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Volumn 17, Issue 1, 2005, Pages 87-94

CTL secretory lysosomes: Biogenesis and secretion of a harmful organelle

Author keywords

Cytotoxic T cell; Lytic proteins; Secretory lysosomes

Indexed keywords

2 AMINO 3 PHOSPHONOPROPIONIC ACID; ADAPTOR PROTEIN; AMINO ACID; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; RAB PROTEIN;

EID: 9644275363     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.smim.2004.09.007     Document Type: Article
Times cited : (102)

References (79)
  • 1
    • 0025597939 scopus 로고
    • The lytic granules of natural killer cells are dual-function organelles combining secretory and pre-lysosomal compartments
    • J.K. Burkhardt, S. Hester, C.K. Lapham, and Y. Argon The lytic granules of natural killer cells are dual-function organelles combining secretory and pre-lysosomal compartments J Cell Biol 111 1990 2327 2340
    • (1990) J Cell Biol , vol.111 , pp. 2327-2340
    • Burkhardt, J.K.1    Hester, S.2    Lapham, C.K.3    Argon, Y.4
  • 2
    • 0025905925 scopus 로고
    • Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes
    • P.J. Peters Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes J Exp Med 173 1991 1099 1109
    • (1991) J Exp Med , vol.173 , pp. 1099-1109
    • Peters, P.J.1
  • 4
    • 0034330457 scopus 로고    scopus 로고
    • Traffic jam: A compendium of human diseases that affect intracellular transport processes
    • M. Aridor, and L.A. Hannan Traffic jam: a compendium of human diseases that affect intracellular transport processes Traffic 1 2000 836 851
    • (2000) Traffic , vol.1 , pp. 836-851
    • Aridor, M.1    Hannan, L.A.2
  • 5
    • 0036843129 scopus 로고    scopus 로고
    • Traffic jams II: An update of diseases of intracellular transport
    • M. Aridor, and L.A. Hannan Traffic jams II: an update of diseases of intracellular transport Traffic 3 2002 781 790
    • (2002) Traffic , vol.3 , pp. 781-790
    • Aridor, M.1    Hannan, L.A.2
  • 6
    • 0034189092 scopus 로고    scopus 로고
    • Secretory lysosome biogenesis in cytotoxic T lymphocytes from normal and Chediak Higashi syndrome patients
    • J.C. Stinchcombe, L.J. Page, and G.M. Griffiths Secretory lysosome biogenesis in cytotoxic T lymphocytes from normal and Chediak Higashi syndrome patients Traffic 1 2000 435 444
    • (2000) Traffic , vol.1 , pp. 435-444
    • Stinchcombe, J.C.1    Page, L.J.2    Griffiths, G.M.3
  • 7
    • 0024464780 scopus 로고
    • Two proteins targeted to the same lytic granule compartment undergo very different posttranslational processing
    • J.K. Burkhardt, S. Hester, and Y. Argon Two proteins targeted to the same lytic granule compartment undergo very different posttranslational processing Proc Natl Acad Sci USA 86 1989 7128 7132
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7128-7132
    • Burkhardt, J.K.1    Hester, S.2    Argon, Y.3
  • 8
    • 0025215719 scopus 로고
    • Morphologic analysis of human lymphokine-activated killer (LAK) cells
    • P. Groscurth Morphologic analysis of human lymphokine-activated killer (LAK) cells Int J Cancer 45 1990 694 704
    • (1990) Int J Cancer , vol.45 , pp. 694-704
    • Groscurth, P.1
  • 9
    • 0027452741 scopus 로고
    • Granzymes a and B are targeted to the lytic granules of lymphocytes by the mannose-6-phosphate receptor
    • G.M. Griffiths, and S. Isaaz Granzymes A and B are targeted to the lytic granules of lymphocytes by the mannose-6-phosphate receptor J Cell Biol 120 1993 885 896
    • (1993) J Cell Biol , vol.120 , pp. 885-896
    • Griffiths, G.M.1    Isaaz, S.2
  • 10
    • 0242539818 scopus 로고    scopus 로고
    • Adaptor protein 3-dependent microtubule-mediated movement of lytic granules to the immunological synapse
    • R.H. Clark Adaptor protein 3-dependent microtubule-mediated movement of lytic granules to the immunological synapse Nat Immunol 4 2003 1111 1120
    • (2003) Nat Immunol , vol.4 , pp. 1111-1120
    • Clark, R.H.1
  • 12
    • 0023839303 scopus 로고
    • The mannose 6-phosphate receptor and the biogenesis of lysosomes
    • G. Griffiths, B. Hoflack, K. Simons, I. Mellman, and S. Kornfeld The mannose 6-phosphate receptor and the biogenesis of lysosomes Cell 52 1988 329 341
    • (1988) Cell , vol.52 , pp. 329-341
    • Griffiths, G.1    Hoflack, B.2    Simons, K.3    Mellman, I.4    Kornfeld, S.5
  • 13
    • 0036196266 scopus 로고    scopus 로고
    • Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes
    • B.A. Rous Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes Mol Biol Cell 13 2002 1071 1082
    • (2002) Mol Biol Cell , vol.13 , pp. 1071-1082
    • Rous, B.A.1
  • 15
    • 0034327809 scopus 로고    scopus 로고
    • Regulation of cell surface expression of CTLA-4 by secretion of CTLA-4-containing lysosomes upon activation of CD4+ T cells
    • T. Iida Regulation of cell surface expression of CTLA-4 by secretion of CTLA-4-containing lysosomes upon activation of CD4+ T cells J Immunol 165 2000 5062 5068
    • (2000) J Immunol , vol.165 , pp. 5062-5068
    • Iida, T.1
  • 16
    • 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
    • Q.G. Medley 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 1996 685 689
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 685-689
    • Medley, Q.G.1
  • 17
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • J. Gruenberg, and H. Stenmark The biogenesis of multivesicular endosomes Nat Rev Mol Cell Biol 5 2004 317 323
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 18
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of GGA3 with the ubiquitin sorting machinery
    • R. Puertollano, and J.S. Bonifacino Interactions of GGA3 with the ubiquitin sorting machinery Nat Cell Biol 6 2004 244 251
    • (2004) Nat Cell Biol , vol.6 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 19
    • 11144225699 scopus 로고    scopus 로고
    • GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network
    • P.M. Scott GGA proteins bind ubiquitin to facilitate sorting at the trans-Golgi network Nat Cell Biol 6 2004 252 259
    • (2004) Nat Cell Biol , vol.6 , pp. 252-259
    • Scott, P.M.1
  • 20
    • 0028927607 scopus 로고
    • The Fas death factor
    • S. Nagata, and P. Golstein The Fas death factor Science 267 1995 1449 1456
    • (1995) Science , vol.267 , pp. 1449-1456
    • Nagata, S.1    Golstein, P.2
  • 21
    • 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
    • G. Bossi, and G.M. Griffiths Degranulation plays an essential part in regulating cell surface expression of Fas ligand in T cells and natural killer cells Nat Med 5 1999 90 96
    • (1999) Nat Med , vol.5 , pp. 90-96
    • Bossi, G.1    Griffiths, G.M.2
  • 23
    • 0034927311 scopus 로고    scopus 로고
    • Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail
    • E.J. Blott, G. Bossi, R. Clark, M. Zvelebil, and G.M. Griffiths Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail J Cell Sci 114 2001 2405 2416
    • (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
  • 24
    • 0031464539 scopus 로고    scopus 로고
    • Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid-binding C2 domain
    • R. Uellner Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid-binding C2 domain EMBO J 16 1997 7287 7296
    • (1997) EMBO J , vol.16 , pp. 7287-7296
    • Uellner, R.1
  • 25
    • 0025672874 scopus 로고
    • Interaction of chondroitin sulfate with perforin and granzymes of cytolytic T-cells is dependent on pH
    • D. Masson, P.J. Peters, H.J. Geuze, J. Borst, and J. Tschopp Interaction of chondroitin sulfate with perforin and granzymes of cytolytic T-cells is dependent on pH Biochemistry 29 1990 11229 11235
    • (1990) Biochemistry , vol.29 , pp. 11229-11235
    • Masson, D.1    Peters, P.J.2    Geuze, H.J.3    Borst, J.4    Tschopp, J.5
  • 26
    • 0024794498 scopus 로고
    • Structure of perforin and its role in cytolysis
    • E.R. Podack, and H. Hengartner Structure of perforin and its role in cytolysis Year Immunol 6 1989 245 261
    • (1989) Year Immunol , vol.6 , pp. 245-261
    • Podack, E.R.1    Hengartner, H.2
  • 28
    • 0036195424 scopus 로고    scopus 로고
    • Cytotoxic cell granule-mediated apoptosis: Perforin delivers granzyme B-serglycin complexes into target cells without plasma membrane pore formation
    • S.S. Metkar Cytotoxic cell granule-mediated apoptosis: perforin delivers granzyme B-serglycin complexes into target cells without plasma membrane pore formation Immunity 16 2002 417 428
    • (2002) Immunity , vol.16 , pp. 417-428
    • Metkar, S.S.1
  • 29
    • 2442427374 scopus 로고    scopus 로고
    • Granzyme-mediated cytotoxicity does not involve the mannose 6-phosphate receptors on target cells
    • R. Dressel Granzyme-mediated cytotoxicity does not involve the mannose 6-phosphate receptors on target cells J Biol Chem 279 2004 20200 20210
    • (2004) J Biol Chem , vol.279 , pp. 20200-20210
    • Dressel, R.1
  • 30
    • 0030723209 scopus 로고    scopus 로고
    • In vitro- and ex vivo-derived cytolytic leukocytes from granzyme a × B double knockout mice are defective in granule-mediated apoptosis but not lysis of target cells
    • M.M. Simon In vitro- and ex vivo-derived cytolytic leukocytes from granzyme A × B double knockout mice are defective in granule-mediated apoptosis but not lysis of target cells J Exp Med 186 1997 1781 1786
    • (1997) J Exp Med , vol.186 , pp. 1781-1786
    • Simon, M.M.1
  • 31
    • 0028967988 scopus 로고    scopus 로고
    • Synergistic roles of granzymes a and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin
    • H. Nakajima, H.L. Park, and P.A. Henkart Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin J Exp Med 181 1998 1037 1046
    • (1998) J Exp Med , vol.181 , pp. 1037-1046
    • Nakajima, H.1    Park, H.L.2    Henkart, P.A.3
  • 32
    • 0032516917 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte-assisted suicide: Caspase 3 activation is primarily the result of the direct action of granzyme B
    • E.A. Atkinson Cytotoxic T lymphocyte-assisted suicide Caspase 3 activation is primarily the result of the direct action of granzyme B J Biol Chem 273 1998 21261 21266
    • (1998) J Biol Chem , vol.273 , pp. 21261-21266
    • Atkinson, E.A.1
  • 33
    • 0034107096 scopus 로고    scopus 로고
    • Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving Bid
    • M. Barry Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving Bid Mol Cell Biol 20 2000 3781 3794
    • (2000) Mol Cell Biol , vol.20 , pp. 3781-3794
    • Barry, M.1
  • 34
    • 0033136315 scopus 로고    scopus 로고
    • Granzyme a initiates an alternative pathway for granule-mediated apoptosis
    • S. Shresta, T.A. Graubert, D.A. Thomas, S.Z. Raptis, and T.J. Ley Granzyme A initiates an alternative pathway for granule-mediated apoptosis Immunity 10 1999 595 605
    • (1999) Immunity , vol.10 , pp. 595-605
    • Shresta, S.1    Graubert, T.A.2    Thomas, D.A.3    Raptis, S.Z.4    Ley, T.J.5
  • 35
    • 0033137079 scopus 로고    scopus 로고
    • Granzyme a loading induces rapid cytolysis and a novel form of DNA damage independently of caspase activation
    • P.J. Beresford, Z. Xia, A.H. Greenberg, and J. Lieberman Granzyme A loading induces rapid cytolysis and a novel form of DNA damage independently of caspase activation Immunity 10 1999 585 594
    • (1999) Immunity , vol.10 , pp. 585-594
    • Beresford, P.J.1    Xia, Z.2    Greenberg, A.H.3    Lieberman, J.4
  • 36
    • 0032475823 scopus 로고    scopus 로고
    • An antimicrobial activity of cytolytic T cells mediated by granulysin
    • S. Stenger An antimicrobial activity of cytolytic T cells mediated by granulysin Science 282 1998 121 125
    • (1998) Science , vol.282 , pp. 121-125
    • Stenger, S.1
  • 37
    • 0034641898 scopus 로고    scopus 로고
    • CD95's deadly mission in the immune system
    • P.H. Krammer CD95's deadly mission in the immune system Nature 407 2000 789 795
    • (2000) Nature , vol.407 , pp. 789-795
    • Krammer, P.H.1
  • 38
    • 0028935791 scopus 로고
    • Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration
    • T.A Springer Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration Annu Rev Physiol 57 1995 827 872
    • (1995) Annu Rev Physiol , vol.57 , pp. 827-872
    • Springer, T.A.1
  • 39
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • C.R. Monks, B.A. Freiberg, H. Kupfer, N. Sciaky, and A. Kupfer Three-dimensional segregation of supramolecular activation clusters in T cells Nature 395 1998 82 86
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 40
    • 0035655587 scopus 로고    scopus 로고
    • The immunological synapse of CTL contains a secretory domain and membrane bridges
    • J.C. Stinchcombe, G. Bossi, S. Booth, and G.M. Griffiths The immunological synapse of CTL contains a secretory domain and membrane bridges Immunity 15 2001 751 761
    • (2001) Immunity , vol.15 , pp. 751-761
    • Stinchcombe, J.C.1    Bossi, G.2    Booth, S.3    Griffiths, G.M.4
  • 41
    • 0035652354 scopus 로고    scopus 로고
    • Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin
    • J. Delon, K. Kaibuchi, and R.N. Germain Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin Immunity 15 2001 691 701
    • (2001) Immunity , vol.15 , pp. 691-701
    • Delon, J.1    Kaibuchi, K.2    Germain, R.N.3
  • 42
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T cell activation
    • A. Grakoui The immunological synapse: a molecular machine controlling T cell activation Science 285 1999 221 227
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1
  • 43
    • 2442651482 scopus 로고    scopus 로고
    • T cell killing does not require the formation of a stable mature immunological synapse
    • M.A. Purbhoo, D.J. Irvine, J.B. Huppa, and M.M. Davis T cell killing does not require the formation of a stable mature immunological synapse Nat Immunol 5 2004 524 530
    • (2004) Nat Immunol , vol.5 , pp. 524-530
    • Purbhoo, M.A.1    Irvine, D.J.2    Huppa, J.B.3    Davis, M.M.4
  • 44
    • 0018082910 scopus 로고
    • Ultrastructural alteration of cytolytic T lymphocytes following their interaction with target cells: I. Hypertrophy and change of orientation of the Golgi apparatus
    • S.N. Bykovskaja, A.N. Rytenko, M.O. Rauschenbach, and A.F. Bykovsky Ultrastructural alteration of cytolytic T lymphocytes following their interaction with target cells I. Hypertrophy and change of orientation of the Golgi apparatus Cell Immunol 40 1978 164 174
    • (1978) Cell Immunol , vol.40 , pp. 164-174
    • Bykovskaja, S.N.1    Rytenko, A.N.2    Rauschenbach, M.O.3    Bykovsky, A.F.4
  • 45
    • 0020309431 scopus 로고
    • Electron microscopic study of natural killer cell-tumor cell conjugates
    • T. Frey, H.R. Petty, and H.M. McConnell Electron microscopic study of natural killer cell-tumor cell conjugates Proc Natl Acad Sci USA 79 1982 5317 5321
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5317-5321
    • Frey, T.1    Petty, H.R.2    McConnell, H.M.3
  • 46
    • 0024419921 scopus 로고
    • Molecules relevant for T cell-target cell interaction are present in cytolytic granules of human T lymphocytes
    • P.J. Peters Molecules relevant for T cell-target cell interaction are present in cytolytic granules of human T lymphocytes Eur J Immunol 19 1989 1469 1475
    • (1989) Eur J Immunol , vol.19 , pp. 1469-1475
    • Peters, P.J.1
  • 47
    • 0035911160 scopus 로고    scopus 로고
    • Rab27a is required for regulated secretion in cytotoxic T lymphocytes
    • J.C. Stinchcombe Rab27a is required for regulated secretion in cytotoxic T lymphocytes J Cell Biol 152 2001 825 834
    • (2001) J Cell Biol , vol.152 , pp. 825-834
    • Stinchcombe, J.C.1
  • 48
    • 12944252970 scopus 로고    scopus 로고
    • Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis
    • J.C. Detter Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis Proc Natl Acad Sci USA 97 2000 4144 4149
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4144-4149
    • Detter, J.C.1
  • 49
    • 0027174293 scopus 로고
    • Inherited abnormalities in platelet organelles and platelet formation and associated altered expression of low molecular weight guanosine triphosphate-binding proteins in the mouse pigment mutant gunmetal
    • R.T. Swank Inherited abnormalities in platelet organelles and platelet formation and associated altered expression of low molecular weight guanosine triphosphate-binding proteins in the mouse pigment mutant gunmetal Blood 81 1993 2626 2635
    • (1993) Blood , vol.81 , pp. 2626-2635
    • Swank, R.T.1
  • 50
    • 0035865135 scopus 로고    scopus 로고
    • Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes
    • G. Cantalupo, P. Alifano, V. Roberti, C.B. Bruni, and C. Bucci Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes EMBO J 20 2001 683 693
    • (2001) EMBO J , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 51
    • 0035975946 scopus 로고    scopus 로고
    • The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors
    • I. Jordens The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors Curr Biol 11 2001 1680 1685
    • (2001) Curr Biol , vol.11 , pp. 1680-1685
    • Jordens, I.1
  • 52
    • 0036915823 scopus 로고    scopus 로고
    • Interorganellar regulation of lysosome positioning by the Golgi apparatus through Rab34 interaction with Rab-interacting lysosomal protein
    • T. Wang, and W. Hong Interorganellar regulation of lysosome positioning by the Golgi apparatus through Rab34 interaction with Rab-interacting lysosomal protein Mol Biol Cell 13 2002 4317 4332
    • (2002) Mol Biol Cell , vol.13 , pp. 4317-4332
    • Wang, T.1    Hong, W.2
  • 53
    • 0033936009 scopus 로고    scopus 로고
    • Connecting vesicle transport to the cytoskeleton
    • A. Kamal, and L.S. Goldstein Connecting vesicle transport to the cytoskeleton Curr Opin Cell Biol 12 2000 503 508
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 503-508
    • Kamal, A.1    Goldstein, L.S.2
  • 54
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • S.R. Gill Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein J Cell Biol 115 1991 1639 1650
    • (1991) J Cell Biol , vol.115 , pp. 1639-1650
    • Gill, S.R.1
  • 55
    • 0035965256 scopus 로고    scopus 로고
    • Beta III spectrin binds to the Arp1 subunit of dynactin
    • E.A. Holleran beta III spectrin binds to the Arp1 subunit of dynactin J Biol Chem 276 2001 36598 36605
    • (2001) J Biol Chem , vol.276 , pp. 36598-36605
    • Holleran, E.A.1
  • 56
    • 0035911157 scopus 로고    scopus 로고
    • Rab27a regulates the peripheral distribution of melanosomes in melanocytes
    • A.N. Hume Rab27a regulates the peripheral distribution of melanosomes in melanocytes J Cell Biol 152 2001 795 808
    • (2001) J Cell Biol , vol.152 , pp. 795-808
    • Hume, A.N.1
  • 57
    • 0035073174 scopus 로고    scopus 로고
    • Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle
    • X. Wu Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle J Cell Sci 114 2001 1091 1100
    • (2001) J Cell Sci , vol.114 , pp. 1091-1100
    • Wu, X.1
  • 58
    • 0036099629 scopus 로고    scopus 로고
    • The leaden gene product is required with Rab27a to recruit myosin Va to melanosomes in melanocytes
    • A.N. Hume The leaden gene product is required with Rab27a to recruit myosin Va to melanosomes in melanocytes Traffic 3 2002 193 202
    • (2002) Traffic , vol.3 , pp. 193-202
    • Hume, A.N.1
  • 59
    • 0035911150 scopus 로고    scopus 로고
    • Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice
    • E.K. Haddad, X. Wu, J.A. Hammer III, and P.A. Henkart Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice J Cell Biol 152 2001 835 842
    • (2001) J Cell Biol , vol.152 , pp. 835-842
    • Haddad, E.K.1    Wu, X.2    Hammer III, J.A.3    Henkart, P.A.4
  • 60
    • 0037088641 scopus 로고    scopus 로고
    • The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain
    • T.S. Kuroda, M. Fukuda, H. Ariga, and K. Mikoshiba The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain J Biol Chem 277 2002 9212 9218
    • (2002) J Biol Chem , vol.277 , pp. 9212-9218
    • Kuroda, T.S.1    Fukuda, M.2    Ariga, H.3    Mikoshiba, K.4
  • 61
    • 0036298197 scopus 로고    scopus 로고
    • Synaptotagmin-like protein 5: A novel Rab27A effector with C-terminal tandem C2 domains
    • T.S. Kuroda, M. Fukuda, H. Ariga, and K. Mikoshiba Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal tandem C2 domains Biochem Biophys Res Commun 293 2002 899 906
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 899-906
    • Kuroda, T.S.1    Fukuda, M.2    Ariga, H.3    Mikoshiba, K.4
  • 62
    • 10744224641 scopus 로고    scopus 로고
    • Munc13-4 is essential for cytolytic granules fusion and is mutated in a form of familial hemophagocytic lymphohistiocytosis (FHL3)
    • J. Feldmann Munc13-4 is essential for cytolytic granules fusion and is mutated in a form of familial hemophagocytic lymphohistiocytosis (FHL3) Cell 115 2003 461 473
    • (2003) Cell , vol.115 , pp. 461-473
    • Feldmann, J.1
  • 63
    • 9644281151 scopus 로고    scopus 로고
    • Munc13-4 is a GTP-Rab27 binding protein regulating dense-core granule secretion in platelets
    • Shirakawa R, et al. Munc13-4 is a GTP-Rab27 binding protein regulating dense-core granule secretion in platelets. J Biol Chem, 2003.
    • (2003) J Biol Chem
    • Shirakawa, R.1
  • 64
    • 0034525617 scopus 로고    scopus 로고
    • Protein-protein interactions in intracellular membrane fusion
    • K.M. Misura, A.P. May, and W.I. Weis Protein-protein interactions in intracellular membrane fusion Curr Opin Struct Biol 10 2000 662 671
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 662-671
    • Misura, K.M.1    May, A.P.2    Weis, W.I.3
  • 66
    • 0034810799 scopus 로고    scopus 로고
    • A post-docking role for active zone protein Rim
    • S.P. Koushika A post-docking role for active zone protein Rim Nat Neurosci 4 2001 997 1005
    • (2001) Nat Neurosci , vol.4 , pp. 997-1005
    • Koushika, S.P.1
  • 67
    • 0035913332 scopus 로고    scopus 로고
    • An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming
    • J.E. Richmond, R.M. Weimer, and E.M. Jorgensen An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming Nature 412 2001 338 341
    • (2001) Nature , vol.412 , pp. 338-341
    • Richmond, J.E.1    Weimer, R.M.2    Jorgensen, E.M.3
  • 68
    • 0037439781 scopus 로고    scopus 로고
    • Evidence of a role for Munc18-2 and microtubules in mast cell granule exocytosis
    • S. Martin-Verdeaux Evidence of a role for Munc18-2 and microtubules in mast cell granule exocytosis J Cell Sci 116 2003 325 334
    • (2003) J Cell Sci , vol.116 , pp. 325-334
    • Martin-Verdeaux, S.1
  • 69
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • R. Jahn, and T.C. Sudhof Membrane fusion and exocytosis Annu Rev Biochem 68 1999 863 911
    • (1999) Annu Rev Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 70
    • 0034142239 scopus 로고    scopus 로고
    • Molecular mechanisms of platelet exocytosis: Role of SNAP-23 and syntaxin 2 in dense core granule release
    • D. Chen, A.M. Bernstein, P.P. Lemons, and S.W. Whiteheart Molecular mechanisms of platelet exocytosis: role of SNAP-23 and syntaxin 2 in dense core granule release Blood 95 2000 921 929
    • (2000) Blood , vol.95 , pp. 921-929
    • Chen, D.1    Bernstein, A.M.2    Lemons, P.P.3    Whiteheart, S.W.4
  • 71
    • 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
    • F. Paumet 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 2000 5850 5857
    • (2000) J Immunol , vol.164 , pp. 5850-5857
    • Paumet, F.1
  • 72
    • 0034307682 scopus 로고    scopus 로고
    • Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis
    • B. Martin-Martin, S.M. Nabokina, J. Blasi, P.A. Lazo, and F. Mollinedo Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis Blood 96 2000 2574 2583
    • (2000) Blood , vol.96 , pp. 2574-2583
    • Martin-Martin, B.1    Nabokina, S.M.2    Blasi, J.3    Lazo, P.A.4    Mollinedo, F.5
  • 73
    • 2442511061 scopus 로고    scopus 로고
    • Activation-induced polarized recycling targets T cell antigen receptors to the immunological synapse; Involvement of SNARE complexes
    • V. Das Activation-induced polarized recycling targets T cell antigen receptors to the immunological synapse; involvement of SNARE complexes Immunity 20 2004 577 588
    • (2004) Immunity , vol.20 , pp. 577-588
    • Das, V.1
  • 74
    • 0033520970 scopus 로고    scopus 로고
    • Perforin gene defects in familial hemophagocytic lymphohistiocytosis
    • S.E. Stepp Perforin gene defects in familial hemophagocytic lymphohistiocytosis Science 286 1999 1957 1959
    • (1999) Science , vol.286 , pp. 1957-1959
    • Stepp, S.E.1
  • 75
    • 0036277746 scopus 로고    scopus 로고
    • Functional consequences of perforin gene mutations in 22 patients with familial haemophagocytic lymphohistiocytosis
    • J. Feldmann Functional consequences of perforin gene mutations in 22 patients with familial haemophagocytic lymphohistiocytosis Br J Haematol 117 2002 965 972
    • (2002) Br J Haematol , vol.117 , pp. 965-972
    • Feldmann, J.1
  • 76
    • 0035479955 scopus 로고    scopus 로고
    • The role of cytotoxicity in lymphocyte homeostasis
    • G. de Saint Basile, and A. Fischer The role of cytotoxicity in lymphocyte homeostasis Curr Opin Immunol 13 2001 549 554
    • (2001) Curr Opin Immunol , vol.13 , pp. 549-554
    • De Saint Basile, G.1    Fischer, A.2
  • 77
    • 17144450359 scopus 로고    scopus 로고
    • Homeostatic regulation of CD8+ T cells by perforin
    • D. Kagi, B. Odermatt, and T.W. Mak Homeostatic regulation of CD8+ T cells by perforin Eur J Immunol 29 1999 3262 3272
    • (1999) Eur J Immunol , vol.29 , pp. 3262-3272
    • Kagi, D.1    Odermatt, B.2    Mak, T.W.3
  • 78
    • 0033615606 scopus 로고    scopus 로고
    • TCR-mediated internalization of peptide-MHC complexes acquired by T cells
    • J.F. Huang TCR-mediated internalization of peptide-MHC complexes acquired by T cells Science 286 1999 952 954
    • (1999) Science , vol.286 , pp. 952-954
    • Huang, J.F.1
  • 79
    • 0034599597 scopus 로고    scopus 로고
    • T cells can use either T cell receptor or CD28 receptors to absorb and internalize cell surface molecules derived from antigen-presenting cells
    • I. Hwang T cells can use either T cell receptor or CD28 receptors to absorb and internalize cell surface molecules derived from antigen-presenting cells J Exp Med 191 2000 1137 1148
    • (2000) J Exp Med , vol.191 , pp. 1137-1148
    • Hwang, I.1


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