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Volumn 18, Issue 9, 2008, Pages 664-678

Strategies for carbohydrate recognition by the mannose 6-phosphate receptors

Author keywords

Lectin; Lysosome; Mannose 6 phosphate receptor; Protein targeting

Indexed keywords

BETA GLUCOSIDASE II; CARBOHYDRATE; CATION DEPENDENT MANNOSE 6 PHOSPHATE; CATION INDEPENDENT MANNOSE 6 PHOSPHATE; ERLECTIN; LECTIN; LYSOSOMAL ENZYME RECEPTOR PROTEIN; LYSOSOME ENZYME; MANNOSE 6 PHOSPHATE; N ACETYLGLUCOSAMINE; N ACETYLGLUCOSAMINE PHOSPHOTRANSFERASE; N ACETYLGLUCOSAMINE PHOSPHOTRANSFERASE GAMMA; PROTEIN OS 9; PROTEIN XTP3 B; UNCLASSIFIED DRUG; GLYCOPROTEIN; MANNOSE PHOSPHATE; MANNOSE-6-PHOSPHATE; OLIGOSACCHARIDE; SOMATOMEDIN B RECEPTOR;

EID: 58149107948     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwn061     Document Type: Review
Times cited : (87)

References (132)
  • 1
    • 0028074281 scopus 로고
    • Glycosylation of recombinant prorenin in insect cells: The insect cell line Sf9 does not express the mannose 6-phosphate recognition signal
    • Aeed PA, Elhammer AP. 1994. Glycosylation of recombinant prorenin in insect cells: The insect cell line Sf9 does not express the mannose 6-phosphate recognition signal. Biochemistry. 33:8793-8797.
    • (1994) Biochemistry , vol.33 , pp. 8793-8797
    • Aeed, P.A.1    Elhammer, A.P.2
  • 2
    • 47749109897 scopus 로고    scopus 로고
    • A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: Inhibiting secretion of misfolded protein conformers and enhancing their disposal
    • Bernasconi R, Pertel T, Luban J, Molinari M. 2008. A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: Inhibiting secretion of misfolded protein conformers and enhancing their disposal. J Biol Chem. 283:16446-16454.
    • (2008) J Biol Chem , vol.283 , pp. 16446-16454
    • Bernasconi, R.1    Pertel, T.2    Luban, J.3    Molinari, M.4
  • 3
    • 24944583185 scopus 로고    scopus 로고
    • Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor misfolded glycoproteins in the ER lumen
    • Bhamidipati A, Denic V, Quan EM, Weissman JS. 2005. Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor misfolded glycoproteins in the ER lumen. Mol Cell. 19:741-751.
    • (2005) Mol Cell , vol.19 , pp. 741-751
    • Bhamidipati, A.1    Denic, V.2    Quan, E.M.3    Weissman, J.S.4
  • 4
    • 0033609918 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor II receptor mediates internalization and degradation of leukemia inhibitory factor but not signal transduction
    • Blanchard F, Duplomb L, Raher S, Vusio P, Hoflack B, Jacques Y, Godard A. 1999. Mannose 6-phosphate/insulin-like growth factor II receptor mediates internalization and degradation of leukemia inhibitory factor but not signal transduction. J Biol Chem. 274:24685-24693.
    • (1999) J Biol Chem , vol.274 , pp. 24685-24693
    • Blanchard, F.1    Duplomb, L.2    Raher, S.3    Vusio, P.4    Hoflack, B.5    Jacques, Y.6    Godard, A.7
  • 5
    • 0032516910 scopus 로고    scopus 로고
    • The mannose 6-phosphate/insulin-like growth factor II receptor is a nanomolar affinity receptor for glycosylated human leukemia inhibitory factor
    • Blanchard F, Raher S, Duplomb L, Vusio P, Pitard V, Taupin JL, Moreau JF, Hoflack B, Minvielle S, Jacques Y, et al. 1998. The mannose 6-phosphate/insulin-like growth factor II receptor is a nanomolar affinity receptor for glycosylated human leukemia inhibitory factor. J Biol Chem. 273:20886-20893.
    • (1998) J Biol Chem , vol.273 , pp. 20886-20893
    • Blanchard, F.1    Raher, S.2    Duplomb, L.3    Vusio, P.4    Pitard, V.5    Taupin, J.L.6    Moreau, J.F.7    Hoflack, B.8    Minvielle, S.9    Jacques, Y.10
  • 6
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: Adaptors on the move
    • Bonifacino JS. 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
  • 7
    • 32944476769 scopus 로고    scopus 로고
    • Enzyme replacement for lysosomal diseases
    • Brady RO. 2006. Enzyme replacement for lysosomal diseases. Annu Rev Med. 57:283-296.
    • (2006) Annu Rev Med , vol.57 , pp. 283-296
    • Brady, R.O.1
  • 8
    • 0026788508 scopus 로고
    • Role of protein phosphatases in insulin-like growth factor II (IGF II)-stimulated mannose 6-phosphate/IGF II receptor redistribution
    • Braulke T,Mieskes G. 1992. Role of protein phosphatases in insulin-like growth factor II (IGF II)-stimulated mannose 6-phosphate/IGF II receptor redistribution. J Biol Chem. 267:17347-17353.
    • (1992) J Biol Chem , vol.267 , pp. 17347-17353
    • Braulke, T.1    Mieskes, G.2
  • 9
    • 1842376232 scopus 로고    scopus 로고
    • Serine phosphorylation site of the 46-kDa mannose 6-phosphate receptor is required for transport to the plasma membrane in Madin-Darby canine kidney and mouse fibroblast cells
    • Breuer P, Korner C, Boker C, Herzog A, Pohlmann R, Braulke T. 1997. Serine phosphorylation site of the 46-kDa mannose 6-phosphate receptor is required for transport to the plasma membrane in Madin-Darby canine kidney and mouse fibroblast cells. Mol Biol Cell. 8:567-576.
    • (1997) Mol Biol Cell , vol.8 , pp. 567-576
    • Breuer, P.1    Korner, C.2    Boker, C.3    Herzog, A.4    Pohlmann, R.5    Braulke, T.6
  • 11
    • 0036499988 scopus 로고    scopus 로고
    • Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur
    • Brown J, Esnouf RM, Jones MA, Linnell J, Harlos K, Hassan AB, Jones EY. 2002. Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur. EMBO J. 21:1054-1062.
    • (2002) EMBO J , vol.21 , pp. 1054-1062
    • Brown, J.1    Esnouf, R.M.2    Jones, M.A.3    Linnell, J.4    Harlos, K.5    Hassan, A.B.6    Jones, E.Y.7
  • 12
    • 0028287949 scopus 로고
    • Herpes simplex virus glycoprotein D acquires mannose 6-phosphate residues and binds to mannose 6-phosphate receptors
    • Brunetti CR, Burke RL, Kornfeld S, Gregory W, Masiarz FR, Dingwell KS, Johnson DC. 1994. Herpes simplex virus glycoprotein D acquires mannose 6-phosphate residues and binds to mannose 6-phosphate receptors. J Biol Chem. 269:17067-17074.
    • (1994) J Biol Chem , vol.269 , pp. 17067-17074
    • Brunetti, C.R.1    Burke, R.L.2    Kornfeld, S.3    Gregory, W.4    Masiarz, F.R.5    Dingwell, K.S.6    Johnson, D.C.7
  • 13
    • 35848956125 scopus 로고    scopus 로고
    • Domain 5 of the cation-independent mannose 6-phosphate receptor preferentially binds phosphodiesters (mannose 6-phosphate N acetylglucosamine ester)
    • Chavez CA, Bohnsack RN, Kudo M, Gotschall RR, Canfield WM, Dahms NM. 2007. Domain 5 of the cation-independent mannose 6-phosphate receptor preferentially binds phosphodiesters (mannose 6-phosphate N acetylglucosamine ester). Biochemistry. 46:12604-12617.
    • (2007) Biochemistry , vol.46 , pp. 12604-12617
    • Chavez, C.A.1    Bohnsack, R.N.2    Kudo, M.3    Gotschall, R.R.4    Canfield, W.M.5    Dahms, N.M.6
  • 14
    • 11144324373 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptor dependence of varicella zoster virus infection in vitro and in the epidermis during varicella and zoster
    • Chen JJ, Zhu Z, Gershon AA, Gershon MD. 2004. Mannose 6-phosphate receptor dependence of varicella zoster virus infection in vitro and in the epidermis during varicella and zoster. Cell. 119:915-926.
    • (2004) Cell , vol.119 , pp. 915-926
    • Chen, J.J.1    Zhu, Z.2    Gershon, A.A.3    Gershon, M.D.4
  • 15
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 delivermutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson JC, Shaler TA, Tyler RE, Kopito RR. 2008. OS-9 and GRP94 delivermutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol. 10:272-282.
    • (2008) Nat Cell Biol , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 16
    • 0029166451 scopus 로고
    • Protein trafficking in kinetoplastid protozoa
    • Clayton C, Hausler T, Blattner J. 1995. Protein trafficking in kinetoplastid protozoa. Microbiol Rev. 59:325-344.
    • (1995) Microbiol Rev , vol.59 , pp. 325-344
    • Clayton, C.1    Hausler, T.2    Blattner, J.3
  • 17
    • 33744965386 scopus 로고    scopus 로고
    • The MRH protein erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition
    • Cruciat CM, Hassler C, Niehrs C. 2006. The MRH protein erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition. J Biol Chem. 281:12986-12993.
    • (2006) J Biol Chem , vol.281 , pp. 12986-12993
    • Cruciat, C.M.1    Hassler, C.2    Niehrs, C.3
  • 18
    • 31644441420 scopus 로고    scopus 로고
    • Proteomic analysis of lysosomal acid hydrolases secreted by osteoclasts: Implications for lytic enzyme transport and bone metabolism
    • Czupalla C, Mansukoski H, Riedl T, Thiel D, Krause E, Hoflack B. 2006. Proteomic analysis of lysosomal acid hydrolases secreted by osteoclasts: Implications for lytic enzyme transport and bone metabolism. Mol Cell Proteomics. 5:134-143.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 134-143
    • Czupalla, C.1    Mansukoski, H.2    Riedl, T.3    Thiel, D.4    Krause, E.5    Hoflack, B.6
  • 20
    • 0028101930 scopus 로고
    • The bovine mannose 6-phosphate/insulin-like growth factor II receptor. Localization of the insulin-like growth factor II binding site to domains 5-11
    • Dahms NM, Wick DA, Brzycki-Wessell MA. 1994. The bovine mannose 6-phosphate/insulin-like growth factor II receptor. Localization of the insulin-like growth factor II binding site to domains 5-11. J Biol Chem. 269:3802-3809.
    • (1994) J Biol Chem , vol.269 , pp. 3802-3809
    • Dahms, N.M.1    Wick, D.A.2    Brzycki-Wessell, M.A.3
  • 21
    • 0035943416 scopus 로고    scopus 로고
    • Intracellular cycling of lysosomal enzyme receptors. Cytoplasmic tails' tales
    • Dell' Angelica EC, Payne GS. 2001. Intracellular cycling of lysosomal enzyme receptors. Cytoplasmic tails' tales. Cell. 106:395-398.
    • (2001) Cell , vol.106 , pp. 395-398
    • Dell' Angelica, E.C.1    Payne, G.S.2
  • 22
    • 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 NS, Eble JA, Hahnenkamp A, 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
  • 23
    • 0026059613 scopus 로고
    • Cellular activation of latent transforming growth factor beta requires binding to the cation-independent mannose 6-phosphate/insulin-like growth factor type II receptor
    • Dennis PA, Rifkin DB. 1991. Cellular activation of latent transforming growth factor beta requires binding to the cation-independent mannose 6-phosphate/insulin-like growth factor type II receptor. Proc Natl Acad Sci USA. 88:580-584.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 580-584
    • Dennis, P.A.1    Rifkin, D.B.2
  • 24
    • 0031724560 scopus 로고    scopus 로고
    • An insulin-like growth factor II (IGF-II) affinity-enhancing domain localized within extracytoplasmic repeat 13 of the IGF-II/mannose 6- phosphate receptor
    • Devi GR, Byrd JC, Slentz DH, MacDonald RG. 1998. An insulin-like growth factor II (IGF-II) affinity-enhancing domain localized within extracytoplasmic repeat 13 of the IGF-II/mannose 6- phosphate receptor. Mol Endocrinol. 12:1661-1672.
    • (1998) Mol Endocrinol , vol.12 , pp. 1661-1672
    • Devi, G.R.1    Byrd, J.C.2    Slentz, D.H.3    MacDonald, R.G.4
  • 25
    • 0041834587 scopus 로고    scopus 로고
    • The secreted glycoprotein CREG inhibits cell growth dependent on the mannose-6-phosphate/insulin-like growth factor II receptor
    • Di Bacco A, Gill G. 2003. The secreted glycoprotein CREG inhibits cell growth dependent on the mannose-6-phosphate/insulin-like growth factor II receptor. Oncogene. 22:5436-5445.
    • (2003) Oncogene , vol.22 , pp. 5436-5445
    • Di Bacco, A.1    Gill, G.2
  • 26
    • 0018293353 scopus 로고
    • Identification of mannose 6-phosphate in glycoproteins that inhibit the assimilation of beta-galactosidase by fibroblasts
    • Distler J, Hieber V, Sahagian G, Schmickel R, Jourdian GW. 1979. Identification of mannose 6-phosphate in glycoproteins that inhibit the assimilation of beta-galactosidase by fibroblasts. Proc Natl Acad Sci USA. 76:4235-4239.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4235-4239
    • Distler, J.1    Hieber, V.2    Sahagian, G.3    Schmickel, R.4    Jourdian, G.W.5
  • 27
    • 0025885735 scopus 로고
    • The binding specificity of high and low molecular weight phosphomannosyl receptors from bovine testes. Inhibition studies with chemically synthesized 6-O-phosphorylated oligomannosides
    • Distler JJ, Guo JF, Jourdian GW, Srivastava OP, Hindsgaul O. 1991. The binding specificity of high and low molecular weight phosphomannosyl receptors from bovine testes. Inhibition studies with chemically synthesized 6-O-phosphorylated oligomannosides. J Biol Chem. 266:21687-21692.
    • (1991) J Biol Chem , vol.266 , pp. 21687-21692
    • Distler, J.J.1    Guo, J.F.2    Jourdian, G.W.3    Srivastava, O.P.4    Hindsgaul, O.5
  • 29
    • 0037119355 scopus 로고    scopus 로고
    • Human mannose 6-phosphate-uncovering enzyme is synthesized as a proenzyme that is activated by the endoprotease furin
    • Do H, Lee WS, Ghosh P, Hollowell T, Canfield W, Kornfeld S. 2002. Human mannose 6-phosphate-uncovering enzyme is synthesized as a proenzyme that is activated by the endoprotease furin. J Biol Chem. 277:29737-29744.
    • (2002) J Biol Chem , vol.277 , pp. 29737-29744
    • Do, H.1    Lee, W.S.2    Ghosh, P.3    Hollowell, T.4    Canfield, W.5    Kornfeld, S.6
  • 30
    • 0034920428 scopus 로고    scopus 로고
    • Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity
    • Dodd RB, Drickamer K. 2001. Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity. Glycobiology. 11:71R-79R.
    • (2001) Glycobiology , vol.11
    • Dodd, R.B.1    Drickamer, K.2
  • 31
    • 0032860314 scopus 로고    scopus 로고
    • C-type lectin-like domains
    • Drickamer K. 1999. C-type lectin-like domains. Curr Opin Struct Biol 9:585-590.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 585-590
    • Drickamer, K.1
  • 32
    • 0023550868 scopus 로고
    • Renin, a secretory glycoprotein, acquires phosphomannosyl residues
    • Faust PL, Chirgwin JM, Kornfeld S. 1987. Renin, a secretory glycoprotein, acquires phosphomannosyl residues. J Cell Biol. 105:1947-1955.
    • (1987) J Cell Biol , vol.105 , pp. 1947-1955
    • Faust, P.L.1    Chirgwin, J.M.2    Kornfeld, S.3
  • 33
    • 0022834819 scopus 로고
    • Modifications of lysosomal enzymes in Dictyostelium discoideum
    • Freeze HH. 1986. Modifications of lysosomal enzymes in Dictyostelium discoideum. Mol Cell Biochem. 72:47-65.
    • (1986) Mol Cell Biochem , vol.72 , pp. 47-65
    • Freeze, H.H.1
  • 34
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • Futerman AH, van Meer G. 2004. The cell biology of lysosomal storage disorders. Nat Rev Mol Cell Biol. 5:554-565.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 554-565
    • Futerman, A.H.1    van Meer, G.2
  • 35
    • 0021746042 scopus 로고
    • Identification of methylphosphomannosyl residues as components of the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins
    • Gabel CA, Costello CE, Reinhold VN, Kurz L, Kornfeld S. 1984. Identification of methylphosphomannosyl residues as components of the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins. J Biol Chem. 259:13762-13769.
    • (1984) J Biol Chem , vol.259 , pp. 13762-13769
    • Gabel, C.A.1    Costello, C.E.2    Reinhold, V.N.3    Kurz, L.4    Kornfeld, S.5
  • 36
    • 0024434510 scopus 로고
    • Varicella-zoster virus glycoprotein oligosaccharides are phosphorylated during posttranslational maturation
    • Gabel CA, Dubey L, Steinberg SP, Sherman D, Gershon MD, Gershon AA. 1989. Varicella-zoster virus glycoprotein oligosaccharides are phosphorylated during posttranslational maturation. J Virol. 63:4264-4276.
    • (1989) J Virol , vol.63 , pp. 4264-4276
    • Gabel, C.A.1    Dubey, L.2    Steinberg, S.P.3    Sherman, D.4    Gershon, M.D.5    Gershon, A.A.6
  • 37
    • 36849049303 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptor targeting and its applications in human diseases
    • Gary-Bobo M, Nirde P, Jeanjean A, Morere A, Garcia M. 2007. Mannose 6-phosphate receptor targeting and its applications in human diseases. Curr Med Chem. 14:2945-2953.
    • (2007) Curr Med Chem , vol.14 , pp. 2945-2953
    • Gary-Bobo, M.1    Nirde, P.2    Jeanjean, A.3    Morere, A.4    Garcia, M.5
  • 38
    • 0026318490 scopus 로고
    • Purification of a lysosomal DNase from Drosophila melanogaster
    • Gaszner M, Udvardy A. 1991. Purification of a lysosomal DNase from Drosophila melanogaster. Biochem Biophys Res Commun. 181:44-50.
    • (1991) Biochem Biophys Res Commun , vol.181 , pp. 44-50
    • Gaszner, M.1    Udvardy, A.2
  • 39
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: New twists in the tale
    • Ghosh P, Dahms NM, Kornfeld S. 2003. Mannose 6-phosphate receptors: New twists in the tale. Nat Rev Mol Cell Biol. 4:202-213.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 202-213
    • Ghosh, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 40
    • 4744364138 scopus 로고    scopus 로고
    • The GGA proteins: Key players in protein sorting at the trans-Golgi network
    • Ghosh P, Kornfeld S. 2004. The GGA proteins: Key players in protein sorting at the trans-Golgi network. Eur J Cell Biol. 83:257-262.
    • (2004) Eur J Cell Biol , vol.83 , pp. 257-262
    • Ghosh, P.1    Kornfeld, S.2
  • 41
    • 0344026339 scopus 로고    scopus 로고
    • M6P/IGFII-receptor complexes urokinase receptor and plasminogen for activation of transforming growth factor-beta1
    • Godar S, Horejsi V, Weidle UH, Binder BR, Hansmann C, Stockinger H. 1999. M6P/IGFII-receptor complexes urokinase receptor and plasminogen for activation of transforming growth factor-beta1. Eur J Immunol. 29:1004-1013.
    • (1999) Eur J Immunol , vol.29 , pp. 1004-1013
    • Godar, S.1    Horejsi, V.2    Weidle, U.H.3    Binder, B.R.4    Hansmann, C.5    Stockinger, H.6
  • 42
    • 0027452741 scopus 로고
    • Granzymes A and B are targeted to the lytic granules of lymphocytes by the mannose-6-phosphate receptor
    • Griffiths GM, Isaaz S. 1993. Granzymes A and B are targeted to the lytic granules of lymphocytes by the mannose-6-phosphate receptor. J Cell Biol. 120:885-896.
    • (1993) J Cell Biol , vol.120 , pp. 885-896
    • Griffiths, G.M.1    Isaaz, S.2
  • 43
    • 0037192762 scopus 로고    scopus 로고
    • Identification of residues essential for carbohydrate recognition by the insulin-like growth factor II/mannose 6-phosphate receptor
    • Hancock MK, Haskins DJ, Sun G, Dahms NM. 2002. Identification of residues essential for carbohydrate recognition by the insulin-like growth factor II/mannose 6-phosphate receptor. J Biol Chem. 277:11255-11264.
    • (2002) J Biol Chem , vol.277 , pp. 11255-11264
    • Hancock, M.K.1    Haskins, D.J.2    Sun, G.3    Dahms, N.M.4
  • 44
    • 0037033019 scopus 로고    scopus 로고
    • Localization of the carbohydrate recognition sites of the insulin-like growth factor II/mannose 6-phosphate receptor to domains 3 and 9 of the extracytoplasmic region
    • Hancock MK, Yammani RD, Dahms NM. 2002. Localization of the carbohydrate recognition sites of the insulin-like growth factor II/mannose 6-phosphate receptor to domains 3 and 9 of the extracytoplasmic region. J Biol Chem. 277:47205-47212.
    • (2002) J Biol Chem , vol.277 , pp. 47205-47212
    • Hancock, M.K.1    Yammani, R.D.2    Dahms, N.M.3
  • 45
    • 0019132607 scopus 로고
    • Phosphorylated oligosaccharides in lysosomal enzymes: Identification of alpha-N-acetylglucosamine(1)phospho(6)mannose diester groups
    • Hasilik A, Klein U, Waheed A, Strecker G, von Figura K. 1980. Phosphorylated oligosaccharides in lysosomal enzymes: Identification of alpha-N-acetylglucosamine(1)phospho(6)mannose diester groups. Proc Natl Acad Sci USA. 77:7074-7078.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 7074-7078
    • Hasilik, A.1    Klein, U.2    Waheed, A.3    Strecker, G.4    von Figura, K.5
  • 46
    • 0015511150 scopus 로고
    • A hypothesis for I-cell disease: Defective hydrolases that do not enter lysosomes
    • Hickman S, Neufeld EF. 1972. A hypothesis for I-cell disease: Defective hydrolases that do not enter lysosomes. Biochem Biophys Res Commun 49:992-999.
    • (1972) Biochem Biophys Res Commun , vol.49 , pp. 992-999
    • Hickman, S.1    Neufeld, E.F.2
  • 47
    • 0023135074 scopus 로고
    • The interaction of phosphorylated oligosaccharides and lysosomal enzymeswith bovine liver cation-dependent mannose 6-phosphate receptor
    • Hoflack B, Fujimoto K, Kornfeld S. 1987. The interaction of phosphorylated oligosaccharides and lysosomal enzymeswith bovine liver cation-dependent mannose 6-phosphate receptor. J Biol Chem. 262:123-129.
    • (1987) J Biol Chem , vol.262 , pp. 123-129
    • Hoflack, B.1    Fujimoto, K.2    Kornfeld, S.3
  • 48
    • 0038731890 scopus 로고
    • Lysosomal enzyme binding to mouse P388D1 macrophage membranes lacking the 215-kDa mannose 6-phosphate receptor: Evidence for the existence of a second mannose 6-phosphate receptor
    • Hoflack B, Kornfeld S. 1985. Lysosomal enzyme binding to mouse P388D1 macrophage membranes lacking the 215-kDa mannose 6-phosphate receptor: Evidence for the existence of a second mannose 6-phosphate receptor. Proc Natl Acad Sci USA. 82:4428-4432.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4428-4432
    • Hoflack, B.1    Kornfeld, S.2
  • 49
    • 0039702904 scopus 로고    scopus 로고
    • Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif
    • Huete-Perez JA, Engel JC, Brinen LS, Mottram JC, McKerrow JH. 1999. Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif. J Biol Chem. 274:16249-16256.
    • (1999) J Biol Chem , vol.274 , pp. 16249-16256
    • Huete-Perez, J.A.1    Engel, J.C.2    Brinen, L.S.3    Mottram, J.C.4    McKerrow, J.H.5
  • 51
    • 0020559445 scopus 로고
    • Biosynthesis and transport of lysosomal enzymes in human monocytes and macrophages. Effects of ammonium chloride, zymosan and tunicamycin
    • Imort M, Zuhlsdorf M, Feige U, Hasilik A, von Figura K. 1983. Biosynthesis and transport of lysosomal enzymes in human monocytes and macrophages. Effects of ammonium chloride, zymosan and tunicamycin. Biochem J. 214:671-678.
    • (1983) Biochem J , vol.214 , pp. 671-678
    • Imort, M.1    Zuhlsdorf, M.2    Feige, U.3    Hasilik, A.4    von Figura, K.5
  • 53
    • 0036668520 scopus 로고    scopus 로고
    • Proteomic analysis of human lysosomes: Application to monocytic and breast cancer cells
    • Journet A, Chapel A, Kieffer S, Roux F, Garin J. 2002. Proteomic analysis of human lysosomes: Application to monocytic and breast cancer cells. Proteomics. 2:1026-1040.
    • (2002) Proteomics , vol.2 , pp. 1026-1040
    • Journet, A.1    Chapel, A.2    Kieffer, S.3    Roux, F.4    Garin, J.5
  • 54
    • 0031456570 scopus 로고    scopus 로고
    • Mannose-6-phosphate/insulin-like growth factor-II receptor is a receptor for retinoic acid
    • Kang JX, Li Y, Leaf A. 1997. Mannose-6-phosphate/insulin-like growth factor-II receptor is a receptor for retinoic acid. Proc Natl Acad Sci USA. 94:13671-13676.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13671-13676
    • Kang, J.X.1    Li, Y.2    Leaf, A.3
  • 55
    • 0011596655 scopus 로고
    • Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts
    • SlyWS
    • Kaplan A, Achord DT, SlyWS. 1977. Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts. Proc Natl Acad Sci USA. 74:2026-2030.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2026-2030
    • Kaplan, A.1    Achord, D.T.2
  • 56
    • 0029737710 scopus 로고    scopus 로고
    • Neither type of mannose 6-phosphate receptor is sufficient for targeting of lysosomal enzymes along intracellular routes
    • Kasper D, Dittmer F, von Figura K, Pohlmann R. 1996. Neither type of mannose 6-phosphate receptor is sufficient for targeting of lysosomal enzymes along intracellular routes. J Cell Biol. 134:615-623.
    • (1996) J Cell Biol , vol.134 , pp. 615-623
    • Kasper, D.1    Dittmer, F.2    von Figura, K.3    Pohlmann, R.4
  • 57
    • 24944552879 scopus 로고    scopus 로고
    • Yos9p detects and targets misfolded glycoproteins for ER-associated degradation
    • Kim W, Spear ED, Ng DT. 2005. Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell. 19:753-764.
    • (2005) Mol Cell , vol.19 , pp. 753-764
    • Kim, W.1    Spear, E.D.2    Ng, D.T.3
  • 58
    • 0031970586 scopus 로고    scopus 로고
    • Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines
    • Kimura Y, Nakazawa M, Yamada M. 1998. Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines. J Biochem. 123:876-882.
    • (1998) J Biochem , vol.123 , pp. 876-882
    • Kimura, Y.1    Nakazawa, M.2    Yamada, M.3
  • 59
    • 0001261457 scopus 로고    scopus 로고
    • I cell disease and pseudo-Hurler polydystrophy: Disorders of lysosomal enzyme phosphorylation and localization
    • Scriver CR, Beaudet AL, SlyWS, Valle D, editors, New York: McGraw-Hill. pp
    • Kornfeld S, Sly WS. 2001. I cell disease and pseudo-Hurler polydystrophy: Disorders of lysosomal enzyme phosphorylation and localization. In: Scriver CR, Beaudet AL, SlyWS, Valle D, editors. Metabolic and Molecular Bases of Inherited Diseases. New York: McGraw-Hill. pp. 3469-3482.
    • (2001) Metabolic and Molecular Bases of Inherited Diseases , pp. 3469-3482
    • Kornfeld, S.1    Sly, W.S.2
  • 60
    • 0038419654 scopus 로고    scopus 로고
    • Kreiling JL, Byrd JC, Deisz RJ, Mizukami IF, Todd RF 3rd3rd, MacDonald RG. 2003. Binding of Urokinase-type plasminogen activator receptor (uPAR) to the mannose 6-phosphate/insulin-like growth factor II receptor: Contrasting interactions of full-length and soluble forms of uPAR. J Biol Chem. 278:20628-20637.
    • Kreiling JL, Byrd JC, Deisz RJ, Mizukami IF, Todd RF 3rd3rd, MacDonald RG. 2003. Binding of Urokinase-type plasminogen activator receptor (uPAR) to the mannose 6-phosphate/insulin-like growth factor II receptor: Contrasting interactions of full-length and soluble forms of uPAR. J Biol Chem. 278:20628-20637.
  • 61
    • 33344471661 scopus 로고    scopus 로고
    • Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase alpha/beta-subunits precursor gene
    • Kudo M, Brem MS, Canfield WM. 2006. Mucolipidosis II (I-cell disease) and mucolipidosis IIIA (classical pseudo-hurler polydystrophy) are caused by mutations in the GlcNAc-phosphotransferase alpha/beta-subunits precursor gene. Am J Hum Genet. 78:451-463.
    • (2006) Am J Hum Genet , vol.78 , pp. 451-463
    • Kudo, M.1    Brem, M.S.2    Canfield, W.M.3
  • 62
    • 0033510416 scopus 로고    scopus 로고
    • Identification of the putative mannose 6-phosphate receptor protein (MPR 300) in the invertebrate unio
    • Lakshmi YU, Radha Y, Hille-Rehfeld A, von Figura K, Kumar NS. 1999. Identification of the putative mannose 6-phosphate receptor protein (MPR 300) in the invertebrate unio. Biosci Rep. 19:403-409.
    • (1999) Biosci Rep , vol.19 , pp. 403-409
    • Lakshmi, Y.U.1    Radha, Y.2    Hille-Rehfeld, A.3    von Figura, K.4    Kumar, N.S.5
  • 63
    • 0022996804 scopus 로고
    • Glycoprotein phosphorylation in simple eucaryotic organisms. Identification of UDP-GlcNAc:gLycoprotein N-acetylglucosamine-1-phosphotransferase activity and analysis of substrate specificity
    • Lang L, Couso R, Kornfeld S. 1986. Glycoprotein phosphorylation in simple eucaryotic organisms. Identification of UDP-GlcNAc:gLycoprotein N-acetylglucosamine-1-phosphotransferase activity and analysis of substrate specificity. J Biol Chem. 261:6320-6325.
    • (1986) J Biol Chem , vol.261 , pp. 6320-6325
    • Lang, L.1    Couso, R.2    Kornfeld, S.3
  • 64
    • 0023753261 scopus 로고
    • Biosynthesis of the mannose 6-phosphate recognition marker in transport-impaired mouse lymphoma cells. Demonstration of a two-step phosphorylation
    • Lazzarino DA, Gabel CA. 1988. Biosynthesis of the mannose 6-phosphate recognition marker in transport-impaired mouse lymphoma cells. Demonstration of a two-step phosphorylation. J Biol Chem. 263:10118-10126.
    • (1988) J Biol Chem , vol.263 , pp. 10118-10126
    • Lazzarino, D.A.1    Gabel, C.A.2
  • 65
    • 0032516810 scopus 로고    scopus 로고
    • Protein transport from the secretory to the endocytic pathway in mammalian cells
    • Le Borgne R, Hoflack B. 1998. Protein transport from the secretory to the endocytic pathway in mammalian cells. Biochim Biophys Acta. 1404:195-209.
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 195-209
    • Le Borgne, R.1    Hoflack, B.2
  • 66
    • 0023860003 scopus 로고
    • Proliferin secreted by cultured cells binds to mannose 6-phosphate receptors
    • Lee SJ, Nathans D. 1988. Proliferin secreted by cultured cells binds to mannose 6-phosphate receptors. J Biol Chem. 263:3521-3527.
    • (1988) J Biol Chem , vol.263 , pp. 3521-3527
    • Lee, S.J.1    Nathans, D.2
  • 67
    • 34848903008 scopus 로고    scopus 로고
    • Murine UDP-GlcNAc: Lysosomal enzyme N acetylglucosamine-1-phosphotransferase lacking the gamma-subunit retains substantial activity toward acid hydrolases
    • Lee WS, Payne BJ, Gelfman CM, Vogel P, Kornfeld S. 2007. Murine UDP-GlcNAc: Lysosomal enzyme N acetylglucosamine-1-phosphotransferase lacking the gamma-subunit retains substantial activity toward acid hydrolases. J Biol Chem. 282:27198-27203.
    • (2007) J Biol Chem , vol.282 , pp. 27198-27203
    • Lee, W.S.1    Payne, B.J.2    Gelfman, C.M.3    Vogel, P.4    Kornfeld, S.5
  • 68
    • 0037174862 scopus 로고    scopus 로고
    • The N terminus of mannose 6-phosphate/ insulin-like growth factor 2 receptor in regulation of fibrinolysis and cell migration
    • StockingerH
    • Leksa V, Godar S, Cebecauer M, Hilgert I, Breuss J, Weidle UH, Horejsi V, Binder BR, StockingerH. 2002. The N terminus of mannose 6-phosphate/ insulin-like growth factor 2 receptor in regulation of fibrinolysis and cell migration. J Biol Chem. 277:40575-40582.
    • (2002) J Biol Chem , vol.277 , pp. 40575-40582
    • Leksa, V.1    Godar, S.2    Cebecauer, M.3    Hilgert, I.4    Breuss, J.5    Weidle, U.H.6    Horejsi, V.7    Binder, B.R.8
  • 69
    • 33947685420 scopus 로고    scopus 로고
    • The cation-independent mannose 6-phosphate receptor is involved in lysosomal delivery of serglycin
    • Lemansky P, Fester I, Smolenova E, Uhlander C, Hasilik A. 2007. The cation-independent mannose 6-phosphate receptor is involved in lysosomal delivery of serglycin. J Leukoc Biol. 81:1149-1158.
    • (2007) J Leukoc Biol , vol.81 , pp. 1149-1158
    • Lemansky, P.1    Fester, I.2    Smolenova, E.3    Uhlander, C.4    Hasilik, A.5
  • 70
    • 0035968216 scopus 로고    scopus 로고
    • Real time kinetics of insulin-like growth factor II (IGF-II) interaction with the IGF-II/ mannose 6-phosphate receptor. The effects of domain 13 and pH
    • Linnell J, Groeger G, Hassan AB. 2001. Real time kinetics of insulin-like growth factor II (IGF-II) interaction with the IGF-II/ mannose 6-phosphate receptor. The effects of domain 13 and pH. J Biol Chem. 276:23986-23991.
    • (2001) J Biol Chem , vol.276 , pp. 23986-23991
    • Linnell, J.1    Groeger, G.2    Hassan, A.B.3
  • 71
    • 0030221121 scopus 로고    scopus 로고
    • Ludwig T, Eggenschwiler J, Fisher P, D Ercole AJ, Davenport ML, Efstratiadis A. 1996. Mouse mutants lacking the type 2 IGF receptor (IGF2R) are rescued from perinatal lethality in Igf2 and Igf1r null backgrounds. Dev Biol. 177:517-535.
    • Ludwig T, Eggenschwiler J, Fisher P, D Ercole AJ, Davenport ML, Efstratiadis A. 1996. Mouse mutants lacking the type 2 IGF receptor (IGF2R) are rescued from perinatal lethality in Igf2 and Igf1r null backgrounds. Dev Biol. 177:517-535.
  • 72
    • 0027932822 scopus 로고
    • Differential sorting of lysosomal enzymes in mannose 6-phosphate receptor-deficient fibroblasts
    • Ludwig T, Munier-Lehmann H, Bauer U, Hollinshead M, Ovitt C, Lobel P, Hoflack B. 1994. Differential sorting of lysosomal enzymes in mannose 6-phosphate receptor-deficient fibroblasts. EMBO J. 13:3430-3437.
    • (1994) EMBO J , vol.13 , pp. 3430-3437
    • Ludwig, T.1    Munier-Lehmann, H.2    Bauer, U.3    Hollinshead, M.4    Ovitt, C.5    Lobel, P.6    Hoflack, B.7
  • 73
    • 0034056050 scopus 로고    scopus 로고
    • Recognition of Dictyostelium discoideum lysosomal enzymes is conferred by the amino-terminal carbohydrate binding site of the insulin-like growth factor II/mannose 6-phosphate receptor
    • Marron-Terada PG, Hancock MK, Haskins DJ, Dahms NM. 2000. Recognition of Dictyostelium discoideum lysosomal enzymes is conferred by the amino-terminal carbohydrate binding site of the insulin-like growth factor II/mannose 6-phosphate receptor. Biochemistry. 39:2243-2253.
    • (2000) Biochemistry , vol.39 , pp. 2243-2253
    • Marron-Terada, P.G.1    Hancock, M.K.2    Haskins, D.J.3    Dahms, N.M.4
  • 74
    • 0346059334 scopus 로고    scopus 로고
    • Lysosomal storage disorders: Emerging therapeutic options require early diagnosis
    • Meikle PJ, Hopwood JJ. 2003. Lysosomal storage disorders: Emerging therapeutic options require early diagnosis. Eur J Pediatr. 162:S34-S37.
    • (2003) Eur J Pediatr , vol.162
    • Meikle, P.J.1    Hopwood, J.J.2
  • 75
    • 0027393090 scopus 로고
    • Phosphorylation of the cation-independent mannose 6-phosphate receptor is closely associated with its exit from the trans-Golgi network
    • Meresse S, Hoflack B. 1993. Phosphorylation of the cation-independent mannose 6-phosphate receptor is closely associated with its exit from the trans-Golgi network. J Cell Biol. 120:67-75.
    • (1993) J Cell Biol , vol.120 , pp. 67-75
    • Meresse, S.1    Hoflack, B.2
  • 76
    • 34547571027 scopus 로고    scopus 로고
    • TheM-Coffee web server: A meta-method for computing multiple sequence alignments by combining alternative alignment methods
    • Moretti S, Armougom F, Wallace IM, Higgins DG, Jongeneel CV, Notredame C. 2007. TheM-Coffee web server: A meta-method for computing multiple sequence alignments by combining alternative alignment methods. Nucleic Acids Res. 35:W645-W648.
    • (2007) Nucleic Acids Res , vol.35
    • Moretti, S.1    Armougom, F.2    Wallace, I.M.3    Higgins, D.G.4    Jongeneel, C.V.5    Notredame, C.6
  • 77
    • 0035074341 scopus 로고    scopus 로고
    • The molecular machinery for lysosome biogenesis
    • Mullins C, Bonifacino JS. 2001. The molecular machinery for lysosome biogenesis. Bioessays. 23:333-343.
    • (2001) Bioessays , vol.23 , pp. 333-343
    • Mullins, C.1    Bonifacino, J.S.2
  • 78
    • 0029883027 scopus 로고    scopus 로고
    • Re-expression of the mannose 6-phosphate receptors in receptor-deficient fibroblasts. Complementary function of the two mannose 6-phosphate receptors in lysosomal enzyme targeting
    • Munier-Lehmann H, Mauxion F, Bauer U, Lobel P, Hoflack B. 1996. Re-expression of the mannose 6-phosphate receptors in receptor-deficient fibroblasts. Complementary function of the two mannose 6-phosphate receptors in lysosomal enzyme targeting. J Biol Chem. 271:15166-15174.
    • (1996) J Biol Chem , vol.271 , pp. 15166-15174
    • Munier-Lehmann, H.1    Mauxion, F.2    Bauer, U.3    Lobel, P.4    Hoflack, B.5
  • 79
    • 0035838410 scopus 로고    scopus 로고
    • The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins
    • Munro S. 2001. The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins. Curr Biol. 11:R499-R501.
    • (2001) Curr Biol , vol.11
    • Munro, S.1
  • 80
    • 4444241847 scopus 로고    scopus 로고
    • Biochemical and immunological characterization of a glycosylated alpha-fucosidase from the invertebrate Unio: Interaction of the enzyme with its in vivo binding partners
    • Nadimpalli SK, Padmanabhan N, Koduru S. 2004. Biochemical and immunological characterization of a glycosylated alpha-fucosidase from the invertebrate Unio: Interaction of the enzyme with its in vivo binding partners. Protein Expr Purif. 37:279-287.
    • (2004) Protein Expr Purif , vol.37 , pp. 279-287
    • Nadimpalli, S.K.1    Padmanabhan, N.2    Koduru, S.3
  • 81
    • 0242515804 scopus 로고    scopus 로고
    • Identification of the putative mannose 6-phosphate receptor (MPR 46) protein in the invertebrate mollusc
    • Nadimpalli SK, von Figura K. 2002. Identification of the putative mannose 6-phosphate receptor (MPR 46) protein in the invertebrate mollusc. Biosci Rep. 22:513-521.
    • (2002) Biosci Rep , vol.22 , pp. 513-521
    • Nadimpalli, S.K.1    von Figura, K.2
  • 82
    • 0018305643 scopus 로고
    • Enzymatic identification of mannose 6-phosphate on the recognition marker for receptor-mediated pinocytosis of beta-glucuronidase by human fibroblasts
    • Natowicz MR, Chi MM, Lowry OH, Sly WS. 1979. Enzymatic identification of mannose 6-phosphate on the recognition marker for receptor-mediated pinocytosis of beta-glucuronidase by human fibroblasts. Proc Natl Acad Sci USA. 76:4322-4326.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4322-4326
    • Natowicz, M.R.1    Chi, M.M.2    Lowry, O.H.3    Sly, W.S.4
  • 83
    • 0025826050 scopus 로고
    • Lysosomal storage diseases
    • Neufeld EF. 1991. Lysosomal storage diseases. Annu Rev Biochem. 60:257-280.
    • (1991) Annu Rev Biochem , vol.60 , pp. 257-280
    • Neufeld, E.F.1
  • 84
    • 33746174512 scopus 로고    scopus 로고
    • The sorting and trafficking of lysosomal proteins
    • Ni X, Canuel M, Morales CR. 2006. The sorting and trafficking of lysosomal proteins. Histol Histopathol. 21:899-913.
    • (2006) Histol Histopathol , vol.21 , pp. 899-913
    • Ni, X.1    Canuel, M.2    Morales, C.R.3
  • 87
    • 4043147868 scopus 로고    scopus 로고
    • The N-terminal carbohydrate recognition site of the cation-independent mannose 6-phosphate receptor
    • Olson LJ, Dahms NM, Kim JJ. 2004. The N-terminal carbohydrate recognition site of the cation-independent mannose 6-phosphate receptor. J Biol Chem. 279:34000-34009.
    • (2004) J Biol Chem , vol.279 , pp. 34000-34009
    • Olson, L.J.1    Dahms, N.M.2    Kim, J.J.3
  • 88
    • 0033601324 scopus 로고    scopus 로고
    • Mutational analysis of the binding site residues of the bovine cation-dependent mannose 6-phosphate receptor
    • Olson LJ, Hancock MK, Dix D, Kim J-JP, Dahms NM. 1999. Mutational analysis of the binding site residues of the bovine cation-dependent mannose 6-phosphate receptor. J Biol Chem. 274:36905-36911.
    • (1999) J Biol Chem , vol.274 , pp. 36905-36911
    • Olson, L.J.1    Hancock, M.K.2    Dix, D.3    Kim, J.-J.P.4    Dahms, N.M.5
  • 89
    • 44349171796 scopus 로고    scopus 로고
    • Structural insights into the mechanism of pH-dependent ligand binding and release by the cation-dependent mannose 6-phosphate receptor
    • Olson LJ, Hindsgaul O, Dahms NM, Kim JJ. 2008. Structural insights into the mechanism of pH-dependent ligand binding and release by the cation-dependent mannose 6-phosphate receptor. J Biol Chem. 283:10124-10134.
    • (2008) J Biol Chem , vol.283 , pp. 10124-10134
    • Olson, L.J.1    Hindsgaul, O.2    Dahms, N.M.3    Kim, J.J.4
  • 90
    • 2942558373 scopus 로고    scopus 로고
    • Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa mannose 6-phosphate receptor
    • Olson LJ, Yammani RD, Dahms NM, Kim JJ. 2004. Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa mannose 6-phosphate receptor. EMBO J. 23:2019-2028.
    • (2004) EMBO J , vol.23 , pp. 2019-2028
    • Olson, L.J.1    Yammani, R.D.2    Dahms, N.M.3    Kim, J.J.4
  • 91
    • 0037155883 scopus 로고    scopus 로고
    • Twists and turns of the CD-MPR: Ligand-bound versus ligand-free receptor
    • Olson LJ, Zhang J, Dahms NM, Kim J-JP. 2002. Twists and turns of the CD-MPR: Ligand-bound versus ligand-free receptor. J Biol Chem. 277:10156-10161.
    • (2002) J Biol Chem , vol.277 , pp. 10156-10161
    • Olson, L.J.1    Zhang, J.2    Dahms, N.M.3    Kim, J.-J.P.4
  • 92
    • 0033569876 scopus 로고    scopus 로고
    • Structural basis for recognition of phosphorylated high mannose oligosaccharides by the cation-dependent mannose 6-phosphate receptor
    • Olson LJ, Zhang J, Lee YC, Dahms NM, Kim, J-JP. 1999. Structural basis for recognition of phosphorylated high mannose oligosaccharides by the cation-dependent mannose 6-phosphate receptor. J Biol Chem. 274:29889-29896.
    • (1999) J Biol Chem , vol.274 , pp. 29889-29896
    • Olson, L.J.1    Zhang, J.2    Lee, Y.C.3    Dahms, N.M.4    Kim, J.-J.P.5
  • 93
    • 0028834530 scopus 로고
    • The two mannose 6-phosphate receptors transport distinct complements of lysosomal proteins
    • Pohlmann R, Boeker MW, von Figura K. 1995. The two mannose 6-phosphate receptors transport distinct complements of lysosomal proteins. J Biol Chem. 270:27311-27318.
    • (1995) J Biol Chem , vol.270 , pp. 27311-27318
    • Pohlmann, R.1    Boeker, M.W.2    von Figura, K.3
  • 94
    • 0020490654 scopus 로고
    • Synthesis of phosphorylated recognition marker in lysosomal enzymes is located in the cis part of Golgi apparatus
    • Pohlmann R,Waheed A, Hasilik A, von Figura K. 1982. Synthesis of phosphorylated recognition marker in lysosomal enzymes is located in the cis part of Golgi apparatus. J Biol Chem. 257:5323-5325.
    • (1982) J Biol Chem , vol.257 , pp. 5323-5325
    • Pohlmann, R.1    Waheed, A.2    Hasilik, A.3    von Figura, K.4
  • 95
    • 0023710423 scopus 로고
    • Identification of mannose 6-phosphate in two asparagine-linked sugar chains of recombinant transforming growth factor-beta 1 precursor
    • Purchio AF, Cooper JA, Brunner AM, Lioubin MN, Gentry LE, Kovacina KS, Roth RA, Marquardt H. 1988. Identification of mannose 6-phosphate in two asparagine-linked sugar chains of recombinant transforming growth factor-beta 1 precursor. J Biol Chem. 263:14211-14215.
    • (1988) J Biol Chem , vol.263 , pp. 14211-14215
    • Purchio, A.F.1    Cooper, J.A.2    Brunner, A.M.3    Lioubin, M.N.4    Gentry, L.E.5    Kovacina, K.S.6    Roth, R.A.7    Marquardt, H.8
  • 96
    • 39049122146 scopus 로고    scopus 로고
    • Proteomics analysis of serum from mutant mice reveals lysosomal proteins selectively transported by each of the two mannose 6-phosphate receptors
    • Qian M, Sleat DE, Zheng H, Moore D, Lobel P. 2008. Proteomics analysis of serum from mutant mice reveals lysosomal proteins selectively transported by each of the two mannose 6-phosphate receptors. Mol Cell Proteomics. 7:58-70.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 58-70
    • Qian, M.1    Sleat, D.E.2    Zheng, H.3    Moore, D.4    Lobel, P.5
  • 97
    • 4644360229 scopus 로고    scopus 로고
    • Identification of a low affinity mannose 6-phosphate-binding site in domain 5 of the cation-independent mannose 6-phosphate receptor
    • Reddy ST, Chai W, Childs RA, Page JD, Feizi T, Dahms NM. 2004. Identification of a low affinity mannose 6-phosphate-binding site in domain 5 of the cation-independent mannose 6-phosphate receptor. J Biol Chem. 279:38658-38667.
    • (2004) J Biol Chem , vol.279 , pp. 38658-38667
    • Reddy, S.T.1    Chai, W.2    Childs, R.A.3    Page, J.D.4    Feizi, T.5    Dahms, N.M.6
  • 98
    • 0019863331 scopus 로고
    • Lysosomal enzyme targeting. N Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes
    • Reitman ML, Kornfeld S. 1981. Lysosomal enzyme targeting. N Acetylglucosaminylphosphotransferase selectively phosphorylates 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
  • 99
    • 0032524316 scopus 로고    scopus 로고
    • Molecular basis of lysosomal enzyme recognition: Three-dimensional structure of the cation-dependent mannose 6-phosphate receptor
    • Roberts DL, Weix DJ, Dahms NM, Kim J-JP 1998. Molecular basis of lysosomal enzyme recognition: Three-dimensional structure of the cation-dependent mannose 6-phosphate receptor. Cell. 93:639-648.
    • (1998) Cell , vol.93 , pp. 639-648
    • Roberts, D.L.1    Weix, D.J.2    Dahms, N.M.3    Kim, J.-J.P.4
  • 100
    • 0035166947 scopus 로고    scopus 로고
    • Lysosomal hydrolase mannose 6-phosphate uncovering enzyme resides in the trans-Golgi network
    • Rohrer J, Kornfeld R. 2001. Lysosomal hydrolase mannose 6-phosphate uncovering enzyme resides in the trans-Golgi network. Mol Biol Cell. 12:1623-1631.
    • (2001) Mol Biol Cell , vol.12 , pp. 1623-1631
    • Rohrer, J.1    Kornfeld, R.2
  • 101
    • 0028981715 scopus 로고
    • A determinant in the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor prevents trafficking to lysosomes
    • Rohrer J, Schweizer A, Johnson KF, Kornfeld S. 1995. A determinant in the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor prevents trafficking to lysosomes. J Cell Biol. 130:1297-1306.
    • (1995) J Cell Biol , vol.130 , pp. 1297-1306
    • Rohrer, J.1    Schweizer, A.2    Johnson, K.F.3    Kornfeld, S.4
  • 102
    • 0142216276 scopus 로고    scopus 로고
    • Deficiency of mannose 6-phosphate receptors and lysosomal storage: A morphometric analysis of hepatocytes of neonatal mice
    • Schellens JP, Saftig P, von Figura K, Everts V. 2003. Deficiency of mannose 6-phosphate receptors and lysosomal storage: A morphometric analysis of hepatocytes of neonatal mice. Cell Biol Int. 27:897-902.
    • (2003) Cell Biol Int , vol.27 , pp. 897-902
    • Schellens, J.P.1    Saftig, P.2    von Figura, K.3    Everts, V.4
  • 103
    • 0029076383 scopus 로고
    • Localization of the insulin-like growth factor II binding site to amino acids 1508-1566 in repeat 11 of the mannose 6-phosphate/insulin-like growth factor II receptor
    • Schmidt B, Kiecke-Siemsen C, Waheed A, Braulke T, von Figura K. 1995. Localization of the insulin-like growth factor II binding site to amino acids 1508-1566 in repeat 11 of the mannose 6-phosphate/insulin-like growth factor II receptor. J Biol Chem. 270:14975-14982.
    • (1995) J Biol Chem , vol.270 , pp. 14975-14982
    • Schmidt, B.1    Kiecke-Siemsen, C.2    Waheed, A.3    Braulke, T.4    von Figura, K.5
  • 104
    • 17844387148 scopus 로고    scopus 로고
    • Sleat DE, Lackland H, Wang Y, Sohar I, Xiao G, Li H, Lobel P. 2005. The human brain mannose 6-phosphate glycoproteome: A complex mixture composed of multiple isoforms of many soluble lysosomal proteins. Proteomics. 5:1520-1532 [erratum appears in Proteomics. 2005. 5(8):2272].
    • Sleat DE, Lackland H, Wang Y, Sohar I, Xiao G, Li H, Lobel P. 2005. The human brain mannose 6-phosphate glycoproteome: A complex mixture composed of multiple isoforms of many soluble lysosomal proteins. Proteomics. 5:1520-1532 [erratum appears in Proteomics. 2005. 5(8):2272].
  • 105
    • 0031021735 scopus 로고    scopus 로고
    • Ligand binding specificities of the two mannose 6-phosphate receptors
    • Sleat DE, Lobel P. 1997. Ligand binding specificities of the two mannose 6-phosphate receptors. J Biol Chem. 272:731-738.
    • (1997) J Biol Chem , vol.272 , pp. 731-738
    • Sleat, D.E.1    Lobel, P.2
  • 106
    • 33750619371 scopus 로고    scopus 로고
    • Identification and validation of mannose 6-phosphate glycoproteins in human plasma reveal awide range of lysosomal and non-lysosomal proteins
    • Sleat DE, Wang Y, Sohar I, Lackland H, Li Y, Li H, Zheng H, Lobel P. 2006. Identification and validation of mannose 6-phosphate glycoproteins in human plasma reveal awide range of lysosomal and non-lysosomal proteins. Mol Cell Proteomics. 5:1942-1956.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 1942-1956
    • Sleat, D.E.1    Wang, Y.2    Sohar, I.3    Lackland, H.4    Li, Y.5    Li, H.6    Zheng, H.7    Lobel, P.8
  • 107
    • 33847645773 scopus 로고    scopus 로고
    • The human urine mannose 6-phosphate glycoproteome
    • Sleat DE, Zheng H, Lobel P. 2007. The human urine mannose 6-phosphate glycoproteome. Biochim Biophys Acta. 1774:368-372.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 368-372
    • Sleat, D.E.1    Zheng, H.2    Lobel, P.3
  • 108
    • 0032030786 scopus 로고    scopus 로고
    • Mouse mutants lacking the cation-independent mannose 6- phosphate/insulin-like growth factor II receptor are impaired in lysosomal enzyme transport: Comparison of cation-independent and cation-dependent mannose 6-phosphate receptor-deficient mice
    • Sohar I, Sleat D, Gong Liu C, Ludwig T, Lobel P. 1998. Mouse mutants lacking the cation-independent mannose 6- phosphate/insulin-like growth factor II receptor are impaired in lysosomal enzyme transport: Comparison of cation-independent and cation-dependent mannose 6-phosphate receptor-deficient mice. Biochem J. 330:903-908.
    • (1998) Biochem J , vol.330 , pp. 903-908
    • Sohar, I.1    Sleat, D.2    Gong Liu, C.3    Ludwig, T.4    Lobel, P.5
  • 109
    • 25844478020 scopus 로고    scopus 로고
    • Identification of the minimal lysosomal enzyme recognition domain in cathepsin d
    • Steet R, Lee WS, Kornfeld S. 2005. Identification of the minimal lysosomal enzyme recognition domain in cathepsin d. J Biol Chem. 280:33318-33323.
    • (2005) J Biol Chem , vol.280 , pp. 33318-33323
    • Steet, R.1    Lee, W.S.2    Kornfeld, S.3
  • 110
    • 0023411438 scopus 로고
    • Mr 46,000 mannose 6-phosphate specific receptor: Its role in targeting of lysosomal enzymes
    • Stein M, Zijderhand-Bleekemolen JE, Geuze H, Hasilik A, von Figura K. 1987. Mr 46,000 mannose 6-phosphate specific receptor: Its role in targeting of lysosomal enzymes. EMBO J. 6:2677-2681.
    • (1987) EMBO J , vol.6 , pp. 2677-2681
    • Stein, M.1    Zijderhand-Bleekemolen, J.E.2    Geuze, H.3    Hasilik, A.4    von Figura, K.5
  • 111
    • 27944458451 scopus 로고    scopus 로고
    • Identification of residues essential for carbohydrate recognition and cation dependence of the 46-kDa mannose 6-phosphate receptor
    • Sun G, Zhao H, Kalyanaraman B, Dahms NM. 2005. Identification of residues essential for carbohydrate recognition and cation dependence of the 46-kDa mannose 6-phosphate receptor. Glycobiology. 15:1136-1149.
    • (2005) Glycobiology , vol.15 , pp. 1136-1149
    • Sun, G.1    Zhao, H.2    Kalyanaraman, B.3    Dahms, N.M.4
  • 112
    • 24944478240 scopus 로고    scopus 로고
    • Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD
    • Szathmary R, Bielmann R, Nita-Lazar M, Burda P, Jakob CA. 2005. Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell. 19:765-775.
    • (2005) Mol Cell , vol.19 , pp. 765-775
    • Szathmary, R.1    Bielmann, R.2    Nita-Lazar, M.3    Burda, P.4    Jakob, C.A.5
  • 113
    • 0019332713 scopus 로고
    • Biosynthetic intermediates of beta-glucuronidase contain high mannose oligosaccharides with blocked phosphate residues
    • Tabas I, Kornfeld S. 1980. Biosynthetic intermediates of beta-glucuronidase contain high mannose oligosaccharides with blocked phosphate residues. J Biol Chem. 255:6633-6639.
    • (1980) J Biol Chem , vol.255 , pp. 6633-6639
    • Tabas, I.1    Kornfeld, S.2
  • 115
    • 0024382077 scopus 로고
    • Ligand interactions of the cation-independent mannose 6-phosphate receptor. The stoichiometry of mannose 6-phosphate binding
    • Tong PY, Gregory W, Kornfeld S. 1989. Ligand interactions of the cation-independent mannose 6-phosphate receptor. The stoichiometry of mannose 6-phosphate binding. J Biol Chem. 264:7962-7969.
    • (1989) J Biol Chem , vol.264 , pp. 7962-7969
    • Tong, P.Y.1    Gregory, W.2    Kornfeld, S.3
  • 116
    • 0024333810 scopus 로고
    • Ligand interactions of the cation-dependent mannose 6-phosphate receptor. Comparison with the cation-independent mannose 6-phosphate receptor
    • Tong PY, Kornfeld S. 1989. Ligand interactions of the cation-dependent mannose 6-phosphate receptor. Comparison with the cation-independent mannose 6-phosphate receptor. J Biol Chem. 264:7970-7975.
    • (1989) J Biol Chem , vol.264 , pp. 7970-7975
    • Tong, P.Y.1    Kornfeld, S.2
  • 119
    • 0019333242 scopus 로고
    • Structural studies of phosphorylated high mannosetype oligosaccharides
    • Varki A, Kornfeld S. 1980. Structural studies of phosphorylated high mannosetype oligosaccharides. J Biol Chem. 255:10847-10858.
    • (1980) J Biol Chem , vol.255 , pp. 10847-10858
    • Varki, A.1    Kornfeld, S.2
  • 120
    • 0019877434 scopus 로고
    • Purification and characterization of rat liver alpha-N-acetylglucosaminyl phosphodiesterase
    • Varki A, Kornfeld S. 1981. Purification and characterization of rat liver alpha-N-acetylglucosaminyl phosphodiesterase. J Biol Chem 256:9937-9943.
    • (1981) J Biol Chem , vol.256 , pp. 9937-9943
    • Varki, A.1    Kornfeld, S.2
  • 121
    • 0020745118 scopus 로고
    • Demonstration of the enzymatic mechanisms of alpha-N-acetyl-D-glucosamine-1-phosphodiester N acetylglucosaminidase (formerly called alpha-N acetylglucosaminylphosphodiesterase) and lysosomal alpha-Nacetylglucosaminidase
    • Varki A, Sherman W, Kornfeld S. 1983. Demonstration of the enzymatic mechanisms of alpha-N-acetyl-D-glucosamine-1-phosphodiester N acetylglucosaminidase (formerly called alpha-N acetylglucosaminylphosphodiesterase) and lysosomal alpha-Nacetylglucosaminidase. Arch Biochem Biophys. 222:145-149.
    • (1983) Arch Biochem Biophys , vol.222 , pp. 145-149
    • Varki, A.1    Sherman, W.2    Kornfeld, S.3
  • 122
    • 14144255733 scopus 로고    scopus 로고
    • Lysosomal storage disorders
    • Vellodi A. 2004. Lysosomal storage disorders. Br J Haematol. 128:413-431.
    • (2004) Br J Haematol , vol.128 , pp. 413-431
    • Vellodi, A.1
  • 123
    • 0019876975 scopus 로고
    • Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterization and partial purification of a microsomal alpha-N acetylglucosaminyl phosphodiesterase
    • Waheed A, Hasilik A, von Figura K. 1981. Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterization and partial purification of a microsomal alpha-N acetylglucosaminyl phosphodiesterase. J Biol Chem. 256:5717-5721.
    • (1981) J Biol Chem , vol.256 , pp. 5717-5721
    • Waheed, A.1    Hasilik, A.2    von Figura, K.3
  • 124
    • 0020491261 scopus 로고
    • UDP-N-acetylglucosamine: Lysosomal enzyme precursor N-acetylglucosamine- 1-phosphotransferase. Partial purification and characterization of the rat liver Golgi enzyme
    • Waheed A, Hasilik A, von Figura K. 1982. UDP-N-acetylglucosamine: lysosomal enzyme precursor N-acetylglucosamine- 1-phosphotransferase. Partial purification and characterization of the rat liver Golgi enzyme. J Biol Chem. 257:12322-12331.
    • (1982) J Biol Chem , vol.257 , pp. 12322-12331
    • Waheed, A.1    Hasilik, A.2    von Figura, K.3
  • 125
  • 126
    • 0036830569 scopus 로고    scopus 로고
    • Role of N linked oligosaccharide flexibility in mannose phosphorylation of lysosomal enzyme cathepsin L
    • Warner JB, Thalhauser C, Tao K, Sahagian GG. 2002. Role of N linked oligosaccharide flexibility in mannose phosphorylation of lysosomal enzyme cathepsin L. J Biol Chem. 277:41897-41905.
    • (2002) J Biol Chem , vol.277 , pp. 41897-41905
    • Warner, J.B.1    Thalhauser, C.2    Tao, K.3    Sahagian, G.G.4
  • 127
    • 0025096054 scopus 로고
    • The overexpressed human 46-kDa mannose 6-phosphate receptor mediates endocytosis and sorting of beta-glucuronidase
    • Watanabe H, Grubb JH, Sly WS. 1990. The overexpressed human 46-kDa mannose 6-phosphate receptor mediates endocytosis and sorting of beta-glucuronidase. Proc Natl Acad Sci USA. 87:8036-8040.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8036-8040
    • Watanabe, H.1    Grubb, J.H.2    Sly, W.S.3
  • 128
    • 0025734570 scopus 로고
    • Mutational analysis of disulfide bridges in the Mr 46,000 mannose 6-phosphate receptor. Localization and role for ligand binding
    • Wendland M, von Figura K, Pohlmann R. 1991. Mutational analysis of disulfide bridges in the Mr 46,000 mannose 6-phosphate receptor. Localization and role for ligand binding. J Biol Chem. 266:7132-7136.
    • (1991) J Biol Chem , vol.266 , pp. 7132-7136
    • Wendland, M.1    von Figura, K.2    Pohlmann, R.3
  • 129
    • 0025922158 scopus 로고
    • Mr 46,000 mannose 6-phosphate receptor. The role of histidine and arginine residues for binding of ligand
    • Wendland M,Waheed A, von Figura K, Pohlmann R. 1991. Mr 46,000 mannose 6-phosphate receptor. The role of histidine and arginine residues for binding of ligand. J Biol Chem. 266:2917-2923.
    • (1991) J Biol Chem , vol.266 , pp. 2917-2923
    • Wendland, M.1    Waheed, A.2    von Figura, K.3    Pohlmann, R.4
  • 130
    • 0026352780 scopus 로고
    • The bovine mannose 6-phosphate/ insulin-like growth factor II receptor. Localization of mannose 6-phosphate binding sites to domains 1-3 and 7-11 of the extracytoplasmic region
    • Westlund B, Dahms NM, Kornfeld S. 1991. The bovine mannose 6-phosphate/ insulin-like growth factor II receptor. Localization of mannose 6-phosphate binding sites to domains 1-3 and 7-11 of the extracytoplasmic region. J Biol Chem. 266:23233-23239.
    • (1991) J Biol Chem , vol.266 , pp. 23233-23239
    • Westlund, B.1    Dahms, N.M.2    Kornfeld, S.3
  • 131
    • 0035838461 scopus 로고    scopus 로고
    • A yeast homolog of the mammalian mannose 6-phosphate receptors contributes to the sorting of vacuolar hydrolases
    • Whyte JR, Munro S. 2001. A yeast homolog of the mammalian mannose 6-phosphate receptors contributes to the sorting of vacuolar hydrolases. Curr Biol. 11:1074-1078.
    • (2001) Curr Biol , vol.11 , pp. 1074-1078
    • Whyte, J.R.1    Munro, S.2
  • 132
    • 42949156428 scopus 로고    scopus 로고
    • Cell surface-expressed cation-independent mannose 6-phosphate receptor (CD222) binds enzymatically active heparanase independently of mannose 6-phosphate to promote extracellular matrix degradation
    • Wood RJ, Hulett MD. 2008. Cell surface-expressed cation-independent mannose 6-phosphate receptor (CD222) binds enzymatically active heparanase independently of mannose 6-phosphate to promote extracellular matrix degradation. J Biol Chem. 283:4165-4176.
    • (2008) J Biol Chem , vol.283 , pp. 4165-4176
    • Wood, R.J.1    Hulett, M.D.2


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