메뉴 건너뛰기




Volumn 4, Issue 11, 2003, Pages 1111-1120

Adaptor protein 3-dependent microtubule-mediated movement of lytic granules to the immunological synapse

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CD63 ANTIGEN; GRANZYME A; PERFORIN; SECRETORY PROTEIN;

EID: 0242539818     PISSN: 15292908     EISSN: None     Source Type: Journal    
DOI: 10.1038/ni1000     Document Type: Article
Times cited : (207)

References (44)
  • 1
    • 0022362235 scopus 로고
    • The reorientation of the Golgi apparatus and the microtubule-organizing center in the cytotoxic effector cell is a prerequisite in the lysis of bound target cells
    • Kupfer, A., Dennert, G. & Singer, S.J. The reorientation of the Golgi apparatus and the microtubule-organizing center in the cytotoxic effector cell is a prerequisite in the lysis of bound target cells. J. Mol. Cell. Immunol. 2, 37-49 (1985).
    • (1985) J. Mol. Cell. Immunol. , vol.2 , pp. 37-49
    • Kupfer, A.1    Dennert, G.2    Singer, S.J.3
  • 2
    • 0036166541 scopus 로고    scopus 로고
    • Dynamic polarization of the microtubule cytoskeleton during CTL-mediated killing
    • Kuhn, J.R. & Poenie, M. Dynamic polarization of the microtubule cytoskeleton during CTL-mediated killing. Immunity 16, 111-121 (2002).
    • (2002) Immunity , vol.16 , pp. 111-121
    • Kuhn, J.R.1    Poenie, M.2
  • 3
    • 0036863736 scopus 로고    scopus 로고
    • The secretory synapse: The secrets of a serial killer
    • Bossi, G. et al. The secretory synapse: the secrets of a serial killer. Immunol. Rev. 189, 152-160 (2002).
    • (2002) Immunol. Rev. , vol.189 , pp. 152-160
    • Bossi, G.1
  • 4
    • 0035655587 scopus 로고    scopus 로고
    • The immunological synapse of CTL contains a secretory domain and membrane bridges
    • Stinchcombe, J.C., Bossi, G., Booth, S. & Griffiths, G.M. The immunological synapse of CTL contains a secretory domain and membrane bridges. Immunity 15, 751-761 (2001).
    • (2001) Immunity , vol.15 , pp. 751-761
    • Stinchcombe, J.C.1    Bossi, G.2    Booth, S.3    Griffiths, G.M.4
  • 5
    • 0344002689 scopus 로고    scopus 로고
    • Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome
    • Menasche, G. et al. Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. Nat. Genet. 25, 173-176 (2000).
    • (2000) Nat. Genet. , vol.25 , pp. 173-176
    • Menasche, G.1
  • 6
    • 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).
    • (2001) J. Cell Biol. , vol.152 , pp. 825-834
    • Stinchcombe, J.C.1
  • 7
    • 0035911150 scopus 로고    scopus 로고
    • Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice
    • Haddad, E.K., Wu, X., Hammer, J.A., 3rd & 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 III, J.A.3    Henkart, P.A.4
  • 8
    • 0034330540 scopus 로고    scopus 로고
    • Analysis of the lysosomal storage disease Chediak-Higashi syndrome
    • Ward, D.M., 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
    • Ward, D.M.1    Griffiths, G.M.2    Stinchcombe, J.C.3    Kaplan, J.4
  • 9
    • 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
  • 10
    • 0034911704 scopus 로고    scopus 로고
    • Hermansky-Pudlak syndrome and Chediak-Higashi syndrome: Disorders of vesicle formation and trafficking
    • Huizing, M., Anikster, Y. & Gahl, W.A. Hermansky-Pudlak syndrome and Chediak-Higashi syndrome: disorders of vesicle formation and trafficking. Thromb. Haemost. 86, 233-245 (2001).
    • (2001) Thromb. Haemost. , vol.86 , pp. 233-245
    • Huizing, M.1    Anikster, Y.2    Gahl, W.A.3
  • 11
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor
    • Dell'Angelica, E.C., Shotelersuk, V., Aguilar, R.C., Gahl, W.A. & Bonifacino, J.S. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor. Mol. Cell 3, 11-21 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 11-21
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 12
    • 0036157244 scopus 로고    scopus 로고
    • Nonsense mutations in ADTB3A cause complete deficiency of the β3A subunit of adaptor complex-3 and severe Hermansky-Pudlak syndrome type 2
    • Huizing, M. et al. Nonsense mutations in ADTB3A cause complete deficiency of the β3A subunit of adaptor complex-3 and severe Hermansky-Pudlak syndrome type 2. Pediatr. Res. 51, 150-158 (2002 ).
    • (2002) Pediatr. Res. , vol.51 , pp. 150-158
    • Huizing, M.1
  • 13
    • 0036285648 scopus 로고    scopus 로고
    • Failure of trafficking and antigen presentation by CD1 in AP-3-deficient cells
    • Sugita, M. et al. Failure of trafficking and antigen presentation by CD1 in AP-3-deficient cells. Immunity 16, 697-706 (2002).
    • (2002) Immunity , vol.16 , pp. 697-706
    • Sugita, M.1
  • 14
    • 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
    • Honing, S., Sandoval, I.V. & von Figura, K. 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).
    • (1998) EMBO J. , vol.17 , pp. 1304-1314
    • Honing, S.1    Sandoval, I.V.2    von Figura, K.3
  • 15
    • 0035150104 scopus 로고    scopus 로고
    • AP-3 mediates tyrosinase but not TRP-1 trafficking in human melanocytes
    • Huizing, M. et al. AP-3 mediates tyrosinase but not TRP-1 trafficking in human melanocytes. Mol. Biol. Cell 12, 2075-2085 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2075-2085
    • Huizing, M.1
  • 16
    • 0037148533 scopus 로고    scopus 로고
    • Assembly and function of AP-3 complexes in cells expressing mutant subunits
    • Peden, A.A., Rudge, R.E., Lui, W.W. & Robinson, M.S. Assembly and function of AP-3 complexes in cells expressing mutant subunits. J. Cell Biol. 156, 327-336 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 327-336
    • Peden, A.A.1    Rudge, R.E.2    Lui, W.W.3    Robinson, M.S.4
  • 17
    • 0030926547 scopus 로고    scopus 로고
    • Characterization of the adaptor-related protein complex, AP-3
    • Simpson, F., Peden, A.A., Christopoulou, L. & Robinson, M.S. Characterization of the adaptor-related protein complex, AP-3. J. Cell Biol. 137, 835-845 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 835-845
    • Simpson, F.1    Peden, A.A.2    Christopoulou, L.3    Robinson, M.S.4
  • 18
    • 0036196266 scopus 로고    scopus 로고
    • Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes
    • Rous, B.A. et al. Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes. Mol. Biol. Cell 13, 1071-1082 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1071-1082
    • Rous, B.A.1
  • 19
    • 0027452741 scopus 로고
    • Granzymes A and B are targeted to the lytic granules of lymphocytes by the mannose-6-phosphate receptor
    • Griffiths, G.M. & Isaaz, S. Granzymes A and B are targeted to the lytic granules of lymphocytes by the mannose-6-phosphate receptor. J. Cell Biol. 120, 885-896 (1993).
    • (1993) J. Cell Biol. , vol.120 , pp. 885-896
    • Griffiths, G.M.1    Isaaz, S.2
  • 20
    • 0024464780 scopus 로고
    • Two proteins targeted to the same lytic granule compartment undergo very different posttranslational processing
    • Burkhardt, J.K., Hester, S. & Argon, Y. Two proteins targeted to the same lytic granule compartment undergo very different posttranslational processing. Proc. Natl. Acad. Sci. USA 86, 7128-7132 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7128-7132
    • Burkhardt, J.K.1    Hester, S.2    Argon, Y.3
  • 21
    • 0031464539 scopus 로고    scopus 로고
    • Perform is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid-binding C2 domain
    • Uellner, R. et al. Perform is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid-binding C2 domain. EMBO J. 16, 7287-7296 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7287-7296
    • Uellner, R.1
  • 22
    • 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 Jr., J.M.2    Sheetz, M.P.3    Argon, Y.4
  • 23
    • 0036428014 scopus 로고    scopus 로고
    • The molecular machinery for the biogenesis of lysosome-related organelles: Lessons from Hermansky-Pudlak syndrome
    • Starcevic, M., Nazarian, R. & Dell'Angelica, E.C. The molecular machinery for the biogenesis of lysosome-related organelles: lessons from Hermansky-Pudlak syndrome. Semin. Cell Dev. Biol. 13, 271-278 (2002).
    • (2002) Semin. Cell Dev. Biol. , vol.13 , pp. 271-278
    • Starcevic, M.1    Nazarian, R.2    Dell'Angelica, E.C.3
  • 25
    • 0037312933 scopus 로고    scopus 로고
    • Ru2 and Ru encode mouse orthologs of the genes mutated in human Hermansky-Pudlak syndrome types 5 and 6
    • Zhang, Q. et al. Ru2 and Ru encode mouse orthologs of the genes mutated in human Hermansky-Pudlak syndrome types 5 and 6. Nat. Genet. 33, 145-153 (2003).
    • (2003) Nat. Genet. , vol.33 , pp. 145-153
    • Zhang, Q.1
  • 26
    • 0037666799 scopus 로고    scopus 로고
    • Hermansky-Pudlak syndrome type 4 (HPS-4): Clinical and molecular characteristics
    • Anderson, P.D., Huizing, M., Claassen, D.A., White, J. & Gahl, W.A. Hermansky-Pudlak syndrome type 4 (HPS-4): clinical and molecular characteristics. Hum. Genet. 113, 10-17 (2003).
    • (2003) Hum. Genet. , vol.113 , pp. 10-17
    • Anderson, P.D.1    Huizing, M.2    Claassen, D.A.3    White, J.4    Gahl, W.A.5
  • 27
    • 0038713390 scopus 로고    scopus 로고
    • The Hermansky-Pudlak syndrome 1 (HPS1) and HPS4 proteins are components of two complexes, BLOC-3 and BLOC-4, involved in the biogenesis of lysosome-related organelles
    • Chiang, P.W., Oiso, N., Gautam, R., Swank, R.T. & Spritz, R.A. The Hermansky-Pudlak syndrome 1 (HPS1) and HPS4 proteins are components of two complexes, BLOC-3 and BLOC-4, involved in the biogenesis of lysosome-related organelles. J. Biol. Chem. 278, 20332-20337 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 20332-20337
    • Chiang, P.W.1    Oiso, N.2    Gautam, R.3    Swank, R.T.4    Spritz, R.A.5
  • 28
    • 0038142358 scopus 로고    scopus 로고
    • Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1)
    • Ciciotte, S.L. et al. Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1). Blood 101, 4402-4407 (2003).
    • (2003) Blood , vol.101 , pp. 4402-4407
    • Ciciotte, S.L.1
  • 29
    • 0041854263 scopus 로고    scopus 로고
    • Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1)
    • Li, W. et al. Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1). Nat. Genet. 35, 84-89 (2003).
    • (2003) Nat. Genet. , vol.35 , pp. 84-89
    • Li, W.1
  • 30
    • 18744385809 scopus 로고    scopus 로고
    • Hermansky-Pudlak syndrome: Vesicle formation from yeast to man
    • Huizing, M., Boissy, R.E. & Gahl, W.A. Hermansky-Pudlak syndrome: vesicle formation from yeast to man. Pigment Cell Res. 15, 405-419 (2002).
    • (2002) Pigment Cell Res. , vol.15 , pp. 405-419
    • Huizing, M.1    Boissy, R.E.2    Gahl, W.A.3
  • 31
    • 0027739852 scopus 로고
    • Mutations in U6 snRNA that alter splice site specificity: Implications for the active site
    • Lesser, C.F. & Guthrie, C. Mutations in U6 snRNA that alter splice site specificity: implications for the active site. Science 262, 1982-1988 (1993).
    • (1993) Science , vol.262 , pp. 1982-1988
    • Lesser, C.F.1    Guthrie, C.2
  • 32
    • 0028175201 scopus 로고
    • Randomization-selection analysis of snRNAs in vivo: Evidence for a tertiary interaction in the spliceosome
    • Madhani, H.D. & Guthrie, C. Randomization-selection analysis of snRNAs in vivo: evidence for a tertiary interaction in the spliceosome. Genes Dev. 8, 1071-1086 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 1071-1086
    • Madhani, H.D.1    Guthrie, C.2
  • 33
    • 0032491411 scopus 로고    scopus 로고
    • The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins
    • Le Borgne, R., Alconada, A., Bauer, U. & Hoflack, B. The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins. J. Biol. Chem. 273, 29451-29461 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 29451-29461
    • Le Borgne, R.1    Alconada, A.2    Bauer, U.3    Hoflack, B.4
  • 34
    • 0018474252 scopus 로고
    • Lysosomal dysfunctions associated with mutations at mouse pigment genes
    • Novak, E.K. & Swank, R.T. Lysosomal dysfunctions associated with mutations at mouse pigment genes. Genetics 92, 189-204 (1979).
    • (1979) Genetics , vol.92 , pp. 189-204
    • Novak, E.K.1    Swank, R.T.2
  • 35
    • 0033168252 scopus 로고    scopus 로고
    • Abnormal expression and subcellular distribution of subunit proteins of the AP-3 adaptor complex lead to platelet storage pool deficiency in the pearl mouse
    • Zhen, L. et al. Abnormal expression and subcellular distribution of subunit proteins of the AP-3 adaptor complex lead to platelet storage pool deficiency in the pearl mouse. Blood 94, 146-155 (1999).
    • (1999) Blood , vol.94 , pp. 146-155
    • Zhen, L.1
  • 36
    • 0033836583 scopus 로고    scopus 로고
    • The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Iα-like isoform
    • Faundez, V.V. & Kelly, R.B. The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Iα-like isoform. Mol. Biol. Cell 11, 2591-2604 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2591-2604
    • Faundez, V.V.1    Kelly, R.B.2
  • 37
    • 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
  • 38
    • 0034471359 scopus 로고    scopus 로고
    • Defective organellar membrane protein trafficking in Ap3b1-deficient cells
    • Yang, W., Li, C., Ward, D.M., Kaplan, J. & Mansour, S.L. Defective organellar membrane protein trafficking in Ap3b1-deficient cells. J. Cell Sci. 113, 4077-4086 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 4077-4086
    • Yang, W.1    Li, C.2    Ward, D.M.3    Kaplan, J.4    Mansour, S.L.5
  • 39
    • 0033697037 scopus 로고    scopus 로고
    • A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex
    • Nakagawa, T. et al. A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex. Cell 103, 569-581 (2000).
    • (2000) Cell , vol.103 , pp. 569-581
    • Nakagawa, T.1
  • 40
    • 0029039291 scopus 로고
    • Loss of cytotoxic T lymphocyte function in Chediak-Higashi syndrome arises from a secretory defect that prevents lytic granule exocytosis
    • Baetz, K., Isaaz, S. & Griffiths, G.M. Loss of cytotoxic T lymphocyte function in Chediak-Higashi syndrome arises from a secretory defect that prevents lytic granule exocytosis. J. Immunol. 154, 6122-6131 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 6122-6131
    • Baetz, K.1    Isaaz, S.2    Griffiths, G.M.3
  • 41
    • 0030747460 scopus 로고    scopus 로고
    • Altered expression of a novel adaptin leads to defective pigment granule biogenesis in the Drosophila eye color mutant garnet
    • Ooi, C.E. et al. Altered expression of a novel adaptin leads to defective pigment granule biogenesis in the Drosophila eye color mutant garnet. Embo J. 16, 4508-4518 (1997).
    • (1997) Embo J. , vol.16 , pp. 4508-4518
    • Ooi, C.E.1
  • 42
    • 0031566379 scopus 로고    scopus 로고
    • β3A-adaptin, a subunit of the adaptor-like complex AP-3
    • Dell'Angelica, E.C., Ooi, C.E. & Bonifacino, J.S. β3A-adaptin, a subunit of the adaptor-like complex AP-3. J. Biol. Chem. 272, 15078-15084 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 15078-15084
    • Dell'Angelica, E.C.1    Ooi, C.E.2    Bonifacino, J.S.3
  • 43
    • 0031051571 scopus 로고    scopus 로고
    • AP-3: An adaptor-like protein complex with ubiquitous expression
    • Dell'Angelica, E.C. et al. AP-3: an adaptor-like protein complex with ubiquitous expression. Embo J. 16, 917-928 (1997).
    • (1997) Embo J. , vol.16 , pp. 917-928
    • Dell'Angelica, E.C.1
  • 44
    • 0023640891 scopus 로고
    • A novel cytotoxic T lymphocyte activation assay. Optimized conditions for antigen receptor triggered granule enzyme secretion
    • Takayama, H., Trenn, G. & Sitkovsky, M.V. A novel cytotoxic T lymphocyte activation assay. Optimized conditions for antigen receptor triggered granule enzyme secretion. J. Immunol. Meth. 104, 183-190 (1987).
    • (1987) J. Immunol. Meth. , vol.104 , pp. 183-190
    • Takayama, H.1    Trenn, G.2    Sitkovsky, M.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.