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Volumn 120, Issue 6, 1996, Pages 1088-1094

Biosynthetic transport of a major lysosome-associated membrane glycoprotein 2, lamp-2: A significant fraction of newly synthesized lamp-2 is delivered to lysosomes by way of early endosomes

Author keywords

Biosynthesis; Endocytosis; Endosome; Lysosome; Membrane glycoprotein

Indexed keywords

GLYCOPROTEIN; MEMBRANE PROTEIN;

EID: 0030462963     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021526     Document Type: Article
Times cited : (28)

References (37)
  • 1
    • 0004266608 scopus 로고
    • Plenum Press, New York
    • Holtzman, E. (1989) Lysosomes, Plenum Press, New York
    • (1989) Lysosomes
    • Holtzman, E.1
  • 4
    • 0024449827 scopus 로고
    • Membrane traffic in endocytosis: Insights from cell-free assays
    • Gruenberg, J. and Howell, K.E. (1989) Membrane traffic in endocytosis: Insights from cell-free assays. Annu. Rev. Cell Biol. 5, 453-481
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 453-481
    • Gruenberg, J.1    Howell, K.E.2
  • 5
    • 0025789665 scopus 로고
    • Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking
    • Fukuda, M. (1991) Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking. J. Biol. Chem. 266, 21327-21330
    • (1991) J. Biol. Chem. , vol.266 , pp. 21327-21330
    • Fukuda, M.1
  • 6
    • 0028232681 scopus 로고
    • Biogenesis of lysosomal membranes
    • Peters, C. and von Figura, K. (1994) Biogenesis of lysosomal membranes. FEBS Lett. 346, 108-114
    • (1994) FEBS Lett. , vol.346 , pp. 108-114
    • Peters, C.1    Von Figura, K.2
  • 7
    • 0030137994 scopus 로고    scopus 로고
    • Intracellular trafficking of lysosomal membrane proteins
    • Hunziker, W. and Geuze, H.J. (1996) Intracellular trafficking of lysosomal membrane proteins. Bioessays 18, 379-389
    • (1996) Bioessays , vol.18 , pp. 379-389
    • Hunziker, W.1    Geuze, H.J.2
  • 8
    • 0022515318 scopus 로고
    • Lysosomal membrane dynamics: Structure and interorganellar movement of a major lysosomal membrane glycoprotein
    • Lippincott-Schwartz, J. and Fambrough, D.M. (1986) Lysosomal membrane dynamics: Structure and interorganellar movement of a major lysosomal membrane glycoprotein. J. Cell Biol. 102, 1593-1605
    • (1986) J. Cell Biol. , vol.102 , pp. 1593-1605
    • Lippincott-Schwartz, J.1    Fambrough, D.M.2
  • 9
    • 0023644927 scopus 로고
    • Cycling of the integral membrane glycoprotein, LEP100, between plasma membrane and lysosomes: Kinetic and morphological analysis
    • Lippincott-Schwartz, J. and Fambrough, D.M. (1987) Cycling of the integral membrane glycoprotein, LEP100, between plasma membrane and lysosomes: Kinetic and morphological analysis. Cell 49, 669-677
    • (1987) Cell , vol.49 , pp. 669-677
    • Lippincott-Schwartz, J.1    Fambrough, D.M.2
  • 11
    • 0024449198 scopus 로고
    • Biochemical analysis of the movement of a major lysosomal membrane glycoprotein in the endocytic membrane system
    • Furuno, K., Yano, S., Akasaki, K., Tanaka, Y., Yamaguchi, Y., Tsuji, H., Himeno, M., and Kato, K. (1989) Biochemical analysis of the movement of a major lysosomal membrane glycoprotein in the endocytic membrane system. J. Biochem. 106, 717-722
    • (1989) J. Biochem. , vol.106 , pp. 717-722
    • Furuno, K.1    Yano, S.2    Akasaki, K.3    Tanaka, Y.4    Yamaguchi, Y.5    Tsuji, H.6    Himeno, M.7    Kato, K.8
  • 12
    • 0027433881 scopus 로고
    • Cycling of two endogenous lysosomal membrane proteins, lamp-2 and acid phosphatase, between the cell surface and lysosomes in cultured rat hepatocytes
    • Akasaki, K., Fukuzawa, M., Kinoshita, H., Furuno, K., and Tsuji, H. (1993) Cycling of two endogenous lysosomal membrane proteins, lamp-2 and acid phosphatase, between the cell surface and lysosomes in cultured rat hepatocytes. J. Biochem. 114, 598-604
    • (1993) J. Biochem. , vol.114 , pp. 598-604
    • Akasaki, K.1    Fukuzawa, M.2    Kinoshita, H.3    Furuno, K.4    Tsuji, H.5
  • 14
    • 0028273713 scopus 로고
    • Anti-tumor antibody BR96 blocks cell migration and binds to a lysosomal membrane glycoprotein on cell surface microspikes and ruffled membranes
    • Garrigues, J., Anderson, J., Hellström, K.E., and Hellström, I. (1994) Anti-tumor antibody BR96 blocks cell migration and binds to a lysosomal membrane glycoprotein on cell surface microspikes and ruffled membranes. J. Cell Biol. 125, 129-142
    • (1994) J. Cell Biol. , vol.125 , pp. 129-142
    • Garrigues, J.1    Anderson, J.2    Hellström, K.E.3    Hellström, I.4
  • 15
    • 0023580391 scopus 로고
    • Kinetics of intracellular transport and sorting of lysosomal membrane and plasma membrane proteins
    • Green, S.A., Zimmer, K.-P., Griffiths, G., and Mellman, I. (1987) Kinetics of intracellular transport and sorting of lysosomal membrane and plasma membrane proteins. J. Cell Biol. 105, 1227-1240
    • (1987) J. Cell Biol. , vol.105 , pp. 1227-1240
    • Green, S.A.1    Zimmer, K.-P.2    Griffiths, G.3    Mellman, I.4
  • 16
    • 0022508705 scopus 로고
    • A kinetic analysis of biosynthesis and localization of a lysosome-associated membrane glycoprotein
    • D'Souza, M.P. and August, J.T. (1986) A kinetic analysis of biosynthesis and localization of a lysosome-associated membrane glycoprotein. Arch. Biochem. Biophys. 249, 522-532
    • (1986) Arch. Biochem. Biophys. , vol.249 , pp. 522-532
    • D'Souza, M.P.1    August, J.T.2
  • 17
    • 0026702499 scopus 로고
    • The lysosomal membrane glycoprotein lamp-1 is transported to lysosomes by two alternative pathways
    • Carlsson, S.R. and Fukuda, M. (1992) The lysosomal membrane glycoprotein lamp-1 is transported to lysosomes by two alternative pathways. Arch. Biochem. Biophys. 296, 630-639
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 630-639
    • Carlsson, S.R.1    Fukuda, M.2
  • 18
    • 0026327392 scopus 로고
    • An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes
    • Nabi, I.R., Le Bivic, A., Fambrough, D., and Rodriguez-Boulan, E. (1991) An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes. J. Cell Biol. 115, 1573-1584
    • (1991) J. Cell Biol. , vol.115 , pp. 1573-1584
    • Nabi, I.R.1    Le Bivic, A.2    Fambrough, D.3    Rodriguez-Boulan, E.4
  • 19
    • 0024845390 scopus 로고
    • Lysosomal acid phosphatase is transported to lysosomes via the cell surface
    • Braun, M., Waheed, A., and von Figura, K. (1989) Lysosomal acid phosphatase is transported to lysosomes via the cell surface. EMBO J. 8, 3633-3640
    • (1989) EMBO J. , vol.8 , pp. 3633-3640
    • Braun, M.1    Waheed, A.2    Von Figura, K.3
  • 20
    • 0026726955 scopus 로고
    • The pathway and targeting signal for delivery of the integral membrane glycoprotein LEP100 to lysosomes
    • Mathews, P.M., Martinie, J.B., and Fambrough, D.M. (1992) The pathway and targeting signal for delivery of the integral membrane glycoprotein LEP100 to lysosomes. J. Cell Biol. 118, 1027-1040
    • (1992) J. Cell Biol. , vol.118 , pp. 1027-1040
    • Mathews, P.M.1    Martinie, J.B.2    Fambrough, D.M.3
  • 21
    • 0026545549 scopus 로고
    • Transport of the lysosomal membrane glycoprotein Igp120 (Igp-A) to lysosomes does not require appearance on the plasma membrane
    • Harter, C. and Mellman, I. (1992) Transport of the lysosomal membrane glycoprotein Igp120 (Igp-A) to lysosomes does not require appearance on the plasma membrane. J. Cell Biol. 117, 311-325
    • (1992) J. Cell Biol. , vol.117 , pp. 311-325
    • Harter, C.1    Mellman, I.2
  • 22
    • 0029084767 scopus 로고
    • Biosynthetic transport of a major lysosomal membrane glycoprotein, lamp-1: Convergence of biosynthetic and endocytic pathways occurs at three distinctive points
    • Akasaki, K., Michihara, A., Mibuka, K., Fujiwara, Y., and Tsuji, H. (1995) Biosynthetic transport of a major lysosomal membrane glycoprotein, lamp-1: Convergence of biosynthetic and endocytic pathways occurs at three distinctive points. Exp. Cell Res. 220, 464-473
    • (1995) Exp. Cell Res. , vol.220 , pp. 464-473
    • Akasaki, K.1    Michihara, A.2    Mibuka, K.3    Fujiwara, Y.4    Tsuji, H.5
  • 23
    • 0026347730 scopus 로고
    • Purification, some properties, and tissue distribution of a major lysosome-associated membrane glycoprotein (r-lamp-2) of rat liver
    • Akasaki, K., Yamaguchi, Y., Furuno, K., and Tsuji, H. (1991) Purification, some properties, and tissue distribution of a major lysosome-associated membrane glycoprotein (r-lamp-2) of rat liver. J. Biochem. 110, 922-927
    • (1991) J. Biochem. , vol.110 , pp. 922-927
    • Akasaki, K.1    Yamaguchi, Y.2    Furuno, K.3    Tsuji, H.4
  • 24
    • 0017101039 scopus 로고
    • Preparation of isolated rat liver cells
    • Seglen, P.O. (1976) Preparation of isolated rat liver cells. Methods Cell Biol. 13, 29-83
    • (1976) Methods Cell Biol. , vol.13 , pp. 29-83
    • Seglen, P.O.1
  • 25
    • 0014429914 scopus 로고
    • Glycosidases in the nervous system. I. Assay, some properties, and distribution of β-galactosidase, β-glucuronidase, and β-glucosidase
    • Robins, E., Hirsch, H.E., and Emmons, S.S. (1968) Glycosidases in the nervous system. I. Assay, some properties, and distribution of β-galactosidase, β-glucuronidase, and β-glucosidase. J. Biol. Chem. 243, 4246-4252
    • (1968) J. Biol. Chem. , vol.243 , pp. 4246-4252
    • Robins, E.1    Hirsch, H.E.2    Emmons, S.S.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 29
    • 0022975133 scopus 로고
    • The trans Golgi network: Sorting at the exit site of the Golgi complex
    • Griffiths, G. and Simons, K. (1986) The trans Golgi network: sorting at the exit site of the Golgi complex. Science 234, 438-443
    • (1986) Science , vol.234 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 30
    • 0027211772 scopus 로고
    • Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer
    • Nabi, I.R. and Rodriguez-Boulan, E. (1993) Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer. Mol. Biol. Cell 4, 627-635
    • (1993) Mol. Biol. Cell , vol.4 , pp. 627-635
    • Nabi, I.R.1    Rodriguez-Boulan, E.2
  • 31
    • 0025172954 scopus 로고
    • Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail
    • Williams, M.A. and Fukuda, M. (1990) Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail. J. Cell Biol. 111, 955-966
    • (1990) J. Cell Biol. , vol.111 , pp. 955-966
    • Williams, M.A.1    Fukuda, M.2
  • 32
    • 0027396163 scopus 로고
    • The motif Tyr-X-X-hydrophobic residue mediates lysosomal membrane targeting of lysosome-associated membrane protein 1
    • Guarnieri, F.G., Arterburn, L.M., Penno, M.B., Cha, Y., and August, J.T. (1993) The motif Tyr-X-X-hydrophobic residue mediates lysosomal membrane targeting of lysosome-associated membrane protein 1. J. Biol. Chem. 268, 1941-1946
    • (1993) J. Biol. Chem. , vol.268 , pp. 1941-1946
    • Guarnieri, F.G.1    Arterburn, L.M.2    Penno, M.B.3    Cha, Y.4    August, J.T.5
  • 33
    • 0028929058 scopus 로고
    • Cytoplasmic determinants involved in direct lysosomal sorting, endocytosis, and basolateral targeting of rat Igp120 (lamp-1) in MDCK cells
    • Honing, S. and Hunziker, W. (1995) Cytoplasmic determinants involved in direct lysosomal sorting, endocytosis, and basolateral targeting of rat Igp120 (lamp-1) in MDCK cells. J. Cell Biol. 128, 321-332
    • (1995) J. Cell Biol. , vol.128 , pp. 321-332
    • Honing, S.1    Hunziker, W.2
  • 34
    • 0029670902 scopus 로고    scopus 로고
    • The targeting of lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane
    • Rohrer, J., Schweizer, A., Russell, D., and Kornfeld, S. (1996) The targeting of lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. J. Cell Biol. 132, 565-576
    • (1996) J. Cell Biol. , vol.132 , pp. 565-576
    • Rohrer, J.1    Schweizer, A.2    Russell, D.3    Kornfeld, S.4
  • 36
    • 0029047863 scopus 로고
    • Multiple mRNAs encode the avian lysosomal membrane protein LAMP-2, resulting in alternative transmembrane and cytoplasmic domains
    • Hatem, C.L., Gough, N.R., and Fambrough, D.M. (1995) Multiple mRNAs encode the avian lysosomal membrane protein LAMP-2, resulting in alternative transmembrane and cytoplasmic domains. J. Cell. Sci. 108, 2093-2100
    • (1995) J. Cell. Sci. , vol.108 , pp. 2093-2100
    • Hatem, C.L.1    Gough, N.R.2    Fambrough, D.M.3
  • 37
    • 0028804783 scopus 로고
    • An alternatively spliced form of the human lysosome-associated membrane protein-2 gene is expressed in a tissue-specific manner
    • Konecki, D.S., Foetisch, K., Zimmer, K.-P., Schlotter, M., and Lichter-Konecki, U. (1995) An alternatively spliced form of the human lysosome-associated membrane protein-2 gene is expressed in a tissue-specific manner. Biochem. Biophys. Res. Commun. 215, 757-767
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 757-767
    • Konecki, D.S.1    Foetisch, K.2    Zimmer, K.-P.3    Schlotter, M.4    Lichter-Konecki, U.5


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