메뉴 건너뛰기




Volumn 208, Issue 2, 2015, Pages 171-180

Mannose 6 phosphorylation of lysosomal enzymes controls B cell functions

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; CATHEPSIN B; CATHEPSIN L; CD27 ANTIGEN; CD74 ANTIGEN; GAMMA INTERFERON; GRANZYME A; GRANZYME B; IMMUNOGLOBULIN; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; LYSOSOME ENZYME; MANNOSE 6 PHOSPHATE; SYNDECAN 1; TUMOR NECROSIS FACTOR; GNPTAB PROTEIN, MOUSE; MANNOSE PHOSPHATE; MANNOSE-6-PHOSPHATE; PEPTIDE HYDROLASE; PHOSPHOTRANSFERASE;

EID: 84921737623     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201407077     Document Type: Article
Times cited : (22)

References (46)
  • 1
    • 0029906622 scopus 로고    scopus 로고
    • Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. II. Enzymatic characterization and identification of the catalytic subunit
    • Bao, M., B.J. Elmendorf, J.L. Booth, R.R. Drake, and W.M. Canfield. 1996. Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. II. Enzymatic characterization and identification of the catalytic subunit. J. Biol. Chem. 271: 31446-31451. http://dx.doi.org/10.1074/jbc.271.49.31446
    • (1996) J. Biol. Chem , vol.271 , pp. 31446-31451
    • Bao, M.1    Elmendorf, B.J.2    Booth, J.L.3    Drake, R.R.4    Canfield, W.M.5
  • 2
    • 0031897801 scopus 로고    scopus 로고
    • Defective TCR expression in transgenic mice constructed using cDNA-based α- and β-chain genes under the control of heterologous regulatory elements
    • Barnden, M.J., J. Allison, W.R. Heath, and F.R. Carbone. 1998. Defective TCR expression in transgenic mice constructed using cDNA-based α- and β-chain genes under the control of heterologous regulatory elements. Immunol. Cell Biol. 76: 34-40. http://dx.doi.org/10.1046/j.1440-1711.1998.00709.x
    • (1998) Immunol. Cell Biol , vol.76 , pp. 34-40
    • Barnden, M.J.1    Allison, J.2    Heath, W.R.3    Carbone, F.R.4
  • 3
    • 63149193317 scopus 로고    scopus 로고
    • Sorting of lysosomal proteins
    • Braulke, T., and J.S. Bonifacino. 2009. Sorting of lysosomal proteins. Biochim. Biophys. Acta 1793: 605-614. http://dx.doi.org/10.1016/j.bbamcr.2008.10.016
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 605-614
    • Braulke, T.1    Bonifacino, J.S.2
  • 4
    • 84896904825 scopus 로고    scopus 로고
    • I-Cell Disease and Pseudo-Hurler Polydystrophy: Disorders of Lysosomal Enzyme Phosphorylation and Localization
    • D. Valle, A.L. Beaudet, B. Vogelstein, K.W. Kinzler, S.E. Antonarakis, A. Ballabio, C. Scriver, B. Childs, W. Sly, F. Bunz, K.M. Gibson, G. Mitchell, editors. McGraw Hill, New York. Chapter 138
    • Braulke, T., A. Raas-Rothschild, and S. Kornfeld. 2013. I-Cell Disease and Pseudo-Hurler Polydystrophy: Disorders of Lysosomal Enzyme Phosphorylation and Localization. In The Online Metabolic and Molecular Bases of Inherited Disease. D. Valle, A.L. Beaudet, B. Vogelstein, K.W. Kinzler, S.E. Antonarakis, A. Ballabio, C. Scriver, B. Childs, W. Sly, F. Bunz, K.M. Gibson, G. Mitchell, editors. McGraw Hill, New York. Chapter 138.
    • (2013) The Online Metabolic and Molecular Bases of Inherited Disease
    • Braulke, T.1    Raas-Rothschild, A.2    Kornfeld, S.3
  • 6
    • 0034094433 scopus 로고    scopus 로고
    • Abnormal immune function in vivo in a murine model of lysosomal storage disease
    • Daly, T.M., R.G. Lorenz, and M.S. Sands. 2000. Abnormal immune function in vivo in a murine model of lysosomal storage disease. Pediatr. Res. 47: 757-762. http://dx.doi.org/10.1203/00006450-200006000-00012
    • (2000) Pediatr. Res , vol.47 , pp. 757-762
    • Daly, T.M.1    Lorenz, R.G.2    Sands, M.S.3
  • 7
    • 14844340568 scopus 로고    scopus 로고
    • Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
    • Delamarre, L., M. Pack, H. Chang, I. Mellman, and E.S. Trombetta. 2005. Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate. Science307: 1630-1634. http://dx.doi.org/10.1126/science.1108003
    • (2005) Science , vol.307 , pp. 1630-1634
    • Delamarre, L.1    Pack, M.2    Chang, H.3    Mellman, I.4    Trombetta, E.S.5
  • 8
    • 33748475526 scopus 로고    scopus 로고
    • Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis
    • Delamarre, L., R. Couture, I. Mellman, and E.S. Trombetta. 2006. Enhancing immunogenicity by limiting susceptibility to lysosomal proteolysis. J. Exp. Med. 203: 2049-2055. http://dx.doi.org/10.1084/jem.20052442
    • (2006) J. Exp. Med , vol.203 , pp. 2049-2055
    • Delamarre, L.1    Couture, R.2    Mellman, I.3    Trombetta, E.S.4
  • 10
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson, J.G., D. Finazzi, and R.D. Klausner. 1992. Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature360: 350-352. http://dx.doi.org/10.1038/360350a0
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 12
    • 39649084660 scopus 로고    scopus 로고
    • Plasma cell development: from B-cell subsets to long-term survival niches
    • Fairfax, K.A., A. Kallies, S.L. Nutt, and D.M. Tarlinton. 2008. Plasma cell development: from B-cell subsets to long-term survival niches. Semin. Immunol. 20: 49-58. http://dx.doi.org/10.1016/j.smim.2007.12.002
    • (2008) Semin. Immunol , vol.20 , pp. 49-58
    • Fairfax, K.A.1    Kallies, A.2    Nutt, S.L.3    Tarlinton, D.M.4
  • 13
    • 0014567351 scopus 로고
    • The defect in Hurler and Hunter syndromes. II. Deficiency of specific factors involved in mucopolysaccharide degradation
    • Fratantoni, J.C., C.W. Hall, and E.F. Neufeld. 1969. The defect in Hurler and Hunter syndromes. II. Deficiency of specific factors involved in mucopolysaccharide degradation. Proc. Natl. Acad. Sci. USA64: 360-366. http://dx.doi.org/10.1073/pnas.64.1.360
    • (1969) Proc. Natl. Acad. Sci. USA , vol.64 , pp. 360-366
    • Fratantoni, J.C.1    Hall, C.W.2    Neufeld, E.F.3
  • 14
    • 84890280164 scopus 로고    scopus 로고
    • Internalizing MHC class II-peptide complexes are ubiquitinated in early endosomes and targeted for lysosomal degradation
    • Furuta, K., E. Walseng, and P.A. Roche. 2013. Internalizing MHC class II-peptide complexes are ubiquitinated in early endosomes and targeted for lysosomal degradation. Proc. Natl. Acad. Sci. USA110: 20188-20193. http://dx.doi.org/10.1073/pnas.1312994110
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 20188-20193
    • Furuta, K.1    Walseng, E.2    Roche, P.A.3
  • 15
    • 0027443394 scopus 로고
    • Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts
    • Glickman, J.N., and S. Kornfeld. 1993. Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts. J. Cell Biol. 123: 99-108. http://dx.doi.org/10.1083/jcb.123.1.99
    • (1993) J. Cell Biol , vol.123 , pp. 99-108
    • Glickman, J.N.1    Kornfeld, S.2
  • 16
    • 0027452741 scopus 로고
    • Granzymes A and B are targeted to the lytic granules of lymphocytes by the mannose-6-phosphate receptor
    • Griffiths, G.M., and S. Isaaz. 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. http://dx.doi.org/10.1083/jcb.120.4.885
    • (1993) J. Cell Biol , vol.120 , pp. 885-896
    • Griffiths, G.M.1    Isaaz, S.2
  • 17
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey, K., and A.Y. Rudensky. 2003. Lysosomal cysteine proteases regulate antigen presentation. Nat. Rev. Immunol. 3: 472-482. http://dx.doi.org/10.1038/nri1110
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 20
    • 0018755046 scopus 로고
    • A case of mucolipidosis II: Biochemical, nutritional, and immunological studies
    • Kojima, S., S. Okada, H. Kai, K. Ha, O. Nose, T. Ikeda, T. Yutaka, M. Kato, and H. Yabuuchi. 1979. A case of mucolipidosis II: Biochemical, nutritional, and immunological studies. Brain Dev. 1: 26-30. http://dx.doi.org/10.1016/S0387-7604(79)80031-5
    • (1979) Brain Dev , vol.1 , pp. 26-30
    • Kojima, S.1    Okada, S.2    Kai, H.3    Ha, K.4    Nose, O.5    Ikeda, T.6    Yutaka, T.7    Kato, M.8    Yabuuchi, H.9
  • 23
    • 27744606539 scopus 로고    scopus 로고
    • The α- and β-subunits of the human UDP-N-acetylglucosamine: lysosomal enzyme N-acetylglucosamine-1-phosphotransferase [corrected] are encoded by a single cDNA
    • Kudo, M., M. Bao, A. D'Souza, F. Ying, H. Pan, B.A. Roe, and W.M. Canfield. 2005. The α- and β-subunits of the human UDP-N-acetylglucosamine: lysosomal enzyme N-acetylglucosamine-1-phosphotransferase [corrected] are encoded by a single cDNA. J. Biol. Chem. 280: 36141-36149. http://dx.doi.org/10.1074/jbc.M509008200
    • (2005) J. Biol. Chem , vol.280 , pp. 36141-36149
    • Kudo, M.1    Bao, M.2    D'Souza, A.3    Ying, F.4    Pan, H.5    Roe, B.A.6    Canfield, W.M.7
  • 25
    • 84861914965 scopus 로고    scopus 로고
    • MHC class II distribution in dendritic cells and B cells is determined by ubiquitin chain length
    • Ma, J.K., M.Y. Platt, J. Eastham-Anderson, J.S. Shin, and I. Mellman. 2012. MHC class II distribution in dendritic cells and B cells is determined by ubiquitin chain length. Proc. Natl. Acad. Sci. USA109: 8820-8827. http://dx.doi.org/10.1073/pnas.1202977109
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 8820-8827
    • Ma, J.K.1    Platt, M.Y.2    Eastham-Anderson, J.3    Shin, J.S.4    Mellman, I.5
  • 26
    • 0033840811 scopus 로고    scopus 로고
    • Immunodeficiency in α-mannosidosis: a matched case-control study on immunoglobulins, complement factors, receptor density, phagocytosis and intracellular killing in leucocytes
    • Malm, D., D.S. Halvorsen, L. Tranebjaerg, and H. Sjursen. 2000. Immunodeficiency in α-mannosidosis: a matched case-control study on immunoglobulins, complement factors, receptor density, phagocytosis and intracellular killing in leucocytes. Eur. J. Pediatr. 159: 699-703. http://dx.doi.org/10.1007/s004310000545
    • (2000) Eur. J. Pediatr , vol.159 , pp. 699-703
    • Malm, D.1    Halvorsen, D.S.2    Tranebjaerg, L.3    Sjursen, H.4
  • 28
    • 78649314286 scopus 로고    scopus 로고
    • Reference values for B cell subpopulations from infancy to adulthood
    • Morbach, H., E.M. Eichhorn, J.G. Liese, and H.J. Girschick. 2010. Reference values for B cell subpopulations from infancy to adulthood. Clin. Exp. Immunol. 162: 271-279. http://dx.doi.org/10.1111/j.1365-2249.2010.04206.x
    • (2010) Clin. Exp. Immunol , vol.162 , pp. 271-279
    • Morbach, H.1    Eichhorn, E.M.2    Liese, J.G.3    Girschick, H.J.4
  • 32
    • 0020370152 scopus 로고
    • Is there a mechanism for introducing acid hydrolases into liver lysosomes that is independent of mannose 6-phosphate recognition? Evidence from I-cell disease
    • Owada, M., and E.F. Neufeld. 1982. Is there a mechanism for introducing acid hydrolases into liver lysosomes that is independent of mannose 6-phosphate recognition? Evidence from I-cell disease. Biochem. Biophys. Res. Commun. 105: 814-820. http://dx.doi.org/10.1016/0006-291X(82)91042-7
    • (1982) Biochem. Biophys. Res. Commun , vol.105 , pp. 814-820
    • Owada, M.1    Neufeld, E.F.2
  • 35
    • 0019420191 scopus 로고
    • Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5'-diphosphate-N-acetylglucosamine: glycoprotein N-acetylglucosaminylphosphotransferase activity
    • Reitman, M.L., A. Varki, and S. Kornfeld. 1981. Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5'-diphosphate-N-acetylglucosamine: glycoprotein N-acetylglucosaminylphosphotransferase activity. J. Clin. Invest. 67: 1574-1579. http://dx.doi.org/10.1172/JCI110189
    • (1981) J. Clin. Invest , vol.67 , pp. 1574-1579
    • Reitman, M.L.1    Varki, A.2    Kornfeld, S.3
  • 37
    • 0026353496 scopus 로고
    • Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules
    • Roche, P.A., and P. Cresswell. 1991. Proteolysis of the class II-associated invariant chain generates a peptide binding site in intracellular HLA-DR molecules. Proc. Natl. Acad. Sci. USA88: 3150-3154. http://dx.doi.org/10.1073/pnas.88.8.3150
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3150-3154
    • Roche, P.A.1    Cresswell, P.2
  • 38
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function
    • Saftig, P., and J. Klumperman. 2009. Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat. Rev. Mol. Cell Biol. 10: 623-635. http://dx.doi.org/10.1038/nrm2745
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 39
    • 33745293617 scopus 로고    scopus 로고
    • Therapeutic strategies to ameliorate lysosomal storage disorders-a focus on Gaucher disease
    • Sawkar, A.R., W. D'Haeze, and J.W. Kelly. 2006. Therapeutic strategies to ameliorate lysosomal storage disorders-a focus on Gaucher disease. Cell. Mol. Life Sci. 63: 1179-1192. http://dx.doi.org/10.1007/s00018-005-5437-0
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 1179-1192
    • Sawkar, A.R.1    D'Haeze, W.2    Kelly, J.W.3
  • 40
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger, H. 2006. Tricine-SDS-PAGE. Nat. Protoc. 1: 16-22. http://dx.doi.org/10.1038/nprot.2006.4
    • (2006) Nat. Protoc , vol.1 , pp. 16-22
    • Schägger, H.1
  • 42
    • 0013913044 scopus 로고
    • Serum levels of immune globulins in health and disease: a survey
    • Tiede, S., S. Storch, T. Lübke, B. Henrissat, R. Bargal, A. Raas-Rothschild, and
    • Stiehm, E.R., and H.H. Fudenberg. 1966. Serum levels of immune globulins in health and disease: a survey. Pediatrics37: 715-727. Tiede, S., S. Storch, T. Lübke, B. Henrissat, R. Bargal, A. Raas-Rothschild, and
    • (1966) Pediatrics , vol.37 , pp. 715-727
    • Stiehm, E.R.1    Fudenberg, H.H.2
  • 43
    • 27144550841 scopus 로고    scopus 로고
    • Mucolipidosis II is caused by mutations in GNPTA encoding the α/β GlcNAc-1-phosphotransferase
    • T. Braulke. 2005. Mucolipidosis II is caused by mutations in GNPTA encoding the α/β GlcNAc-1-phosphotransferase. Nat. Med. 11: 1109-1112. http://dx.doi.org/10.1038/nm1305
    • (2005) Nat. Med , vol.11 , pp. 1109-1112
    • Braulke, T.1
  • 44
    • 0023733908 scopus 로고
    • I-cell disease: evidence for a mannose 6-phosphate independent pathway for translocation of lysosomal enzymes in lymphoblastoid cells
    • Tsuji, A., K. Omura, and Y. Suzuki. 1988. I-cell disease: evidence for a mannose 6-phosphate independent pathway for translocation of lysosomal enzymes in lymphoblastoid cells. Clin. Chim. Acta176: 115-121. http://dx.doi.org/10.1016/0009-8981(88)90181-7
    • (1988) Clin. Chim. Acta , vol.176 , pp. 115-121
    • Tsuji, A.1    Omura, K.2    Suzuki, Y.3
  • 45
    • 0019876859 scopus 로고
    • Subcellular location of two enzymes involved in the synthesis of phosphorylated recognition markers in lysosomal enzymes
    • Waheed, A., R. Pohlmann, A. Hasilik, and K. von Figura. 1981. Subcellular location of two enzymes involved in the synthesis of phosphorylated recognition markers in lysosomal enzymes. J. Biol. Chem. 256:4150-4152.
    • (1981) J. Biol. Chem , vol.256 , pp. 4150-4152
    • Waheed, A.1    Pohlmann, R.2    Hasilik, A.3    von Figura, K.4
  • 46
    • 0020411893 scopus 로고
    • Deficiency of UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase in organs of I-cell patients
    • Waheed, A., R. Pohlmann, A. Hasilik, K. von Figura, A. van Elsen, and J.G. Leroy. 1982. Deficiency of UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase in organs of I-cell patients. Biochem. Biophys. Res. Commun. 105: 1052-1058. http://dx.doi.org/10.1016/0006-291X(82)91076-2
    • (1982) Biochem. Biophys. Res. Commun , vol.105 , pp. 1052-1058
    • Waheed, A.1    Pohlmann, R.2    Hasilik, A.3    von Figura, K.4    van Elsen, A.5    Leroy, J.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.