메뉴 건너뛰기




Volumn 289, Issue 43, 2014, Pages 30063-30074

The LIMP-2/SCARB2 binding motif on acid β-Glucosidase: Basic and applied implications for gaucher disease and associated neurodegenerative diseases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; NEURODEGENERATIVE DISEASES; PROTEINS;

EID: 84908190426     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.593616     Document Type: Article
Times cited : (24)

References (44)
  • 1
    • 0013927537 scopus 로고
    • Demonstration of a deficiency of glucocerebroside-cleaving enzyme in Gaucher's disease
    • Brady, R. O., Kanfer, J. N., Bradley, R. M., and Shapiro, D. (1966) Demonstration of a deficiency of glucocerebroside-cleaving enzyme in Gaucher's disease. J. Clin. Invest. 45, 1112-1115
    • (1966) J. Clin. Invest. , vol.45 , pp. 1112-1115
    • Brady, R.O.1    Kanfer, J.N.2    Bradley, R.M.3    Shapiro, D.4
  • 2
    • 50549198437 scopus 로고
    • Metabolism of glucocerebrosides. II. Evidence of an enzymatic deficiency in Gaucher's disease
    • Brady, R. O., Kanfer, J. N., and Shapiro, D. (1965) Metabolism of glucocerebrosides. II. Evidence of an enzymatic deficiency in Gaucher's disease. Biochem. Biophys. Res. Commun. 18, 221-225
    • (1965) Biochem. Biophys. Res. Commun. , vol.18 , pp. 221-225
    • Brady, R.O.1    Kanfer, J.N.2    Shapiro, D.3
  • 3
    • 79955424976 scopus 로고    scopus 로고
    • Gaucher disease
    • (Valle, D., Beaudet, A. L., Vogelstein, B., Kinzler, K. W., Antonarakis, S. E., Ballabio, A., and Sly, W. S., eds) McGraw-Hill, New York
    • Grabowski, G. A., Petsko, G. A., and Kolodny, E. (2010) Gaucher disease. in The Metabolic and Molecular Bases of Inherited Disease (Valle, D., Beaudet, A. L., Vogelstein, B., Kinzler, K. W., Antonarakis, S. E., Ballabio, A., and Sly, W. S., eds) McGraw-Hill, New York
    • (2010) The Metabolic and Molecular Bases of Inherited Disease
    • Grabowski, G.A.1    Petsko, G.A.2    Kolodny, E.3
  • 5
  • 6
    • 0022345601 scopus 로고
    • Molecular cloning and nucleotide sequence of the human glucocerebrosidase gene
    • Sorge, J., West, C., Westwood, B., and Beutler, E. (1985) Molecular cloning and nucleotide sequence of the human glucocerebrosidase gene. Proc. Natl. Acad. Sci. U.S.A. 82, 7289-7293
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 7289-7293
    • Sorge, J.1    West, C.2    Westwood, B.3    Beutler, E.4
  • 7
    • 0027179238 scopus 로고
    • Human acid β-glucosidase: N-glycosylation site occupancy and the effect of glycosylation on enzymatic activity
    • Berg-Fussman, A., Grace, M. E., Ioannou, Y., and Grabowski, G. A. (1993) Human acid β-glucosidase: N-glycosylation site occupancy and the effect of glycosylation on enzymatic activity. J. Biol. Chem. 268, 14861-14866
    • (1993) J. Biol. Chem. , vol.268 , pp. 14861-14866
    • Berg-Fussman, A.1    Grace, M.E.2    Ioannou, Y.3    Grabowski, G.A.4
  • 8
    • 0001261457 scopus 로고    scopus 로고
    • I-cell disease and pseudo-Hurler polydystrophy: Disorders of lysosomal enzyme phosphorylation and localization
    • (Scriver, C. R., Beaudet, A., Sly, W., and Valle, D., Eds) McGraw-Hill, New York
    • Kornfeld, S., and Sly, W. S. (2001) I-cell disease and pseudo-Hurler polydystrophy: disorders of lysosomal enzyme phosphorylation and localization. in The Metabolic and Molecular Bases of Inherited Disease (Scriver, C. R., Beaudet, A., Sly, W., and Valle, D., eds) McGraw-Hill, New York
    • (2001) The Metabolic and Molecular Bases of Inherited Disease
    • Kornfeld, S.1    Sly, W.S.2
  • 9
    • 0019863331 scopus 로고
    • Lysosomal enzyme targeting: N-acetylglucosaminylphosphotransferase selectively phosphorylated native lysosomal enzymes
    • Reitman, M. L., and Kornfeld, S. (1981) Lysosomal enzyme targeting: N-acetylglucosaminylphosphotransferase selectively phosphorylated native lysosomal enzymes. J. Biol. Chem. 256, 11977-11980
    • (1981) J. Biol. Chem. , vol.256 , pp. 11977-11980
    • Reitman, M.L.1    Kornfeld, S.2
  • 11
    • 0033795520 scopus 로고    scopus 로고
    • Fate and sorting of acid β-glucosidase in transgenic mammalian cells
    • Leonova, T., and Grabowski, G. A. (2000) Fate and sorting of acid β-glucosidase in transgenic mammalian cells. Mol. Genet. Metab. 70, 281-294
    • (2000) Mol. Genet. Metab. , vol.70 , pp. 281-294
    • Leonova, T.1    Grabowski, G.A.2
  • 12
    • 78649729542 scopus 로고    scopus 로고
    • Lysosomal membrane proteins: Life between acid and neutral conditions
    • Saftig, P., Schröder, B., and Blanz, J. (2010) Lysosomal membrane proteins: life between acid and neutral conditions. Biochem. Soc. Trans. 38, 1420-1423
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1420-1423
    • Saftig, P.1    Schröder, B.2    Blanz, J.3
  • 13
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function
    • Saftig, P., and Klumperman, J. (2009) Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat. Rev. Mol. Cell Biol. 10, 623-635
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 14
    • 0028170209 scopus 로고
    • Lysosomal targeting of Limp II membrane glycoprotein requires a novel Leu-Ile motif at a particular position in its cytoplasmic tail
    • Ogata, S., and Fukuda, M. (1994) Lysosomal targeting of Limp II membrane glycoprotein requires a novel Leu-Ile motif at a particular position in its cytoplasmic tail. J. Biol. Chem. 269, 5210-5217
    • (1994) J. Biol. Chem. , vol.269 , pp. 5210-5217
    • Ogata, S.1    Fukuda, M.2
  • 15
    • 84863871382 scopus 로고    scopus 로고
    • A critical histidine residue within LIMP-2 mediates pH sensitive binding to its ligand β-glucocerebrosidase
    • Zachos, C., Blanz, J., Saftig, P., and Schwake, M. (2012) A critical histidine residue within LIMP-2 mediates pH sensitive binding to its ligand β-glucocerebrosidase. Traffic 13, 1113-1123
    • (2012) Traffic , vol.13 , pp. 1113-1123
    • Zachos, C.1    Blanz, J.2    Saftig, P.3    Schwake, M.4
  • 17
    • 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 B2
    • Chen, P., Song, Z., Qi, Y., Feng, X., Xu, N., Sun, Y., Wu, X., Yao, X., Mao, Q., Li, X., Dong, W., Wan, X., Huang, N., Shen, X., Liang, Z., and Li, W. (2012) Molecular determinants of enterovirus 71 viral entry: cleft around Gln-172 on VP1 protein interacts with variable region on scavenge receptor B2. J. Biol. Chem. 287, 6406-6420
    • (2012) J. Biol. Chem. , vol.287 , pp. 6406-6420
    • Chen, P.1    Song, Z.2    Qi, Y.3    Feng, X.4    Xu, N.5    Sun, Y.6    Wu, X.7    Yao, X.8    Mao, Q.9    Li, X.10    Dong, W.11    Wan, X.12    Huang, N.13    Shen, X.14    Liang, Z.15    Li, W.16
  • 18
    • 79955405162 scopus 로고    scopus 로고
    • Identification of a human SCARB2 region that is important for enterovirus 71 binding and infection
    • Yamayoshi, S., and Koike, S. (2011) Identification of a human SCARB2 region that is important for enterovirus 71 binding and infection. J. Virol. 85, 4937-4946
    • (2011) J. Virol. , vol.85 , pp. 4937-4946
    • Yamayoshi, S.1    Koike, S.2
  • 21
    • 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 β-glucocerebrosidase
    • Blanz, J., Groth, J., Zachos, C., Wehling, C., Saftig, P., and Schwake, M. (2010) Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand β-glucocerebrosidase. Hum. Mol. Genet. 19, 563-572
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 563-572
    • Blanz, J.1    Groth, J.2    Zachos, C.3    Wehling, C.4    Saftig, P.5    Schwake, M.6
  • 22
    • 84875245748 scopus 로고    scopus 로고
    • Is Parkinson disease associated with lysosomal integral membrane protein type-2?: Challenges in interpreting association data
    • Maniwang, E., Tayebi, N., and Sidransky, E. (2013) Is Parkinson disease associated with lysosomal integral membrane protein type-2?: challenges in interpreting association data. Mol. Genet. Metab. 108, 269-271
    • (2013) Mol. Genet. Metab. , vol.108 , pp. 269-271
    • Maniwang, E.1    Tayebi, N.2    Sidransky, E.3
  • 23
    • 84891372638 scopus 로고    scopus 로고
    • Predicting parkinsonism: New opportunities from Gaucher disease
    • Lopez, G., and Sidransky, E. (2013) Predicting parkinsonism: new opportunities from Gaucher disease. Mol. Genet. Metab. 109, 235-236
    • (2013) Mol. Genet. Metab. , vol.109 , pp. 235-236
    • Lopez, G.1    Sidransky, E.2
  • 24
    • 80052028927 scopus 로고    scopus 로고
    • Exploring the link between glucocerebrosidase mutations and parkinsonism
    • Westbroek, W., Gustafson, A. M., and Sidransky, E. (2011) Exploring the link between glucocerebrosidase mutations and parkinsonism. Trends Mol. Med. 17, 485-493
    • (2011) Trends Mol. Med. , vol.17 , pp. 485-493
    • Westbroek, W.1    Gustafson, A.M.2    Sidransky, E.3
  • 28
    • 0025824346 scopus 로고
    • Human acid β-glucosidase: Use of inhibitory and activating monoclonal antibodies to investigate the enzyme's catalytic mechanism and saposin A and C binding sites
    • Fabbro, D., and Grabowski, G. A. (1991) Human acid β-glucosidase: use of inhibitory and activating monoclonal antibodies to investigate the enzyme's catalytic mechanism and saposin A and C binding sites. J. Biol. Chem. 266, 15021-15027
    • (1991) J. Biol. Chem. , vol.266 , pp. 15021-15027
    • Fabbro, D.1    Grabowski, G.A.2
  • 29
    • 84858296346 scopus 로고    scopus 로고
    • Is E326K glucocerebrosidase a polymorphic or pathological variant?
    • Liou, B., and Grabowski, G. A. (2012) Is E326K glucocerebrosidase a polymorphic or pathological variant? Mol. Genet. Metab. 105, 528-529
    • (2012) Mol. Genet. Metab. , vol.105 , pp. 528-529
    • Liou, B.1    Grabowski, G.A.2
  • 30
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 31
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar, R. C. (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5, 113
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 32
    • 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
  • 33
    • 0033491059 scopus 로고    scopus 로고
    • Utilization of the indirect lysosome targeting pathway by lysosome-associated membrane proteins (LAMPs) is influenced largely by the C-terminal residue of their GYXXφ targeting signals
    • Gough, N. R., Zweifel, M. E., Martinez-Augustin, O., Aguilar, R. C., Bonifacino, J. S., and Fambrough, D. M. (1999) Utilization of the indirect lysosome targeting pathway by lysosome-associated membrane proteins (LAMPs) is influenced largely by the C-terminal residue of their GYXXφ targeting signals. J. Cell Sci. 112, 4257-4269
    • (1999) J. Cell Sci. , vol.112 , pp. 4257-4269
    • Gough, N.R.1    Zweifel, M.E.2    Martinez-Augustin, O.3    Aguilar, R.C.4    Bonifacino, J.S.5    Fambrough, D.M.6
  • 34
    • 0022894660 scopus 로고
    • Biosynthesis, glycosylation, movement through the Golgi system and transport to lysosomes by N-linked carbohydrate-independent mechanism of three lysosomal integral membrane proteins
    • Barriocanal, J. G., Bonifacino, J. S., Yuan, L., and Sandoval, I. V. (1986) Biosynthesis, glycosylation, movement through the Golgi system and transport to lysosomes by N-linked carbohydrate-independent mechanism of three lysosomal integral membrane proteins. J. Biol. Chem. 261, 16755-16763
    • (1986) J. Biol. Chem. , vol.261 , pp. 16755-16763
    • Barriocanal, J.G.1    Bonifacino, J.S.2    Yuan, L.3    Sandoval, I.V.4
  • 35
    • 0030614532 scopus 로고    scopus 로고
    • 2+ and monosaccharide binding to a C-type carbohydrate-recognition domain of the macrophage mannose receptor
    • 2+ and monosaccharide binding to a C-type carbohydrate-recognition domain of the macrophage mannose receptor. J. Biol. Chem. 272, 5668-5681
    • (1997) J. Biol. Chem. , vol.272 , pp. 5668-5681
    • Mullin, N.P.1    Hitchen, P.G.2    Taylor, M.E.3
  • 36
    • 0025608606 scopus 로고
    • Molecular characterization of the human macrophage mannose receptor: Demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells
    • Ezekowitz, R. A., Sastry, K., Bailly, P., and Warner, A. (1990) Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells. J. Exp. Med. 172, 1785-1794
    • (1990) J. Exp. Med. , vol.172 , pp. 1785-1794
    • Ezekowitz, R.A.1    Sastry, K.2    Bailly, P.3    Warner, A.4
  • 37
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors
    • Kornfeld, S. (1992) Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors. Annu. Rev. Biochem. 61, 307-330
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 39
    • 0041355292 scopus 로고    scopus 로고
    • Saposin C is required for normal resistance of acid β-glucosidase to proteolytic degradation
    • Sun, Y., Qi, X., and Grabowski, G. A. (2003) Saposin C is required for normal resistance of acid β-glucosidase to proteolytic degradation. J. Biol. Chem. 278, 31918-31923
    • (2003) J. Biol. Chem. , vol.278 , pp. 31918-31923
    • Sun, Y.1    Qi, X.2    Grabowski, G.A.3
  • 42
    • 84860216725 scopus 로고    scopus 로고
    • Mutant GBA1 expression and synucleinopathy risk: First insights from cellular and mouse models
    • Sardi, S. P., Singh, P., Cheng, S. H., Shihabuddin, L. S., and Schlossmacher, M. G. (2012) Mutant GBA1 expression and synucleinopathy risk: first insights from cellular and mouse models. Neurodegener. Dis. 10, 195-202
    • (2012) Neurodegener. Dis. , vol.10 , pp. 195-202
    • Sardi, S.P.1    Singh, P.2    Cheng, S.H.3    Shihabuddin, L.S.4    Schlossmacher, M.G.5
  • 44
    • 84904469837 scopus 로고    scopus 로고
    • Lysosomal sorting of β-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor
    • Zhao, Y., Ren, J., Padilla-Parra, S., Fry, E. E., and Stuart, D. I. (2014) Lysosomal 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.