메뉴 건너뛰기




Volumn 3, Issue 2, 2002, Pages 122-131

Secretory lysosomes

Author keywords

[No Author keywords available]

Indexed keywords

CELL COMPARTMENTALIZATION; CELL ORGANELLE; CELL TYPE; GENETIC DISORDER; IMMUNE SYSTEM; LYSOSOME; PIGMENTATION; PRIORITY JOURNAL; PROTEIN TARGETING; REVIEW; SECRETORY CELL; SECRETORY GRANULE; SECRETORY LYSOSOME; ANIMAL; BIOLOGICAL MODEL; ENDOCYTOSIS; EVOLUTION; EXOCYTOSIS; HUMAN; MEMBRANE FUSION; METABOLISM; PATHOPHYSIOLOGY; PHYSIOLOGY; SECRETION;

EID: 0036481624     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm732     Document Type: Review
Times cited : (619)

References (97)
  • 1
    • 0035490904 scopus 로고    scopus 로고
    • The melanosome: Membrane dynamics in black and white
    • Marks, M. S. & Seabra, M. C. The melanosome: membrane dynamics in black and white. Nature Rev. Mol. Cell Biol. 2, 738-748 (2001). Together with reference 12, this reference provides a comprehensive account of melanosome function. Reference 1 in particular provides complementary reading to this review, especially on aspects of melanosome function in the inherited diseases, such as HPS.
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 738-748
    • Marks, M.S.1    Seabra, M.C.2
  • 2
    • 0022348139 scopus 로고
    • Cell-mediated extracellular acidification and bone resorption: Evidence for a low pH in resorbing lacunae and localization of a 100-kD lysosomal membrane protein at the osteoclast ruffled border
    • Baron, R., Neff, L., Louvard, D. & Courtoy, P. J. Cell-mediated extracellular acidification and bone resorption: evidence for a low pH in resorbing lacunae and localization of a 100-kD lysosomal membrane protein at the osteoclast ruffled border. J. Cell Biol. 101, 2210-2222 (1985).
    • (1985) J. Cell Biol. , vol.101 , pp. 2210-2222
    • Baron, R.1    Neff, L.2    Louvard, D.3    Courtoy, P.J.4
  • 3
    • 0024419921 scopus 로고
    • Molecules relevant for T cell-target cell interaction are present in cytolytic granules of human T lymphocytes
    • Peters, P. J. et al. Molecules relevant for T cell-target cell interaction are present in cytolytic granules of human T lymphocytes. Eur. J. Immunol. 19, 1469-1475 (1989).
    • (1989) Eur. J. Immunol. , vol.19 , pp. 1469-1475
    • Peters, P.J.1
  • 4
    • 0025905925 scopus 로고
    • Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes
    • Peters, P. J. et al. Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes. J. Exp. Med. 173, 1099-1109 (1991).
    • (1991) J. Exp. Med. , vol.173 , pp. 1099-1109
    • Peters, P.J.1
  • 5
    • 0026034448 scopus 로고
    • Segregation of MHC class II molecules from MHC class 1 molecules in the Golgi complex for transport to lysosomal compartments
    • Peters, P. J., Neefjes, J. J., Oorschot, V., Ploegh, H. L. & Geuze, H. J. Segregation of MHC class II molecules from MHC class 1 molecules in the Golgi complex for transport to lysosomal compartments. Nature 349, 669-676 (1991).
    • (1991) Nature , vol.1 , pp. 669-676
    • Peters, P.J.1    Neefjes, J.J.2    Oorschot, V.3    Ploegh, H.L.4    Geuze, H.J.5
  • 6
    • 0033165875 scopus 로고    scopus 로고
    • Platelet dense granules: Structure, function and implications for haemostasis
    • McNicol, A. & Israels, S. J. Platelet dense granules: structure, function and implications for haemostasis. Thromb. Res. 95, 1-18 (1999).
    • (1999) Thromb. Res. , vol.95 , pp. 1-18
    • McNicol, A.1    Israels, S.J.2
  • 8
    • 0030890357 scopus 로고    scopus 로고
    • Biosynthesis, processing and sorting of neutrophil proteins: Insight into neutrophil granule development
    • Gullberg, U., Andersson, E., Garwicz, D., Lindmark, A. & Olsson, I. Biosynthesis, processing and sorting of neutrophil proteins: insight into neutrophil granule development. Eur. J. Haematol. 58, 137-153 (1997).
    • (1997) Eur. J. Haematol. , vol.58 , pp. 137-153
    • Gullberg, U.1    Andersson, E.2    Garwicz, D.3    Lindmark, A.4    Olsson, I.5
  • 9
    • 0028328732 scopus 로고
    • Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus
    • Desjardins, M., Huber, L. A., Parton, R. G. & Griffiths, G. Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus. J. Cell. Biol. 124, 677-688 (1994).
    • (1994) J. Cell. Biol. , vol.124 , pp. 677-688
    • Desjardins, M.1    Huber, L.A.2    Parton, R.G.3    Griffiths, G.4
  • 10
    • 0029071799 scopus 로고
    • The src-family protein-tyrosine kinase p 59hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation
    • Mohn, H., Le Cabec, V., Fischer, S. & Maridonneau-Parini, I. The src-family protein-tyrosine kinase p59hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation. Biochem. J. 309, 657-665 (1995).
    • (1995) Biochem. J. , vol.309 , pp. 657-665
    • Mohn, H.1    Le Cabec, V.2    Fischer, S.3    Maridonneau-Parini, I.4
  • 11
    • 0033709933 scopus 로고    scopus 로고
    • Molecular control of neural crest formation, migration and differentiation
    • Christiansen, J. H., Coles, E. G. & Wilkinson, D. G. Molecular control of neural crest formation, migration and differentiation. Curr. Opin. Cell Biol. 12, 719-724 (2000).
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 719-724
    • Christiansen, J.H.1    Coles, E.G.2    Wilkinson, D.G.3
  • 12
    • 0029081168 scopus 로고
    • Melanosomes are specialized members of the lysosomal lineage of organelles
    • Orlow, S. J. Melanosomes are specialized members of the lysosomal lineage of organelles. J. Invest. Dermatol. 105, 3-7 (1995). This paper highlights and discusses the lysosomal characteristics of melanosomes.
    • (1995) J. Invest. Dermatol. , vol.105 , pp. 3-7
    • Orlow, S.J.1
  • 13
    • 0030783009 scopus 로고    scopus 로고
    • Dense core lysosomes can fuse with late endosomes and are re-formed from the resultant hybrid organelles
    • Bright, N. A., Reaves, B. J., Mullock, B. M. & Luzio, J. P. Dense core lysosomes can fuse with late endosomes and are re-formed from the resultant hybrid organelles. J. Cell Sci. 110, 2027-2040 (1997).
    • (1997) J. Cell Sci. , vol.110 , pp. 2027-2040
    • Bright, N.A.1    Reaves, B.J.2    Mullock, B.M.3    Luzio, J.P.4
  • 14
    • 0034189092 scopus 로고    scopus 로고
    • Secretory lysosome biogenesis in cytotoxic T lymphocytes from normal and Chediak-Higashi syndrome patients
    • Stinchcombe, J. C., Page, L. J. & Griffiths, G. M. Secretory lysosome biogenesis in cytotoxic T lymphocytes from normal and Chediak-Higashi syndrome patients. Traffic 1, 435-444 (2000).
    • (2000) Traffic , vol.1 , pp. 435-444
    • Stinchcombe, J.C.1    Page, L.J.2    Griffiths, G.M.3
  • 15
    • 0030298068 scopus 로고    scopus 로고
    • The biogenesis of lysosomes: Is it a kiss and run, continuous fusion and fission process?
    • Storrie, B. & Desjardins, M. The biogenesis of lysosomes: is it a kiss and run, continuous fusion and fission process? Bioessays 18, 895-903 (1996).
    • (1996) Bioessays , vol.18 , pp. 895-903
    • Storrie, B.1    Desjardins, M.2
  • 16
    • 0035074341 scopus 로고    scopus 로고
    • The molecular machinery for lysosome biogenesis
    • Mullins, C. & Bonifacino, J. S. The molecular machinery for lysosome biogenesis. Bioessays 23, 333-343 (2001).
    • (2001) Bioessays , vol.23 , pp. 333-343
    • Mullins, C.1    Bonifacino, J.S.2
  • 17
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo, A. M. & Dice, J. F. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273, 501-503 (1996). This paper identifies a receptor (Lgp96) on the lysosomal membrane for the selective import of cytosolic proteins that are destined for degradation in the lysosome.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 18
    • 0034232418 scopus 로고    scopus 로고
    • Regulation of lamp2a levels in the lysosomal membrane
    • Cuervo, A. M. & Dice, J. F. Regulation of lamp2a levels in the lysosomal membrane. Traffic 1, 570-583 (2000).
    • (2000) Traffic , vol.1 , pp. 570-583
    • Cuervo, A.M.1    Dice, J.F.2
  • 19
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang, H. L., Terlecky, S. R., Plant, C. P. & Dice, J. F. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246, 382-385 (1989).
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 20
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes, F. A. & Dice, J. F. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J. Cell Sci. 114, 2491-2499 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 21
    • 0026001168 scopus 로고
    • Targeting specific proteins for lysosomal proteolysis
    • Olson, T. S., Terlecky, S. R. & Dice, J. F. Targeting specific proteins for lysosomal proteolysis. Biomed. Biochim. Acta 50, 393-397 (1991).
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 393-397
    • Olson, T.S.1    Terlecky, S.R.2    Dice, J.F.3
  • 22
    • 0034256042 scopus 로고    scopus 로고
    • Regulated secretion of conventional lysosomes
    • Andrews, N. W. Regulated secretion of conventional lysosomes. Trends Cell Biol. 10, 316-321 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 316-321
    • Andrews, N.W.1
  • 23
    • 0035958557 scopus 로고    scopus 로고
    • 2+-regulated exocytosis of lysosomes
    • 2+-regulated lysosomal exocytosis in plasma-membrane repair and highlight a crucial role for SytVII in this process.
    • (2001) Cell , vol.106 , pp. 157-169
    • Reddy, A.1    Caler, E.V.2    Andrews, N.W.3
  • 24
    • 0029837980 scopus 로고    scopus 로고
    • Direct vesicular transport of MHC class II molecules from lysosomal structures to the cell surface
    • Wubbolts, R. et al. Direct vesicular transport of MHC class II molecules from lysosomal structures to the cell surface. J. Cell Biol. 135, 611-622 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 611-622
    • Wubbolts, R.1
  • 25
    • 0029989258 scopus 로고    scopus 로고
    • B lymphocytes secrete antigen-presenting vesicles
    • Raposo, G. et al. B lymphocytes secrete antigen-presenting vesicles. J. Exp. Med. 183, 1161-1172 (1996).
    • (1996) J. Exp. Med. , vol.183 , pp. 1161-1172
    • Raposo, G.1
  • 26
    • 0031863853 scopus 로고    scopus 로고
    • Eradication of established murine tumors using a novel cell-free vaccine: Dendritic cell-derived exosomes
    • Zitvogel, L. et al. Eradication of established murine tumors using a novel cell-free vaccine: dendritic cell-derived exosomes. Nature Med. 4, 594-600 (1998).
    • (1998) Nature Med. , vol.4 , pp. 594-600
    • Zitvogel, L.1
  • 27
    • 0035494424 scopus 로고    scopus 로고
    • Reorganization of multivesicular bodies regulates MHC class II antigen presentation by dendritic cells
    • Kieijmeer, M. et al. Reorganization of multivesicular bodies regulates MHC class II antigen presentation by dendritic cells. J. Cell Biol. 155, 53-63 (2001). Here, the authors describe a mechanism by which proteins that are localized to the internal vesicles of an MVB appear on the limiting membrane of the structure.
    • (2001) J. Cell Biol. , vol.155 , pp. 53-63
    • Kieijmeer, M.1
  • 28
    • 0035911146 scopus 로고    scopus 로고
    • Distinct protein sorting and localization to premelanosomes, melanosomes, and lysosomes in pigmented melanocytic cells
    • Raposo, G., Tenza, D., Murphy, D. M., Berson, J. F. & Marks, M. S. Distinct protein sorting and localization to premelanosomes, melanosomes, and lysosomes in pigmented melanocytic cells. J. Cell Biol. 152, 809-824 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 809-824
    • Raposo, G.1    Tenza, D.2    Murphy, D.M.3    Berson, J.F.4    Marks, M.S.5
  • 29
    • 0025175087 scopus 로고
    • The activation of resting lymphocytes is accompanied by the biogenesis of lysosomal organelles
    • Olsen, I., Bou-Gharios, G. & Abraham, D. The activation of resting lymphocytes is accompanied by the biogenesis of lysosomal organelles. Eur. J. Immunol. 20, 2161-2170 (1990).
    • (1990) Eur. J. Immunol. , vol.20 , pp. 2161-2170
    • Olsen, I.1    Bou-Gharios, G.2    Abraham, D.3
  • 30
    • 0028914352 scopus 로고
    • Serial killing by cytotoxic T lymphocytes: T cell receptor triggers degranulation, re-filling of the lytic granules and secretion of lytic proteins via a non-granule pathway
    • Isaaz, S., Baetz, K., Olsen, K., Podack, E. & Griffiths, G. M. Serial killing by cytotoxic T lymphocytes: T cell receptor triggers degranulation, re-filling of the lytic granules and secretion of lytic proteins via a non-granule pathway. Eur. J. Immunol. 25, 1071-1079 (1995).
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1071-1079
    • Isaaz, S.1    Baetz, K.2    Olsen, K.3    Podack, E.4    Griffiths, G.M.5
  • 31
    • 0025340873 scopus 로고
    • Lysosomal enzyme secretory mutants of Dictyostelium discoideum
    • Ebert, D. L., Jordan, K. B. & Dimond, R. L. Lysosomal enzyme secretory mutants of Dictyostelium discoideum. J. Cell Sci. 96, 491-500 (1990).
    • (1990) J. Cell Sci. , vol.96 , pp. 491-500
    • Ebert, D.L.1    Jordan, K.B.2    Dimond, R.L.3
  • 32
    • 0030730833 scopus 로고    scopus 로고
    • Caenorhabditis elegans rab-3 mutant synapses exhibit impaired function and are partially depleted of vesicles
    • Nonet, M. L. et al. Caenorhabditis elegans rab-3 mutant synapses exhibit impaired function and are partially depleted of vesicles. J. Neurosci. 17, 8061-8073 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 8061-8073
    • Nonet, M.L.1
  • 33
    • 0030943904 scopus 로고    scopus 로고
    • Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells
    • Kuliawat, R., Klumperman, J., Ludwig, T. & Arvan, P. Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells. J. Cell Biol. 137, 595-608 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 595-608
    • Kuliawat, R.1    Klumperman, J.2    Ludwig, T.3    Arvan, P.4
  • 34
    • 0032550222 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles
    • Klumperman, J., Kuliawat, R., Griffith, J. M., Geuze, H. J. & Arvan, P. Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles. J. Cell Biol. 141, 359-371 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 359-371
    • Klumperman, J.1    Kuliawat, R.2    Griffith, J.M.3    Geuze, H.J.4    Arvan, P.5
  • 35
    • 0032742816 scopus 로고    scopus 로고
    • Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis
    • Kundra, R. & Kornfeld, S. Asparagine-linked oligosaccharides protect Lamp-1 and Lamp-2 from intracellular proteolysis. J. Biol. Chem. 274, 31039-31046 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31039-31046
    • Kundra, R.1    Kornfeld, S.2
  • 36
    • 0034689004 scopus 로고    scopus 로고
    • The formation of immunogenic major histocompatibility complex class II-peptide ligands in lysosomal compartments of dendritic cells is regulated by inflammatory stimuli
    • Inaba, K. et al. The formation of immunogenic major histocompatibility complex class II-peptide ligands in lysosomal compartments of dendritic cells is regulated by inflammatory stimuli. J. Exp. Med. 191, 927-936 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 927-936
    • Inaba, K.1
  • 37
    • 0034697282 scopus 로고    scopus 로고
    • Transport of peptide-MHC class II complexes in developing dendritic cells
    • Turley, S. J. et al. Transport of peptide-MHC class II complexes in developing dendritic cells. Science 288, 522-527 (2000).
    • (2000) Science , vol.288 , pp. 522-527
    • Turley, S.J.1
  • 39
    • 0035838984 scopus 로고    scopus 로고
    • Dendritic cells: Specialized and regulated antigen processing machines
    • Mellman, I. & Steinman, R. M. Dendritic cells: specialized and regulated antigen processing machines. Cell 106, 255-258 (2001).
    • (2001) Cell , vol.106 , pp. 255-258
    • Mellman, I.1    Steinman, R.M.2
  • 41
    • 0030060293 scopus 로고    scopus 로고
    • Characterization of GMP-17, a granule membrane protein that moves to the plasma membrane of natural killer cells following target cell recognition
    • Medley, Q. G. et al. Characterization of GMP-17, a granule membrane protein that moves to the plasma membrane of natural killer cells following target cell recognition. Proc. Natl Acad. Sci. USA 93, 685-689 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 685-689
    • Medley, Q.G.1
  • 42
    • 0034327809 scopus 로고    scopus 로고
    • + T cells
    • + T cells. J. Immunol. 165, 5062-5068 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 5062-5068
    • Iida, T.1
  • 43
    • 0030816038 scopus 로고    scopus 로고
    • The trans-Golgi network: A late secretory sorting station
    • Traub, L. M. & Kornfeld, S. The trans-Golgi network: a late secretory sorting station. Curr. Opin. Cell Biol. 9, 527-533 (1997).
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 527-533
    • Traub, L.M.1    Kornfeld, S.2
  • 44
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors
    • Kornfeld, S. Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors. Annu. Rev. Biochem. 61, 307-330 (1992).
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 45
    • 0018903866 scopus 로고
    • Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight
    • Hasilik, A. & Neufeld, E. F. Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight. J. Biol. Chem. 255, 4937-4945 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 4937-4945
    • Hasilik, A.1    Neufeld, E.F.2
  • 46
    • 0018821796 scopus 로고
    • Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues
    • Hasilik, A. & Neufeld, E. F. Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues. J. Biol. Chem. 255, 4946-4950 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 4946-4950
    • Hasilik, A.1    Neufeld, E.F.2
  • 47
    • 0027443394 scopus 로고
    • Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts
    • Glickman, J. N. & Kornfeld, S. Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts. J. Cell Biol. 123, 99-108 (1993).
    • (1993) J. Cell Biol. , vol.123 , pp. 99-108
    • Glickman, J.N.1    Kornfeld, S.2
  • 48
    • 14844345988 scopus 로고
    • Expression of the Fas ligand in cells of T cell lineage
    • Suda, T. et al. Expression of the Fas ligand in cells of T cell lineage. J. Immunol. 154, 3806-3813 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 3806-3813
    • Suda, T.1
  • 49
    • 0032974475 scopus 로고    scopus 로고
    • Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells
    • Bossi, G. & Griffiths, G. M. Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells. Nature Med. 5, 90-96 (1999).
    • (1999) Nature Med. , vol.5 , pp. 90-96
    • Bossi, G.1    Griffiths, G.M.2
  • 50
    • 0034927311 scopus 로고    scopus 로고
    • Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail
    • Blott, E. J., Bossi, G., Clark, R., Zvelebil, M. & Griffiths, G. M. Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail. J. Cell Sci. 114, 2405-2416 (2001). The authors describe a new sorting motif - a proline-rich domain -which is recognized only in cells with secretory lysosomes.
    • (2001) J. Cell Sci. , vol.114 , pp. 2405-2416
    • Blott, E.J.1    Bossi, G.2    Clark, R.3    Zvelebil, M.4    Griffiths, G.M.5
  • 52
    • 0033815395 scopus 로고    scopus 로고
    • The tyrosinase gene and oculocutaneous albinism type 1 (OCA1): A model for understanding the molecular biology of melanin formation
    • Oetting, W, S. The tyrosinase gene and oculocutaneous albinism type 1 (OCA1): a model for understanding the molecular biology of melanin formation. Pigment Cell Res. 13, 320-325 (2000).
    • (2000) Pigment Cell Res. , vol.13 , pp. 320-325
    • Oetting, W.S.1
  • 53
    • 0029122868 scopus 로고
    • Melanocyte differentiation marker gp75, the brown locus protein, can be regulated independently of tyrosinase and pigmentation
    • Vijayasaradhi, S., Doskoch, P. M., Wolchok, J. & Houghton, A. N. Melanocyte differentiation marker gp75, the brown locus protein, can be regulated independently of tyrosinase and pigmentation. J. Invest. Dermatol. 105,113-119 (1995).
    • (1995) J. Invest. Dermatol. , vol.105 , pp. 113-119
    • Vijayasaradhi, S.1    Doskoch, P.M.2    Wolchok, J.3    Houghton, A.N.4
  • 54
    • 0039109678 scopus 로고    scopus 로고
    • Adi-leucine-based motif in the cytoplasmic tail of LIMP-JJ and tyrosinase mediates selective binding of AP-3
    • Honing, S., Sandoval, I. V. & von Figura, K. Adi-leucine-based motif in the cytoplasmic tail of LIMP-JJ and tyrosinase mediates selective binding of AP-3. EMBO J. 17, 1304-1314 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1304-1314
    • Honing, S.1    Sandoval, I.V.2    Von Figura, K.3
  • 55
    • 0034046801 scopus 로고    scopus 로고
    • Sorting and targeting of melanosomal membrane proteins: Signals, pathways, and mechanisms
    • Setaluri, V. Sorting and targeting of melanosomal membrane proteins: signals, pathways, and mechanisms. Pigment Cell Res. 13, 128-134 (2000).
    • (2000) Pigment Cell Res. , vol.13 , pp. 128-134
    • Setaluri, V.1
  • 56
    • 0035929655 scopus 로고    scopus 로고
    • PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1)
    • Liu, T. F., Kandala, G. & Setaluri, V. PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1). J. Biol. Chem. 276, 35768-35777 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 35768-35777
    • Liu, T.F.1    Kandala, G.2    Setaluri, V.3
  • 57
    • 0035654722 scopus 로고    scopus 로고
    • Role of calcium influx in cytotoxic T lymphocyte lytic granule exocytosis during target cell killing
    • Lyubchenko, T. A., Wurth, G. A. & Zweifach, A. Role of calcium influx in cytotoxic T lymphocyte lytic granule exocytosis during target cell killing. Immunity 15, 847-859 (2001).
    • (2001) Immunity , vol.15 , pp. 847-859
    • Lyubchenko, T.A.1    Wurth, G.A.2    Zweifach, A.3
  • 58
    • 0027457958 scopus 로고
    • Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro
    • Burkhardt, J. K., McIlvain, J. M. Jr, Sheetz, M. P. & Argon, Y. Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro. J. Cell Sci. 104, 151-162 (1993).
    • (1993) J. Cell Sci. , vol.104 , pp. 151-162
    • Burkhardt, J.K.1    McIlvain J.M., Jr.2    Sheetz, M.P.3    Argon, Y.4
  • 59
    • 0028942256 scopus 로고
    • Actin- and microtubule-dependent organelle motors: Interrelationships between the two motility systems
    • Langford, G. M. Actin- and microtubule-dependent organelle motors: interrelationships between the two motility systems. Curr. Opin. Cell Biol. 7, 82-88 (1995).
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 82-88
    • Langford, G.M.1
  • 60
    • 0030964893 scopus 로고    scopus 로고
    • Myosin V associates with melanosomes in mouse melanocytes: Evidence that myosin V is an organelle motor
    • Wu, X., Bowers, B., Wei, Q., Kocher, B. & Hammer, J. A. Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor. J. Cell Sci. 110, 847-859 (1997).
    • (1997) J. Cell Sci. , vol.110 , pp. 847-859
    • Wu, X.1    Bowers, B.2    Wei, Q.3    Kocher, B.4    Hammer, J.A.5
  • 61
    • 0032576622 scopus 로고    scopus 로고
    • Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo
    • Wu, X., Bowers, B., Rao, K., Wei, Q. & Hammer, J. A. Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo. J. Cell. Biol. 143, 1899-1918 (1998).
    • (1998) J. Cell. Biol. , vol.143 , pp. 1899-1918
    • Wu, X.1    Bowers, B.2    Rao, K.3    Wei, Q.4    Hammer, J.A.5
  • 62
    • 0034689023 scopus 로고    scopus 로고
    • 2+-dependent exocytosis of lysosomes in fibroblasts
    • 2+-dependent exocytosis of lysosomes in fibroblasts. J. Cell Biol. 148, 1141-1149 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 1141-1149
    • Martinez, I.1
  • 63
    • 0033577802 scopus 로고    scopus 로고
    • 2+-triggered exocytosis of lysosomes in mast cells
    • 2+-triggered exocytosis of lysosomes in mast cells. J. Exp. Med. 189, 1649-1658 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 1649-1658
    • Baram, D.1
  • 67
    • 0028912329 scopus 로고
    • Isolation of a murine cDNA clone encoding Rab19, a novel tissue-specific small GTPase
    • Lutcke, A. et al. Isolation of a murine cDNA clone encoding Rab19, a novel tissue-specific small GTPase. Gene 155, 257-260 (1995).
    • (1995) Gene , vol.155 , pp. 257-260
    • Lutcke, A.1
  • 68
    • 0034081439 scopus 로고    scopus 로고
    • Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast cells: Functional role of syntaxin 4 in exocytosis and identification of a vesicle-associated membrane protein 8-containing secretory compartment
    • Paumet, F. et al. Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast cells: functional role of syntaxin 4 in exocytosis and identification of a vesicle-associated membrane protein 8-containing secretory compartment. J. Immunol. 164, 5850-5857 (2000).
    • (2000) J. Immunol. , vol.164 , pp. 5850-5857
    • Paumet, F.1
  • 69
    • 0032555722 scopus 로고    scopus 로고
    • Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells
    • Guo, Z., Turner, C. & Castle, D, Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells. Cell 94, 537-548 (1998).
    • (1998) Cell , vol.94 , pp. 537-548
    • Guo, Z.1    Turner, C.2    Castle, D.3
  • 70
    • 0034728786 scopus 로고    scopus 로고
    • Rat basophilic leukemia cells express syntaxin-3 and VAMP-7 in granule membranes
    • Hibi, T., Hirashima, N. & Nakanishi, M. Rat basophilic leukemia cells express syntaxin-3 and VAMP-7 in granule membranes. Biochem. Biophys. Res. Commun. 271, 36-41 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 36-41
    • Hibi, T.1    Hirashima, N.2    Nakanishi, M.3
  • 71
    • 0028892237 scopus 로고
    • Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments
    • Brumell, J. H. et al. Subcellular distribution of docking/fusion proteins in neutrophils, secretory cells with multiple exocytic compartments. J. Immunol. 155, 5750-5759 (1995).
    • (1995) J. Immunol. , vol.155 , pp. 5750-5759
    • Brumell, J.H.1
  • 72
    • 0031571873 scopus 로고    scopus 로고
    • Involvement of the ras-like GTPase rab3d in RBL-2H3 mast cell exocytosis following stimulation via high affinity IgE receptors (Fc εRI)
    • Roa, M., Paumet, F., Le Mao, J., David, B. & Blank, U. Involvement of the ras-like GTPase rab3d in RBL-2H3 mast cell exocytosis following stimulation via high affinity IgE receptors (Fc εRI). J. Immunol. 159, 2815-2823 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 2815-2823
    • Roa, M.1    Paumet, F.2    Le Mao, J.3    David, B.4    Blank, U.5
  • 73
    • 0033810376 scopus 로고    scopus 로고
    • Small GTPase rab3A is associated with melanosomes in melanoma cells
    • Araki, K. et al. Small GTPase rab3A is associated with melanosomes in melanoma cells. Pigment Cell Res. 13, 332-336 (2000).
    • (2000) Pigment Cell Res. , vol.13 , pp. 332-336
    • Araki, K.1
  • 74
    • 0035109941 scopus 로고    scopus 로고
    • Rab3a and SNARE proteins: Potential regulators of melanosome movement
    • Scott, G. & Zhao, Q. Rab3a and SNARE proteins: potential regulators of melanosome movement. J. Invest. Dermatol. 116, 296-304 (2001).
    • (2001) J. Invest. Dermatol. , vol.116 , pp. 296-304
    • Scott, G.1    Zhao, Q.2
  • 75
    • 0032614337 scopus 로고    scopus 로고
    • Rab3D, a small GTPase, is localized on mast cell secretory granules and translocates to the plasma membrane upon exocytosis
    • Tuvim, M. J. et al. Rab3D, a small GTPase, is localized on mast cell secretory granules and translocates to the plasma membrane upon exocytosis. Am. J. Respir. Cell Mol. Biol. 20, 79-89 (1999).
    • (1999) Am. J. Respir. Cell Mol. Biol. , vol.20 , pp. 79-89
    • Tuvim, M.J.1
  • 76
    • 0026067472 scopus 로고
    • A small GTP-binding protein dissociates from synaptic vesicles during exocytosis
    • Fischer von Mollard, G., Sudhof, T. C. & Jahn, R. A small GTP-binding protein dissociates from synaptic vesicles during exocytosis. Nature 349, 79-81 (1991).
    • (1991) Nature , vol.349 , pp. 79-81
    • Fischer von Mollard, G.1    Sudhof, T.C.2    Jahn, R.3
  • 77
    • 0029016988 scopus 로고
    • Diffuse vesicular distribution of Rab3D in the polarized neuroendocrine cell line AtT-20
    • Martelli, A. M., Bareggi, R., Baldini, G., Scherer, P. E. & Lodish, H. F. Diffuse vesicular distribution of Rab3D in the polarized neuroendocrine cell line AtT-20. FEBS Lett. 368, 271-275 (1995).
    • (1995) FEBS Lett. , vol.368 , pp. 271-275
    • Martelli, A.M.1    Bareggi, R.2    Baldini, G.3    Scherer, P.E.4    Lodish, H.F.5
  • 78
    • 0033581022 scopus 로고    scopus 로고
    • Comparison of the effects on secretion in chromatin and PC12 cells of Rab3 family members and mutants. Evidence that inhibitory effects are independent of direct interaction with Rabphilin3
    • Chung, S. H., Joberty, G., Gelino, E. A., Macera, I. G. & Holz, R. W. Comparison of the effects on secretion in chromatin and PC12 cells of Rab3 family members and mutants. Evidence that inhibitory effects are independent of direct interaction with Rabphilin3. J. Biol. Chem. 274,18113-18120 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 18113-18120
    • Chung, S.H.1    Joberty, G.2    Gelino, E.A.3    Macera, I.G.4    Holz, R.W.5
  • 79
    • 0034144433 scopus 로고    scopus 로고
    • Two genes are responsible Griscelli syndrome at the same 15q21 locus
    • Pastural, E. et al. Two genes are responsible Griscelli syndrome at the same 15q21 locus. Genomics 63, 299-306 (2000). This paper details a second mutation in MyoVa, the gene that is defective in patients with Griscelli's syndrome.
    • (2000) Genomics , vol.63 , pp. 299-306
    • Pastural, E.1
  • 80
    • 0035911150 scopus 로고    scopus 로고
    • Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice
    • Haddad, E. K., Wu, X., Hammer, J. A. & Henkart, P. A. Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice. J. Cell Biol. 152, 835-842 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 835-842
    • Haddad, E.K.1    Wu, X.2    Hammer, J.A.3    Henkart, P.A.4
  • 81
    • 0035911160 scopus 로고    scopus 로고
    • Rab27a is required for regulated secretion in cytotoxic T lymphocytes
    • Stinchcombe, J. C. et al. Rab27a is required for regulated secretion in cytotoxic T lymphocytes. J. Cell Biol. 152, 825-834 (2001). References 80 and 81 show that cytotoxic granules in CTLs from ashen mice are able to polarize at the site of contact with the target cell, but are unable to dock at the plasma membrane and hence secrete their contents. Reference 81 also describes the phenotype of granules from gunmetal mice, which are partially able to polarize and secrete. These results point to a crucial role for Rab27a in a late stage of granule secretion.
    • (2001) J. Cell Biol. , vol.152 , pp. 825-834
    • Stinchcombe, J.C.1
  • 82
    • 12944255844 scopus 로고    scopus 로고
    • A mutation in Rab27a causes the vesicle transport defects observed in ashen mice
    • Wilson, S.M. et al. A mutation in Rab27a causes the vesicle transport defects observed in ashen mice. Proc. Natl Acad. Sci. USA 97, 7933-7938 (2000). The first paper to identify Rab27a as the defective protein that is responsible for the ashen mouse phenotype.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7933-7938
    • Wilson, S.M.1
  • 83
    • 0034234258 scopus 로고    scopus 로고
    • Serological cloning of a melanocyte rab guanosine 5′ -triphosphate-binding protein and a chromosome condensation protein from a melanoma complementary DNA library
    • Jager, D. et al. Serological cloning of a melanocyte rab guanosine 5′-triphosphate-binding protein and a chromosome condensation protein from a melanoma complementary DNA library Cancer Res. 60, 3584-3591 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 3584-3591
    • Jager, D.1
  • 84
    • 12944252970 scopus 로고    scopus 로고
    • Rab geranylgeranyl transferase α-mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis
    • Detter, J. C. et al. Rab geranylgeranyl transferase α-mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis. Proc. Natl Acad. Sci. USA 97, 4144-4149 (2000). The first paper to identify RGGT as the protein that is defective in the gunmetal mouse.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4144-4149
    • Detter, J.C.1
  • 85
    • 0035010659 scopus 로고    scopus 로고
    • Normal and abnormal secretion by haemopoietic cells
    • Stinchcombe, J. C. & Griffiths, G. M. Normal and abnormal secretion by haemopoietic cells. Immunology 103, 10-16 (2001).
    • (2001) Immunology , vol.103 , pp. 10-16
    • Stinchcombe, J.C.1    Griffiths, G.M.2
  • 86
    • 0035975946 scopus 로고    scopus 로고
    • The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors
    • Jordens, I. et al. The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors. Curr. Biol. 11, 1680-1685 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1680-1685
    • Jordens, I.1
  • 87
    • 0035964395 scopus 로고    scopus 로고
    • Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice
    • Matesic, L. E. et al. Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice. Proc. Natl Acad. Sci. USA 98, 10238-10243 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10238-10243
    • Matesic, L.E.1
  • 88
    • 0033854275 scopus 로고    scopus 로고
    • Identification of a novel myosin-Va mutation in an ataxic mutant rat, dilute-opisthotonus
    • Futaki, S. et al. Identification of a novel myosin-Va mutation in an ataxic mutant rat, dilute-opisthotonus. Mamm. Genome 11, 649-655 (2000).
    • (2000) Mamm. Genome , vol.11 , pp. 649-655
    • Futaki, S.1
  • 90
    • 0035911157 scopus 로고    scopus 로고
    • Rab27a regulates the peripheral distribution of melanosomes in melanocytes
    • Hume, A. N. et al. Rab27a regulates the peripheral distribution of melanosomes in melanocytes. J. Cell Biol. 152, 795-808 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 795-808
    • Hume, A.N.1
  • 91
    • 0030293556 scopus 로고    scopus 로고
    • Identification and mutation analysis of the complete gene for Chediak-Higashi syndrome
    • Nagle, D. L. et al. Identification and mutation analysis of the complete gene for Chediak-Higashi syndrome. Nature Genet. 14, 307-311 (1996).
    • (1996) Nature Genet. , vol.14 , pp. 307-311
    • Nagle, D.L.1
  • 92
    • 8544220356 scopus 로고    scopus 로고
    • Identification of mutations in two major mRNA isoforms of the Chediak-Higashi syndrome gene in human and mouse
    • Barbosa, M. D. et al. Identification of mutations in two major mRNA isoforms of the Chediak-Higashi syndrome gene in human and mouse. Hum. Mol. Genet. 6, 1091-1098 (1997).
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1091-1098
    • Barbosa, M.D.1
  • 93
    • 0034330540 scopus 로고    scopus 로고
    • Analysis of the lysosomal storage disease Chediak-Higashi syndrome
    • McVey Ward, D., Griffiths, G. M., Stinchcombe, J. C. & Kaplan, J. Analysis of the lysosomal storage disease Chediak-Higashi syndrome. Traffic 1, 816-822 (2000).
    • (2000) Traffic , vol.1 , pp. 816-822
    • McVey Ward, D.1    Griffiths, G.M.2    Stinchcombe, J.C.3    Kaplan, J.4
  • 94
    • 0032044504 scopus 로고    scopus 로고
    • Mouse models of Hermansky-Pudlak syndrome: A review
    • Swank, R. T, Novak, E. K., McGarry, M. R. Rusiniak, M. E. & Feng, L. Mouse models of Hermansky-Pudlak syndrome: a review. Pigment Cell Res. 11, 60-80 (1998). A nice overview of the many mouse models of HPS that highlights the multigenic nature of the disease.
    • (1998) Pigment Cell Res. , vol.11 , pp. 60-80
    • Swank, R.T.1    Novak, E.K.2    McGarry, M.R.3    Rusiniak, M.E.4    Feng, L.5
  • 95
    • 0022201056 scopus 로고
    • Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes
    • Pan, B. T., Teng, K., Wu, C., Adam, M. & Johnstone, R. M. Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes. J. Cell Biol. 101, 942-948 (1985).
    • (1985) J. Cell Biol. , vol.101 , pp. 942-948
    • Pan, B.T.1    Teng, K.2    Wu, C.3    Adam, M.4    Johnstone, R.M.5
  • 96
    • 0032493658 scopus 로고    scopus 로고
    • Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes
    • Escola, J. M. et al. Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes. J. Biol. Chem. 273, 20121-20127 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 20121-20127
    • Escola, J.M.1
  • 97
    • 0033485648 scopus 로고    scopus 로고
    • Activated platelets release two types of membrane vesicles: Microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and α-granules
    • Heijnen, H. F., Schiel, A. E., Fijnheer, R., Geuze, H. J. & Sixma, J. J. Activated platelets release two types of membrane vesicles: microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and α-granules. Blood 94, 3791-3799 (1999).
    • (1999) Blood , vol.94 , pp. 3791-3799
    • Heijnen, H.F.1    Schiel, A.E.2    Fijnheer, R.3    Geuze, H.J.4    Sixma, J.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.