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Volumn 3, Issue 1, 1999, Pages 11-21

Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 3 PHOSPHONOPROPIONIC ACID; CD63 ANTIGEN; CELL MEMBRANE PROTEIN; PROTEIN SUBUNIT;

EID: 0033007616     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80170-7     Document Type: Article
Times cited : (589)

References (47)
  • 1
    • 0030774572 scopus 로고    scopus 로고
    • Functional domain mapping of the clathrin-associated adaptor medium chains μ1 and μ2
    • Aguilar, R.C., Ohno, H., Roche, K.W., and Bonifacino, J.S. (1997). Functional domain mapping of the clathrin-associated adaptor medium chains μ1 and μ2. J. Biol. Chem. 272, 27160-27166.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27160-27166
    • Aguilar, R.C.1    Ohno, H.2    Roche, K.W.3    Bonifacino, J.S.4
  • 2
    • 0003362844 scopus 로고    scopus 로고
    • Immunoprecipitation
    • J.S. Bonifacino, M. Dasso, J.B. Harford, J. Lippincott-Schwartz, and K. Yamada, eds. (New York: John Wiley and Sons)
    • Bonifacino, J.S., and Dell'Angelica, E.C. (1998). Immunoprecipitation. In Current Protocols in Cell Biology, J.S. Bonifacino, M. Dasso, J.B. Harford, J. Lippincott-Schwartz, and K. Yamada, eds. (New York: John Wiley and Sons), pp. 7.2.1-7.2.21.
    • (1998) Current Protocols in Cell Biology , pp. 721-7221
    • Bonifacino, J.S.1    Dell'Angelica, E.C.2
  • 3
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathways
    • Bonifacino, J.S., and Weissman, A.M. (1998). Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu. Rev. Cell Dev. Biol. 14, 19-57.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 4
    • 0024577266 scopus 로고
    • Internalization and recycling to serotonin-containing granules of the 80K integral membrane protein exposed on the surface of secreting rat basophilic leukaemia cells
    • Bonifacino, J.S., Yuan, L., and Sandoval, I.V. (1989). Internalization and recycling to serotonin-containing granules of the 80K integral membrane protein exposed on the surface of secreting rat basophilic leukaemia cells. J. Cell Sci. 92, 701-712.
    • (1989) J. Cell Sci. , vol.92 , pp. 701-712
    • Bonifacino, J.S.1    Yuan, L.2    Sandoval, I.V.3
  • 5
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
    • Cowles, C.R., Odorizzi, G., Payne, G.S., and Emr, S.D. (1997). The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole. Cell 91, 109-118.
    • (1997) Cell , vol.91 , pp. 109-118
    • Cowles, C.R.1    Odorizzi, G.2    Payne, G.S.3    Emr, S.D.4
  • 6
    • 0032563630 scopus 로고    scopus 로고
    • Acidic di-leucine motif essential for AP-3-dependent sorting and restriction of the functional specificity of the Vam3p vacuolar t-SNARE
    • Darsow, T., Burd, C.G., and Emr, S.D. (1998). Acidic di-leucine motif essential for AP-3-dependent sorting and restriction of the functional specificity of the Vam3p vacuolar t-SNARE. J. Cell Biol. 142, 913-922.
    • (1998) J. Cell Biol. , vol.142 , pp. 913-922
    • Darsow, T.1    Burd, C.G.2    Emr, S.D.3
  • 7
    • 0022456630 scopus 로고
    • The J.D. mutation in familial hypercholesterolemia: Amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors
    • Davis, C.G., Lehrman, M.A., Russell, D.W., Anderson, R.G., Brown, M.S., and Goldstein, J.L. (1986). The J.D. mutation in familial hypercholesterolemia: Amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors. Cell 45, 15-24.
    • (1986) Cell , vol.45 , pp. 15-24
    • Davis, C.G.1    Lehrman, M.A.2    Russell, D.W.3    Anderson, R.G.4    Brown, M.S.5    Goldstein, J.L.6
  • 9
    • 0031566379 scopus 로고    scopus 로고
    • β3A-adaptin, a subunit of the adaptor-like complex AP-3
    • Dell'Angelica, E.C., Ooi, C.E., and Bonifacino, J.S. (1997b). β3A-adaptin, a subunit of the adaptor-like complex AP-3. J. Biol. Chem. 272, 15078-15084.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15078-15084
    • Dell'Angelica, E.C.1    Ooi, C.E.2    Bonifacino, J.S.3
  • 11
    • 0032076102 scopus 로고    scopus 로고
    • A function for the AP3 coat complex in synaptic vesicle formation from endosomes
    • Faúndez, V., Horng, J.-T., and Kelly, R.B. (1998). A function for the AP3 coat complex in synaptic vesicle formation from endosomes. Cell 93, 423-432.
    • (1998) Cell , vol.93 , pp. 423-432
    • Faúndez, V.1    Horng, J.-T.2    Kelly, R.B.3
  • 12
    • 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
  • 14
    • 6444236367 scopus 로고
    • Albinism associated with hemorrhagic diathesis and unusual pigmented reticular cells in the bone marrow; report of two cases with histochemical studies
    • Hermansky, F., and Pudlak, P. (1959). Albinism associated with hemorrhagic diathesis and unusual pigmented reticular cells in the bone marrow; report of two cases with histochemical studies. Blood 74, 162-169.
    • (1959) Blood , vol.74 , pp. 162-169
    • Hermansky, F.1    Pudlak, P.2
  • 15
    • 0030878575 scopus 로고    scopus 로고
    • Membrane protein biosynthesis all sewn up?
    • High, S., and Laird, V. (1997). Membrane protein biosynthesis all sewn up? Trends Cell. Biol. 7, 206-210.
    • (1997) Trends Cell. Biol. , vol.7 , pp. 206-210
    • High, S.1    Laird, V.2
  • 16
    • 0039109678 scopus 로고    scopus 로고
    • A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3
    • Höning, S., Sandoval, I.V., and von Figura, K. (1998). A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J. 17, 1304-1314.
    • (1998) EMBO J. , vol.17 , pp. 1304-1314
    • Höning, S.1    Sandoval, I.V.2    Von Figura, K.3
  • 17
    • 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
  • 18
    • 0029881147 scopus 로고    scopus 로고
    • The lysosomal granule membrane protein, LAMP-2, is also present in platelet dense granule membranes
    • Israels, S.J., McMillan, E.M., Robertson, C., Singhory, S., and McNiCol, A. (1996). The lysosomal granule membrane protein, LAMP-2, is also present in platelet dense granule membranes. Thromb. Haemost. 75, 623-629.
    • (1996) Thromb. Haemost. , vol.75 , pp. 623-629
    • Israels, S.J.1    McMillan, E.M.2    Robertson, C.3    Singhory, S.4    McNicol, A.5
  • 19
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L., and Riordan, J.R. (1995). Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 21
    • 0030794182 scopus 로고    scopus 로고
    • Linking cargo to vesicle formation: Receptor tail interactions with coat proteins
    • Kirchhausen, T., Bonifacino, J.S., and Riezman, H. (1997). Linking cargo to vesicle formation: Receptor tail interactions with coat proteins. Curr. Opin. Cell Biol. 9, 488-495.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 488-495
    • Kirchhausen, T.1    Bonifacino, J.S.2    Riezman, H.3
  • 23
    • 0028932319 scopus 로고
    • Isolation of 115 human chromosome 8-specific expressed-sequence tags by exon amplification
    • Koyama, K., Sudo, K., and Nakamura, Y. (1995). Isolation of 115 human chromosome 8-specific expressed-sequence tags by exon amplification. Genomics 26, 245-253.
    • (1995) Genomics , vol.26 , pp. 245-253
    • Koyama, K.1    Sudo, K.2    Nakamura, Y.3
  • 25
    • 0028820625 scopus 로고
    • A lysosomal targeting signal in the cytoplasmic tail of the β chain directs HLA-DM to MHC class II compartments
    • Marks, M.S., Roche, P.A., van Donselaar, E., Woodruff, L., Peters, P.J., and Bonifacino, J.S. (1995). A lysosomal targeting signal in the cytoplasmic tail of the β chain directs HLA-DM to MHC class II compartments. J. Cell Biol. 131, 351-369.
    • (1995) J. Cell Biol. , vol.131 , pp. 351-369
    • Marks, M.S.1    Roche, P.A.2    Van Donselaar, E.3    Woodruff, L.4    Peters, P.J.5    Bonifacino, J.S.6
  • 26
    • 0031106781 scopus 로고    scopus 로고
    • Protein sorting by tyrosine-based signals: Adapting to the Ys and wherefores
    • Marks, M.S., Ohno, H., Kirchhausen, T., and Bonifacino, J.S. (1997). Protein sorting by tyrosine-based signals: Adapting to the Ys and wherefores. Trends Cell Biol. 7, 124-128.
    • (1997) Trends Cell Biol. , vol.7 , pp. 124-128
    • Marks, M.S.1    Ohno, H.2    Kirchhausen, T.3    Bonifacino, J.S.4
  • 27
    • 0028981591 scopus 로고
    • Beta-NAP, a cerebellar degeneration antigen, is a neuron-specific vesicle coat protein
    • Newman, L.S., McKeever, M.O., Okano, H.J., and Darnell, R.B. (1995). Beta-NAP, a cerebellar degeneration antigen, is a neuron-specific vesicle coat protein. Cell 82, 773-783.
    • (1995) Cell , vol.82 , pp. 773-783
    • Newman, L.S.1    McKeever, M.O.2    Okano, H.J.3    Darnell, R.B.4
  • 28
  • 29
    • 0030293220 scopus 로고    scopus 로고
    • Positional cloning of a gene for Hermansky-Pudlak syndrome, a disorder of cytoplasmic organelles
    • Oh, J., Bailin, T., Fukai, K., Feng, G.H., Ho, L., Mao, J.I., Frenk, E., Tamura, N., and Spritz, R.A. (1996). Positional cloning of a gene for Hermansky-Pudlak syndrome, a disorder of cytoplasmic organelles. Nat. Genet. 14, 300-306.
    • (1996) Nat. Genet. , vol.14 , pp. 300-306
    • Oh, J.1    Bailin, T.2    Fukai, K.3    Feng, G.H.4    Ho, L.5    Mao, J.I.6    Frenk, E.7    Tamura, N.8    Spritz, R.A.9
  • 31
    • 0029826535 scopus 로고    scopus 로고
    • Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains
    • Ohno, H., Fournier, M.C., Poy, G., and Bonifacino, J.S. (1996). Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains. J. Biol. Chem. 271, 29009-29015.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29009-29015
    • Ohno, H.1    Fournier, M.C.2    Poy, G.3    Bonifacino, J.S.4
  • 32
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals
    • Ohno, H., Aguilar, R.C., Yeh, D., Taura, D., Saito, T., and Bonifacino, J.S. (1998). The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals. J. Biol. Chem. 273, 25915-25921.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25915-25921
    • Ohno, H.1    Aguilar, R.C.2    Yeh, D.3    Taura, D.4    Saito, T.5    Bonifacino, J.S.6
  • 33
    • 0030747460 scopus 로고    scopus 로고
    • Altered expression of a novel daptin leads to defective pigment granule biogenesis in the Drosophila eye color mutant garnet
    • Ooi, C.E., Moreira, J.E., Dell'Angelica, E.G., Poy, G., Wassarman, D.A., and Bonifacino, J.S. (1997). Altered expression of a novel daptin leads to defective pigment granule biogenesis in the Drosophila eye color mutant garnet. EMBO J. 16, 4508-4518.
    • (1997) EMBO J. , vol.16 , pp. 4508-4518
    • Ooi, C.E.1    Moreira, J.E.2    Dell'Angelica, E.G.3    Poy, G.4    Wassarman, D.A.5    Bonifacino, J.S.6
  • 34
    • 0032572560 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes
    • Ooi, C.E., Dell'Angelica, E.C., and Bonifacino, J.S. (1998). ADP-ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes. J. Cell Biol. 142, 391-402.
    • (1998) J. Cell Biol. , vol.142 , pp. 391-402
    • Ooi, C.E.1    Dell'Angelica, E.C.2    Bonifacino, J.S.3
  • 35
    • 0029081168 scopus 로고
    • Melanosomes are specialized members of the lysosomal lineage of organelles
    • Orlow, S.J. (1995). Melanosomes are specialized members of the lysosomal lineage of organelles. J. Invest. Dermatol. 105, 3-7.
    • (1995) J. Invest. Dermatol. , vol.105 , pp. 3-7
    • Orlow, S.J.1
  • 36
    • 0026034448 scopus 로고
    • Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments
    • Peters, P.J., Neefjes, J.J., Oorschot, V., Ploegh, H.L., and Geuze, H.J. (1991). Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments. Nature 349, 669-676.
    • (1991) Nature , vol.349 , pp. 669-676
    • Peters, P.J.1    Neefjes, J.J.2    Oorschot, V.3    Ploegh, H.L.4    Geuze, H.J.5
  • 37
    • 0027981251 scopus 로고
    • Two rat homologs of clathrin-associated adaptor proteins
    • Pevsner, J., Volknandt, W., Wong, B.R., and Scheller, R.H. (1994). Two rat homologs of clathrin-associated adaptor proteins. Gene 146, 279-283.
    • (1994) Gene , vol.146 , pp. 279-283
    • Pevsner, J.1    Volknandt, W.2    Wong, B.R.3    Scheller, R.H.4
  • 38
    • 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
  • 39
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J.E., and Wieland, F.T. (1996). Protein sorting by transport vesicles. Science 272, 227-234.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 40
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and Orci, L. (1996). Coat proteins and vesicle budding. Science 271, 1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 42
    • 0030926547 scopus 로고    scopus 로고
    • Characterization of the adaptor-related protein complex, AP-3
    • Simpson, F., Peden, A.A., Christopoulou, L., and Robinson, M.S. (1997). Characterization of the adaptor-related protein complex, AP-3. J. Cell Biol. 137, 835-845.
    • (1997) J. Cell Biol. , vol.137 , pp. 835-845
    • Simpson, F.1    Peden, A.A.2    Christopoulou, L.3    Robinson, M.S.4
  • 43
    • 0031408332 scopus 로고    scopus 로고
    • The yeast AP-3 complex is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole
    • Stepp, J.D., Huang, K., and Lemmon, S.K. (1997). The yeast AP-3 complex is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole. J. Cell Biol. 139, 1761-1774.
    • (1997) J. Cell Biol. , vol.139 , pp. 1761-1774
    • Stepp, J.D.1    Huang, K.2    Lemmon, S.K.3
  • 44
    • 0029126743 scopus 로고
    • Intracellular sorting and targeting of melanosomal membrane proteins: Identification of signals for sorting of the human brown locus protein, gp75
    • Vijayasaradhi, S., Xu, Y., Bouchard, B., and Houghton, A.N. (1995). Intracellular sorting and targeting of melanosomal membrane proteins: Identification of signals for sorting of the human brown locus protein, gp75. J. Cell Biol. 130, 807-820.
    • (1995) J. Cell Biol. , vol.130 , pp. 807-820
    • Vijayasaradhi, S.1    Xu, Y.2    Bouchard, B.3    Houghton, A.N.4
  • 45
    • 0032079666 scopus 로고    scopus 로고
    • A dileucine-like sorting signal directs transport into an AP-3-dependent, clathrin-independent pathway to the yeast vacuole
    • Vowels, J.J., and Payne, G.S. (1998). A dileucine-like sorting signal directs transport into an AP-3-dependent, clathrin-independent pathway to the yeast vacuole. EMBO J 17, 2482-2493.
    • (1998) EMBO J , vol.17 , pp. 2482-2493
    • Vowels, J.J.1    Payne, G.S.2
  • 46
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S., and Kopito, R.R.(1995). Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 47


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