directed mutagenesis. Identification of residues critical to catalysis and evidence for causality of two ashkenazi jewish gaucher disease type 1 mutations
    • Grace ME, Graves PN, Smith FI, Grabowski GA (1990) Analyses of catalytic activity and inhibitor binding of human acid beta-glucosidase by site-directed mutagenesis. Identification of residues critical to catalysis and evidence for causality of two Ashkenazi Jewish Gaucher disease type 1 mutations. J Biol Chem 265(12):6827-6835.
    • (1990) J Biol Chem , vol.265 , Issue.12 , pp. 6827-6835
    • Grace, M.E.1    Graves, P.N.2    Smith, F.I.3    Grabowski, G.A.4
  • 27
    • 38549097709 scopus 로고    scopus 로고
    • An evolutionary and structure-based docking model for glucocerebrosidase-saposin C and glucocerebrosidase-substrate interactions - relevance for gaucher disease
    • Atrian S, et al. (2008) An evolutionary and structure-based docking model for glucocerebrosidase-saposin C and glucocerebrosidase-substrate interactions - relevance for Gaucher disease. Proteins 70(3):882-891.
    • (2008) Proteins , vol.70 , Issue.3 , pp. 882-891
    • Atrian, S.1
  • 28
    • 84856599940 scopus 로고    scopus 로고
    • A guided tour of the structural biology of gaucher disease: Acid-β-glucosidase and saposin C
    • Lieberman RL (2011) A guided tour of the structural biology of Gaucher disease: Acid-β-glucosidase and saposin C. Enzyme Res 2011:973231.
    • (2011) Enzyme Res , vol.2011 , pp. 973231
    • Lieberman, R.L.1
  • 30
    • 0344094038 scopus 로고
    • Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages
    • Stahl PD, Rodman JS, Miller MJ, Schlesinger PH (1978) Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages. Proc Natl Acad Sci USA 75(3):1399-1403.
    • (1978) Proc Natl Acad Sci USA , vol.75 , Issue.3 , pp. 1399-1403
    • Stahl, P.D.1    Rodman, J.S.2    Miller, M.J.3    Schlesinger, P.H.4
  • 31
    • 4744370348 scopus 로고    scopus 로고
    • Therapeutic goals in the treatment of gaucher disease
    • Pastores GM, et al. (2004) Therapeutic goals in the treatment of Gaucher disease. Semin Hematol 41(4, Suppl 5):4-14.
    • (2004) Semin Hematol , vol.41 , Issue.4 , pp. 4-14
    • Pastores, G.M.1
  • 32
    • 84908190426 scopus 로고    scopus 로고
    • The LIMP-2/SCARB2 binding motif on acid β-glucosidase: Basic and applied implications for gaucher disease and associated neurodegenerative diseases
    • Liou B, Haffey WD, Greis KD, Grabowski GA (2014) The LIMP-2/SCARB2 binding motif on acid β-glucosidase: Basic and applied implications for Gaucher disease and associated neurodegenerative diseases. J Biol Chem 289(43):30063-30074.
    • (2014) J Biol Chem , vol.289 , Issue.43 , pp. 30063-30074
    • Liou, B.1    Haffey, W.D.2    Greis, K.D.3    Grabowski, G.A.4
  • 33
  • 34
    • 84863083762 scopus 로고    scopus 로고
    • Discovery, structure-activity relationship, and biological evaluation of noninhibitory small molecule chaperones of glucocerebrosidase
    • Patnaik S, et al. (2012) Discovery, structure-activity relationship, and biological evaluation of noninhibitory small molecule chaperones of glucocerebrosidase. J Med Chem 55(12):5734-5748.
    • (2012) J Med Chem , vol.55 , Issue.12 , pp. 5734-5748
    • Patnaik, S.1
  • 35
    • 37049236408 scopus 로고
    • Determination of the coefficient of correlation
    • Pearson K (1909) Determination of the Coefficient of Correlation. Science 30(757): 23-25.
    • (1909) Science , vol.30 , Issue.757 , pp. 23-25
    • Pearson, K.1


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