메뉴 건너뛰기




Volumn , Issue , 2008, Pages 402-413

The transport of soluble lysosomal hydrolases from the Golgi complex to lysosomes

Author keywords

[No Author keywords available]

Indexed keywords


EID: 78149349007     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-211-76310-0_25     Document Type: Chapter
Times cited : (3)

References (71)
  • 2
    • 0029958044 scopus 로고    scopus 로고
    • Bovine UDP-N-acetylglucosamine: Lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. I. Purification and subunit structure
    • Bao M, Booth JL, Elmendorf BJ, Canfield WM (1996) Bovine UDP-N-acetylglucosamine: lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. I. Purification and subunit structure. J Biol Chem 271:31437-31445
    • (1996) J Biol Chem , vol.271 , pp. 31437-31445
    • Bao, M.1    Booth, J.L.2    Elmendorf, B.J.3    Canfield, W.M.4
  • 3
    • 0025043421 scopus 로고
    • Generation of a lysosomal enzyme targeting signal in the secretory protein pepsinogen
    • Baranski TJ, Faust PL, Kornfeld S (1990) Generation of a lysosomal enzyme targeting signal in the secretory protein pepsinogen. Cell 63:281-291
    • (1990) Cell , vol.63 , pp. 281-291
    • Baranski, T.J.1    Faust, P.L.2    Kornfeld, S.3
  • 4
    • 0026333687 scopus 로고
    • Mapping and molecular modeling of a recognition domain for lysosomal enzyme targeting
    • Baranski TJ, Koelsch G, Hartsuck JA, Kornfeld S (1991) Mapping and molecular modeling of a recognition domain for lysosomal enzyme targeting. J Biol Chem 266:23365-23372
    • (1991) J Biol Chem , vol.266 , pp. 23365-23372
    • Baranski, T.J.1    Koelsch, G.2    Hartsuck, J.A.3    Kornfeld, S.4
  • 5
    • 0023250992 scopus 로고
    • Is movement of mannose 6-phosphate-specific receptor triggered by binding of lysosomal enzymes?
    • Braulke T, Gartung C, Hasilik A, Von Figura K (1987) Is movement of mannose 6-phosphate-specific receptor triggered by binding of lysosomal enzymes? J Cell Biol 104:1735-1742
    • (1987) J Cell Biol , vol.104 , pp. 1735-1742
    • Braulke, T.1    Gartung, C.2    Hasilik, A.3    Von Figura, K.4
  • 6
    • 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
  • 7
    • 22144468424 scopus 로고    scopus 로고
    • Niemann-Pick type C disease: Subcellular location and functional characterization of NPC2proteins with naturally occurring missense mutations
    • Chikh K, Rodriguez C, Vey S, Vanier MT, Millat G (2005) Niemann-Pick type C disease: subcellular location and functional characterization of NPC2proteins with naturally occurring missense mutations. Hum Mutat 26:20-28
    • (2005) Hum Mutat , vol.26 , pp. 20-28
    • Chikh, K.1    Rodriguez, C.2    Vey, S.3    Vanier, M.T.4    Millat, G.5
  • 8
    • 0029012951 scopus 로고
    • Lysine-based structure in the proregion of procathepsin L is the recognition site for mannose phosphorylation
    • Cuozzo JW, Tao K, Wu QL, Young W, Sahagian GG (1995) Lysine-based structure in the proregion of procathepsin L is the recognition site for mannose phosphorylation. J Biol Chem 270:15611-15619
    • (1995) J Biol Chem , vol.270 , pp. 15611-15619
    • Cuozzo, J.W.1    Tao, K.2    Wu, Q.L.3    Young, W.4    Sahagian, G.G.5
  • 9
    • 31644441420 scopus 로고    scopus 로고
    • Proteomic analysis of lisosoma acid hydrolases secreted by osteoclasts: Implications for lytic enzyme transport and bone metabolism
    • Czupalla C, Manusukoski H, Riedl T, Krause E, Hoflack B (2006) Proteomic analysis of lisosoma 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    Manusukoski, H.2    Riedl, T.3    Krause, E.4    Hoflack, B.5
  • 10
    • 0031724560 scopus 로고    scopus 로고
    • Aninsulin-like growth factor II (IGF-II) affinity-enhancing domainlocalized within extracytoplasmic repeat 13 of the IGF-II/mannose 6-phosphate receptor
    • Devi GR, Byrd JC, Slentz DH, MacDonald RG (1998) Aninsulin-like growth factor II (IGF-II) affinity-enhancing domainlocalized 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
  • 11
    • 0023943263 scopus 로고
    • Cathepsin D is membrane-associated in macrophage endosomes
    • Diment S, Leech MS, Stahl PD (1988) Cathepsin D is membrane-associated in macrophage endosomes. J Biol Chem 263:6901-6907
    • (1988) J Biol Chem , vol.263 , pp. 6901-6907
    • Diment, S.1    Leech, M.S.2    Stahl, P.D.3
  • 12
    • 0033564886 scopus 로고    scopus 로고
    • Phosphorylation of arylsulphatase A occurs through multiple interactions with the UDP-N-acetylglucosamine-1-phosphotransferase proximal and distal to its retrieval site by the KDEL receptor
    • Dittmer F, Von Figura K (1999) Phosphorylation of arylsulphatase A occurs through multiple interactions with the UDP-N-acetylglucosamine-1-phosphotransferase proximal and distal to its retrieval site by the KDEL receptor. Biochem J 340:729-736
    • (1999) Biochem J , vol.340 , pp. 729-736
    • Dittmer, F.1    Von Figura, K.2
  • 13
    • 0031022888 scopus 로고    scopus 로고
    • The phosphorylation pattern of oligosaccharides in secreted procathepsin D is glycosylation site-specific and independent of the expression of mannose 6-phosphate receptors
    • Dittmer F, Pohlmann R, Von Figura K (1997) The phosphorylation pattern of oligosaccharides in secreted procathepsin D is glycosylation site-specific and independent of the expression of mannose 6-phosphate receptors. J Biol Chem 272:852-858
    • (1997) J Biol Chem , vol.272 , pp. 852-858
    • Dittmer, F.1    Pohlmann, R.2    Von Figura, K.3
  • 14
    • 0031736533 scopus 로고    scopus 로고
    • Abnormal lysosomal sorting with an enhanced secretion of cathepsinDprecursor molecules bearingmonoester phosphate groups
    • Faulhaber J, Fensom A, Hasilik A (1998) Abnormal lysosomal sorting with an enhanced secretion of cathepsinDprecursor molecules bearingmonoester phosphate groups. Eur J Cell Biol 77:134-140
    • (1998) Eur J Cell Biol , vol.77 , pp. 134-140
    • Faulhaber, J.1    Fensom, A.2    Hasilik, A.3
  • 15
    • 38449099687 scopus 로고    scopus 로고
    • Mice lacking alpha/beta subunits of GlcNAc-1-phosphotransferase exhibit growth retardation, retinal degeneration, and secretory cell lesions
    • Gelfman CM, Vogel P, Issa TM, Turner CA, Lee WS, Kornfeld S, Rice DS (2007) Mice lacking alpha/beta subunits of GlcNAc-1-phosphotransferase exhibit growth retardation, retinal degeneration, and secretory cell lesions. Invest Ophthalmol Vis Sci 48:5221-5228
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 5221-5228
    • Gelfman, C.M.1    Vogel, P.2    Issa, T.M.3    Turner, C.A.4    Lee, W.S.5    Kornfeld, S.6    Rice, D.S.7
  • 16
    • 0027443394 scopus 로고
    • Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts
    • Glickman JN, Kornfeld S (1993) Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts. J Cell Biol 123:99-108
    • (1993) J Cell Biol , vol.123 , pp. 99-108
    • Glickman, J.N.1    Kornfeld, S.2
  • 17
    • 0018821796 scopus 로고
    • Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues
    • Hasilik A, Neufeld EF (1980) Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues. J Biol Chem 255:4946-4950
    • (1980) J Biol Chem , vol.255 , pp. 4946-4950
    • Hasilik, A.1    Neufeld, E.F.2
  • 18
    • 0031920344 scopus 로고    scopus 로고
    • The kinetics of mannose 6-phosphate receptor trafficking in the endocytic pathway in HEp-2 cells: The receptor enters and rapidly leaves multivesicular endosomes without accumulating in a prelysosomal compartment
    • Hirst J, Futter CE, Hopkins CR (1998) The kinetics of mannose 6-phosphate receptor trafficking in the endocytic pathway in HEp-2 cells: the receptor enters and rapidly leaves multivesicular endosomes without accumulating in a prelysosomal compartment. Mol Biol Cell 9:809-816
    • (1998) Mol Biol Cell , vol.9 , pp. 809-816
    • Hirst, J.1    Futter, C.E.2    Hopkins, C.R.3
  • 19
    • 0025179956 scopus 로고
    • Suppression of the 'uncovering' of mannose-6-phosphate residues in lysosomal enzymes in the presence of NH4Cl
    • Isidoro C, Radons J, Baccino FM, Hasilik A (1990) Suppression of the 'uncovering' of mannose-6-phosphate residues in lysosomal enzymes in the presence of NH4Cl. Eur J Biochem 191:591-597
    • (1990) Eur J Biochem , vol.191 , pp. 591-597
    • Isidoro, C.1    Radons, J.2    Baccino, F.M.3    Hasilik, A.4
  • 20
    • 0029908325 scopus 로고    scopus 로고
    • Exposed thiols confer localization in the endoplasmic reticulum by retention rather than retrieval
    • Isidoro C, Maggioni C, Demoz M, Pizzagalli A, Fra AM, Sitia R (1996) Exposed thiols confer localization in the endoplasmic reticulum by retention rather than retrieval. J Biol Chem 271:26138-26142
    • (1996) J Biol Chem , vol.271 , pp. 26138-26142
    • Isidoro, C.1    Maggioni, C.2    Demoz, M.3    Pizzagalli, A.4    Fra, A.M.5    Sitia, R.6
  • 21
    • 0031967964 scopus 로고    scopus 로고
    • Human and hamster procathepsin D, although equally tagged with mannose-6-phosphate, are differentially targeted to lysosomes in transfected BHK cells
    • Isidoro C, Baccino FM, Hasilik A (1998) Human and hamster procathepsin D, although equally tagged with mannose-6-phosphate, are differentially targeted to lysosomes in transfected BHK cells. Cell Tissue Res 292:303-310
    • (1998) Cell Tissue Res , vol.292 , pp. 303-310
    • Isidoro, C.1    Baccino, F.M.2    Hasilik, A.3
  • 22
    • 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
  • 23
    • 0031456570 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor-II is a receptor for retinoic acid
    • Kang JX, Li Y, Leaf A (1997) Mannose 6-phosphate/insulin-like growth factor-II is a receptor for retinoic acid. Proc Natl Acad Sci USA 95:13671-13676
    • (1997) Proc Natl Acad Sci USA , vol.95 , pp. 13671-13676
    • Kang, J.X.1    Li, Y.2    Leaf, A.3
  • 24
    • 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
  • 27
    • 0023753261 scopus 로고
    • Biosynthesis of the mannose 6-phosphate recognition marker in transport-impaired mouse lymphoma cells
    • Lazzarino DA, Gabel CA (1988) Biosynthesis of the mannose 6-phosphate recognition marker in transport-impaired mouse lymphoma cells. J Biol Chem 263:10118-10126
    • (1988) J Biol Chem , vol.263 , pp. 10118-10126
    • Lazzarino, D.A.1    Gabel, C.A.2
  • 28
    • 0024561806 scopus 로고
    • Mannose processing is an important determinant in the assembly of prosphorylated high mannose-type oligosaccharides
    • Lazzarino DA, Gabel CA (1989) Mannose processing is an important determinant in the assembly of prosphorylated high mannose-type oligosaccharides. J Biol Chem 264:5051-5023
    • (1989) J Biol Chem , vol.264 , pp. 5051-5023
    • Lazzarino, D.A.1    Gabel, C.A.2
  • 29
    • 0345732689 scopus 로고    scopus 로고
    • Thelysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin
    • Lefrancois S, Zeng J, Hassan AJ, Canuel M, Morales CR (2003) Thelysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin. EMBOJ 22:6430-6437
    • (2003) EMBOJ , vol.22 , pp. 6430-6437
    • Lefrancois, S.1    Zeng, J.2    Hassan, A.J.3    Canuel, M.4    Morales, C.R.5
  • 31
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz J, Yuan LC, Bonifacino JS, Klausner RD (1989) Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56:801-813
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 32
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz J, Donaldson JG, Schweizer A, Berger EG, Hauri HP, Yuan LC, Klausner RD (1990) Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell 60:821-836
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.P.5    Yuan, L.C.6    Klausner, R.D.7
  • 33
    • 0023840372 scopus 로고
    • Cloning and sequence analysis of the cationindependent mannose 6-phosphate receptor
    • Lobel P, Dahms NM, Kornfeld S (1988) Cloning and sequence analysis of the cationindependent mannose 6-phosphate receptor. J Biol Chem 263:2563-2570
    • (1988) J Biol Chem , vol.263 , pp. 2563-2570
    • Lobel, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 34
    • 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
  • 36
    • 0025743395 scopus 로고
    • Procathepsins L and D are membrane-bound in acidic microsomal vesicles
    • McIntyre GF, Erickson AH (1991) Procathepsins L and D are membrane-bound in acidic microsomal vesicles. J Biol Chem 266:15438-15445
    • (1991) J Biol Chem , vol.266 , pp. 15438-15445
    • McIntyre, G.F.1    Erickson, A.H.2
  • 37
    • 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
  • 39
    • 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 JJ, 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.4    Dahms, N.M.5
  • 40
    • 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
  • 41
    • 44349171796 scopus 로고    scopus 로고
    • Structural insight into the mechanism of pH-dependent ligand binding and release by the cation-dependent mannose 6-phosphate receptor
    • Olson LJ, Hindgaul O, Dahms NM, Kim JJP (2008) Structural insight into the mechanism of pH-dependent ligand binding and release by the cation-dependent mannose 6-phosphate receptor. JBC http://www.jbc.org/cgi/doi/10.1074/jbc. M708994200
    • (2008) JBC
    • Olson, L.J.1    Hindgaul, O.2    Dahms, N.M.3    Kim, J.J.P.4
  • 42
    • 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, Neufeld EF (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
    • (1982) Biochem Biophys Res Commun , vol.105 , pp. 814-820
    • Owada, M.1    Neufeld, E.F.2
  • 43
    • 0023988955 scopus 로고
    • Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment
    • Pelham HR (1988) Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J 7:913-918
    • (1988) EMBO J , vol.7 , pp. 913-918
    • Pelham, H.R.1
  • 44
    • 0028834530 scopus 로고
    • The two mannose 6-phosphate receptors transport distinct complements of lysosomal proteins
    • Pohlman R, Wendland M, Boeker C, Von Figura H (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
    • Pohlman, R.1    Wendland, M.2    Boeker, C.3    Von Figura, H.4
  • 45
    • 33845888233 scopus 로고    scopus 로고
    • The 46-kDa mannose 6-phosphate receptor does not depend on endosomal acidification for delivery of hydrolases to lysosomes
    • Probst OC, Ton P, Svoboda B, Gannon A, Schuhmann W, Wieser J, Pohlmann R, Mach L (2006) The 46-kDa mannose 6-phosphate receptor does not depend on endosomal acidification for delivery of hydrolases to lysosomes. J Cell Sci 119:4935-4943
    • (2006) J Cell Sci , vol.119 , pp. 4935-4943
    • Probst, O.C.1    Ton, P.2    Svoboda, B.3    Gannon, A.4    Schuhmann, W.5    Wieser, J.6    Pohlmann, R.7    Mach, L.8
  • 46
    • 0023710423 scopus 로고
    • Identification of mannose 6-phosphate in two asparaginelinked 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 asparaginelinked sugar chains of recombinant transforming growth factor-beta 1 precursor. J Biol Chem 1988 263:14211-14215
    • (1988) J Biol Chem 1988 , 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    Marquardt, R.R.A.H.7
  • 47
    • 39049122146 scopus 로고    scopus 로고
    • Proteomics analysis of serum 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 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
  • 48
    • 0025079686 scopus 로고
    • Brefeldin A prevents uncovering but not phosphorylation of the recognition marker in cathepsin D
    • Radons J, Isidoro C, Hasilik A (1990) Brefeldin A prevents uncovering but not phosphorylation of the recognition marker in cathepsin D. Biol Chem Hoppe-Seyler 371:567-573
    • (1990) Biol Chem Hoppe-Seyler , vol.371 , pp. 567-573
    • Radons, J.1    Isidoro, C.2    Hasilik, A.3
  • 50
    • 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
  • 51
    • 0026334198 scopus 로고
    • Mannose 6-phosphate-independent targeting of cathepsin D to lysosomes in HepG2 cells
    • Rijnboutt S, Kal AJ, Geuze HJ, Aerts H, Strous GJ (1991) Mannose 6-phosphate-independent targeting of cathepsin D to lysosomes in HepG2 cells. J Biol Chem 266:23586-23592
    • (1991) J Biol Chem , vol.266 , pp. 23586-23592
    • Rijnboutt, S.1    Kal, A.J.2    Geuze, H.J.3    Aerts, H.4    Strous, G.J.5
  • 52
    • 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
  • 53
    • 0026713211 scopus 로고
    • The spectrum of incomplete N-linked oligosaccharides synthesized by endothelial cells in the presence of brefeldin
    • Sampath D, Varki A, Freeze HH (1992) The spectrum of incomplete N-linked oligosaccharides synthesized by endothelial cells in the presence of brefeldin. J Biol Chem 267:4440-4455
    • (1992) J Biol Chem , vol.267 , pp. 4440-4455
    • Sampath, D.1    Varki, A.2    Freeze, H.H.3
  • 54
    • 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
  • 55
    • 17844387148 scopus 로고    scopus 로고
    • The human brain mannose 6-phosphate glycoproteome: A complex mixture composed of multiple isoforms of many soluble lysosomal proteins
    • 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
    • (2005) Proteomics , vol.5 , pp. 1520-1532
    • Sleat, D.E.1    Lackland, H.2    Wang, Y.3    Sohar, I.4    Xiao, G.5    Li, H.6    Lobel, P.7
  • 56
    • 33645723014 scopus 로고    scopus 로고
    • Identification of sites of mannose 6-phosphorylation on lysosomal proteins
    • Sleat DE, Zheng H, Qian M, Lobel. P (2006) Identification of sites of mannose 6-phosphorylation on lysosomal proteins. Mol Cell Proteomics 5:686-701
    • (2006) Mol Cell Proteomics , vol.5 , pp. 686-701
    • Sleat, D.E.1    Zheng, H.2    Qian, M.3    Lobel, P.4
  • 57
    • 0032030786 scopus 로고    scopus 로고
    • Mouse mutants lacking the cationindependent 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 cationindependent 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
  • 59
    • 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
  • 60
    • 27144550841 scopus 로고    scopus 로고
    • Mucopolidosis II is caused by mutations in GNPTA encoding tha alpha/beta GlcNac-1-phosphotransferase
    • Tiede S, Storch S, Lubke T, Henrissat B, Bargal R, Raas-Rothschild A, Braulke T (2005) Mucopolidosis II is caused by mutations in GNPTA encoding tha alpha/beta GlcNac-1-phosphotransferase. Nat Med 11:1109-1112
    • (2005) Nat Med , vol.11 , pp. 1109-1112
    • Tiede, S.1    Storch, S.2    Lubke, T.3    Henrissat, B.4    Bargal, R.5    Raas-Rothschild, A.6    Braulke, T.7
  • 61
    • 0024382077 scopus 로고
    • Ligand interactions of the cation-independent mannose 6-phosphate receptor
    • Tong PY, Gregory W, Kornfeld S (1989) Ligand interactions of the cation-independent mannose 6-phosphate receptor. 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
  • 62
    • 0024333810 scopus 로고
    • Ligand interactions of the cation-independent mannose 6-phosphate receptor
    • Tong PY, Kornfeld S (1989) Ligand interactions of 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
  • 63
    • 0030816038 scopus 로고    scopus 로고
    • The trans-Golgi network: A late secretory sorting station
    • Traub LM, Kornfeld S (1997) The trans-Golgi network: a late secretory sorting station. Curr Opin Cell Biol. 9:527-533
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 527-533
    • Traub, L.M.1    Kornfeld, S.2
  • 64
    • 0022407152 scopus 로고
    • The subcellular localization of soluble and membrane-bound lysosomal enzymes in I-cell fibroblasts: A comparative immunocytochemical study
    • Van Dongen JM, Willemsen R, Ginns EI, Sips HJ, Tager JM, Barranger JA, Reuser AJ (1985) The subcellular localization of soluble and membrane-bound lysosomal enzymes in I-cell fibroblasts: a comparative immunocytochemical study. Eur J Cell Biol 39:179-189
    • (1985) Eur J Cell Biol , vol.39 , pp. 179-189
    • Van Dongen, J.M.1    Willemsen, R.2    Ginns, E.I.3    Sips, H.J.4    Tager, J.M.5    Barranger, J.A.6    Reuser, A.J.7
  • 65
    • 39749200034 scopus 로고    scopus 로고
    • Imaging and imagination: Understanding the endolysosomal system
    • Van Meel E, Klumperman J (2008) Imaging and imagination: understanding the endolysosomal system. Histochem Cell Biol 129:253-266
    • (2008) Histochem Cell Biol , vol.129 , pp. 253-266
    • Van Meel, E.1    Klumperman, J.2
  • 66
    • 0019332986 scopus 로고
    • Identification of a rat liver alpha-N-acetylglucosaminyl phosphodiesterase capable of removing 'blocking' alpha-N-acetylglucosamine residues from phosphorylated high mannose oligosaccharides of lysosomal enzymes
    • Varki A, Kornfeld S (1980) Identification of a rat liver alpha-N-acetylglucosaminyl phosphodiesterase capable of removing 'blocking' alpha-N-acetylglucosamine residues from phosphorylated high mannose oligosaccharides of lysosomal enzymes. J Biol Chem 255:8398-8401
    • (1980) J Biol Chem , vol.255 , pp. 8398-8401
    • Varki, A.1    Kornfeld, S.2
  • 67
    • 0026201987 scopus 로고
    • Molecular recognition and targeting of lysosomal proteins
    • Von Figura K (1991) Molecular recognition and targeting of lysosomal proteins. Curr Opin Cell Biol 3:642-646
    • (1991) Curr Opin Cell Biol , vol.3 , pp. 642-646
    • Von Figura, K.1
  • 68
    • 0020411893 scopus 로고
    • Deficiency of UDP-N-acetylglucosamine: Lysosomal enzyme N-acetylglucosamine-1-phosphotransferase in organs of I-cell patients
    • Waheed A, Pohlmann R, Hasilik A, Von Figura K, Van Elsen A, Leroy JG (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
    • (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
  • 69
    • 0024066239 scopus 로고
    • Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells
    • Waheed A, Gottschalk S, Hille A, Kreutler C, Pohlmann R, Braulke T, Hauser H, Geuze H, Von Figura K (1988) Human lysosomal acid phosphatase is transported as a transmembrane protein to lysosomes in transfected baby hamster kidney cells. EMBO J 7:2351-2358
    • (1988) EMBO J , vol.7 , pp. 2351-2358
    • Waheed, A.1    Gottschalk, S.2    Hille, A.3    Kreutler, C.4    Pohlmann, R.5    Braulke, T.6    Hauser, H.7    Geuze, H.8    Von Figura, K.9
  • 70
    • 0041856581 scopus 로고    scopus 로고
    • Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine: Lysosomal enzyme N-acetylglucosaminephosphotransferase
    • Yaghootfam A, Schestag F, Dierks T, Gieselmann V (2003) Recognition of arylsulfatase A and B by the UDP-N-acetylglucosamine: lysosomal enzyme N-acetylglucosaminephosphotransferase. J Biol Chem 278:32653-32661
    • (2003) J Biol Chem , vol.278 , pp. 32653-32661
    • Yaghootfam, A.1    Schestag, F.2    Dierks, T.3    Gieselmann, V.4
  • 71
    • 0028049917 scopus 로고
    • Intermolecular association of lysosomal protein precursors during biosynthesis
    • Zhu Y, Conner GE (1994) Intermolecular association of lysosomal protein precursors during biosynthesis. J Biol Chem 269:3846-3851
    • (1994) J Biol Chem , vol.269 , pp. 3846-3851
    • Zhu, Y.1    Conner, G.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.