Regulated secretion from CD4+ T cells

Trends in Immunology

Volumn 28, Issue 11, 2007, Pages 474-481

  Jolly, Clare ^a   Sattentau, Quentin J ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CYTOKINE; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4;

BIOGENESIS; CD4+ T LYMPHOCYTE; CELL KILLING; CELL MIGRATION; IMMUNOCOMPETENT CELL; LYMPHOCYTE; NATURAL KILLER T CELL; REVIEW;

ANIMALS; ANTIGENS, CD; ANTIGENS, DIFFERENTIATION; CD4-POSITIVE T-LYMPHOCYTES; CYTOKINES; FAS LIGAND PROTEIN; HIV-1; HUMAN IMMUNODEFICIENCY VIRUS PROTEINS; HUMANS; KILLER CELLS, NATURAL; LYSOSOMES; PROTEIN TRANSPORT; RECEPTORS, ANTIGEN, T-CELL; T-LYMPHOCYTES, CYTOTOXIC;

EID: 36048947746     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2007.08.008     Document Type: Review

References (80)

1. Davis D.M., and Dustin M.L. What is the importance of the immunological synapse?. Trends Immunol. 25 (2004) 323-327
2. Stinchcombe J.C., and Griffiths G.M. The role of the secretory immunological synapse in killing by CD8+ CTL. Semin. Immunol. 15 (2003) 301-305
3. Bossi G., and Griffiths G.M. CTL secretory lysosomes: biogenesis and secretion of a harmful organelle. Semin. Immunol. 17 (2005) 87-94
4. Peters P.J., et al. Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes. J. Exp. Med. 173 (1991) 1099-1109
5. Stinchcombe J., et al. Linking albinism and immunity: the secrets of secretory lysosomes. Science 305 (2004) 55-59
6. Kupfer A., et al. Polarized expression of cytokines in cell conjugates of helper T cells and splenic B cells. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 775-779
7. Kupfer H., et al. Small splenic B cells that bind to antigen-specific T helper (Th) cells and face the site of cytokine production in the Th cells selectively proliferate: immunofluorescence microscopic studies of Th-B antigen-presenting cell interactions. J. Exp. Med. 179 (1994) 1507-1515
8. Bossi G., and Griffiths G.M. 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
9. Appay V., et al. Characterization of CD4(+) CTLs ex vivo. J. Immunol. 168 (2002) 5954-5958
10. Morales-Tirado V., et al. Cutting edge: selective requirement for the Wiskott-Aldrich syndrome protein in cytokine, but not chemokine, secretion by CD4+ T cells. J. Immunol. 173 (2004) 726-730
11. Huse M., et al. T cells use two directionally distinct pathways for cytokine secretion. Nat. Immunol. 7 (2006) 247-255
12. Iida T., et al. 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
13. Stalder T., et al. Fas antigen is the major target molecule for CD4+ T cell-mediated cytotoxicity. J. Immunol. 152 (1994) 1127-1133
14. Williams N.S., and Engelhard V.H. Identification of a population of CD4+ CTL that utilizes a perforin- rather than a Fas ligand-dependent cytotoxic mechanism. J. Immunol. 156 (1996) 153-159
15. Yasukawa M., et al. Granule exocytosis, and not the fas/fas ligand system, is the main pathway of cytotoxicity mediated by alloantigen-specific CD4(+) as well as CD8(+) cytotoxic T lymphocytes in humans. Blood 95 (2000) 2352-2355
16. Susskind B., et al. Cytolytic effector mechanisms of human CD4+ cytotoxic T lymphocytes. Hum. Immunol. 45 (1996) 64-75
17. Linsley P.S., et al. Intracellular trafficking of CTLA-4 and focal localization towards sites of TCR engagement. Immunity 4 (1996) 535-543
18. Shen D.T., et al. Activation of primary T lymphocytes results in lysosome development and polarized granule exocytosis in CD4+ and CD8+ subsets, whereas expression of lytic molecules confers cytotoxicity to CD8+ T cells. J. Leukoc. Biol. 80 (2006) 827-837
19. Poo W.J., et al. Receptor-directed focusing of lymphokine release by helper T cells. Nature 332 (1988) 378-380
20. Krummel M.F., and Allison J.P. CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation. J. Exp. Med. 182 (1995) 459-465
21. Lee K.M., et al. Molecular basis of T cell inactivation by CTLA-4. Science 282 (1998) 2263-2266
22. Linsley P.S., and Golstein P. Lymphocyte activation: T-cell regulation by CTLA-4. Curr. Biol. 6 (1996) 398-400
23. Zhang Y., and Allison J.P. Interaction of CTLA-4 with AP50, a clathrin-coated pit adaptor protein. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 9273-9278
24. Leung H.T., et al. Cytotoxic T lymphocyte-associated molecule-4, a high-avidity receptor for CD80 and CD86, contains an intracellular localization motif in its cytoplasmic tail. J. Biol. Chem. 270 (1995) 25107-25114
25. Oaks M.K., et al. A native soluble form of CTLA-4. Cell Immunol. 201 (2000) 144-153
26. Ueda H., et al. Association of the T-cell regulatory gene CTLA4 with susceptibility to autoimmune disease. Nature 423 (2003) 506-511
27. Sansom D.M., and Walker L.S. The role of CD28 and cytotoxic T-lymphocyte antigen-4 (CTLA-4) in regulatory T-cell biology. Immunol. Rev. 212 (2006) 131-148
28. Linkermann A., et al. Slowly getting a clue on CD95 ligand biology. Biochem. Pharmacol. 66 (2003) 1417-1426
29. Tanaka M., et al. Downregulation of Fas ligand by shedding. Nat. Med. 4 (1998) 31-36
30. Vignaux F., et al. TCR/CD3 coupling to Fas-based cytotoxicity. J. Exp. Med. 181 (1995) 781-786
31. Zuccato E., et al. Sorting of Fas ligand to secretory lysosomes is regulated by mono-ubiquitylation and phosphorylation. J. Cell Sci. 120 (2007) 191-199
32. Blott E.J., et al. Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail. J. Cell Sci. 114 (2001) 2405-2416
33. Martinez-Lorenzo M.J., et al. Activated human T cells release bioactive Fas ligand and APO2 ligand in microvesicles. J. Immunol. 163 (1999) 1274-1281
34. Williams N.S., and Engelhard V.H. Perforin-dependent cytotoxic activity and lymphokine secretion by CD4+ T cells are regulated by CD8+ T cells. J. Immunol. 159 (1997) 2091-2099
35. Sun Q., et al. Cytokine production and cytolytic mechanism of CD4(+) cytotoxic T lymphocytes in ex vivo expanded therapeutic Epstein-Barr virus-specific T-cell cultures. Blood 99 (2002) 3302-3309
36. Gondek D.C., et al. Cutting edge: contact-mediated suppression by CD4+CD25+ regulatory cells involves a granzyme B-dependent, perforin-independent mechanism. J. Immunol. 174 (2005) 1783-1786
37. Caumartin J., et al. Intercellular exchanges of membrane patches (trogocytosis) highlight the next level of immune plasticity. Transpl. Immunol. 17 (2006) 20-22
38. Olsen I., et al. The activation of resting lymphocytes is accompanied by the biogenesis of lysosomal organelles. Eur. J. Immunol. 20 (1990) 2161-2170
39. Lettau M., et al. The adaptor protein Nck interacts with Fas ligand: Guiding the death factor to the cytotoxic immunological synapse. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 5911-5916
40. Oki S., et al. Augmentation of CTLA-4 expression by wortmannin: involvement of lysosomal sorting properties of CTLA-4. Int. Immunol. 11 (1999) 1563-1571
41. Bonifacino J.S., and Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72 (2003) 395-447
42. Griffiths G.M., and Isaaz S. 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
43. Stinchcombe J.C., et al. Centrosome polarization delivers secretory granules to the immunological synapse. Nature 443 (2006) 462-465
44. Fischer A., et al. Genetic defects affecting lymphocyte cytotoxicity. Curr. Opin. Immunol. 19 (2007) 348-353
45. Stinchcombe J.C., et al. Secretory lysosome biogenesis in cytotoxic T lymphocytes from normal and Chediak Higashi syndrome patients. Traffic 1 (2000) 435-444
46. Ward D.M., et al. Analysis of the lysosomal storage disease Chediak-Higashi syndrome. Traffic 1 (2000) 816-822
47. Stinchcombe J.C., et al. Rab27a is required for regulated secretion in cytotoxic T lymphocytes. J. Cell Biol. 152 (2001) 825-834
48. Haddad E.K., et al. Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice. J. Cell Biol. 152 (2001) 835-842
49. Hume A.N., et al. The leaden gene product is required with Rab27a to recruit myosin Va to melanosomes in melanocytes. Traffic 3 (2002) 193-202
50. Clark R.H., et al. Adaptor protein 3-dependent microtubule-mediated movement of lytic granules to the immunological synapse. Nat. Immunol. 4 (2003) 1111-1120
51. Neeft M., et al. Munc13-4 is an effector of rab27a and controls secretion of lysosomes in hematopoietic cells. Mol. Biol. Cell 16 (2005) 731-741
52. Feldmann J., et al. Munc13-4 is essential for cytolytic granules fusion and is mutated in a form of familial hemophagocytic lymphohistiocytosis (FHL3). Cell 115 (2003) 461-473
53. Tolmachova T., et al. A general role for Rab27a in secretory cells. Mol. Biol. Cell 15 (2004) 332-344
54. Wyss S., et al. The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor. J. Virol. 75 (2001) 2982-2992
55. Jolly C., et al. Requirement for an intact T cell actin and tubulin cytoskeleton for efficient HIV-1 assembly and spread. J. Virol. 81 (2007) 5547-5560
56. Morita E., and Sundquist W.I. Retrovirus budding. Annu. Rev. Cell Dev. Biol. 20 (2004) 395-425
57. Dong X., et al. AP-3 directs the intracellular trafficking of HIV-1 Gag and plays a key role in particle assembly. Cell 120 (2005) 663-674
58. Boge M., et al. A membrane-proximal tyrosine-based signal mediates internalization of the HIV-1 envelope glycoprotein via interaction with the AP-2 clathrin adaptor. J. Biol. Chem. 273 (1998) 15773-15778
59. Murray J.L., et al. Rab9 GTPase is required for replication of human immunodeficiency virus type 1, filoviruses, and measles virus. J. Virol. 79 (2005) 11742-11751
60. Blot G., et al. Targeting of the human immunodeficiency virus type 1 envelope to the trans-Golgi network through binding to TIP47 is required for env incorporation into virions and infectivity. J. Virol. 77 (2003) 6931-6945
61. Fackler O.T., and Krausslich H.G. Interactions of human retroviruses with the host cell cytoskeleton. Curr. Opin. Microbiol. 9 (2006) 409-415
62. Raposo G., et al. Human macrophages accumulate HIV-1 particles in MHC II compartments. Traffic 3 (2002) 718-729
63. Pelchen-Matthews A., et al. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 162 (2003) 443-455
64. Nydegger S., et al. HIV-1 egress is gated through late endosomal membranes. Traffic 4 (2003) 902-910
65. Jolly C., and Sattentau Q.J. HIV-1 assembly, budding and cell-cell spread in T cells takes place in tetraspanin-enriched plasma membrane domains. J. Virol. 81 (2007) 7873-7884
66. Miranda L.R., et al. Cell surface expression of the HIV-1 envelope glycoproteins is directed from intracellular CTLA-4-containing regulated secretory granules. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 8031-8036
67. Steiner K., et al. Enhanced expression of CTLA-4 (CD152) on CD4+ T cells in HIV infection. Clin. Exp. Immunol. 115 (1999) 451-457
68. Jolly C., et al. HIV-1 cell to cell transfer across an Env-induced, actin-dependent synapse. J. Exp. Med. 199 (2004) 283-293
69. Jolly C., and Sattentau Q.J. Retroviral spread by induction of virological synapses. Traffic 5 (2004) 643-650
70. Igakura T., et al. Spread of HTLV-I between lymphocytes by virus-induced polarization of the cytoskeleton. Science 299 (2003) 1713-1716
71. Blanchard N., et al. In the immune synapse. ZAP-70 controls T cell polarization and recruitment of signaling proteins but not formation of the synaptic pattern. Immunity 17 (2002) 389-399
72. Sol-Foulon N., et al. ZAP-70 kinase regulates HIV cell-to-cell spread and virological synapse formation. Embo. J. 26 (2007) 516-526
73. Stinchcombe J.C., and Griffiths G.M. Regulated secretion from hemopoietic cells. J. Cell Biol. 147 (1999) 1-6
74. Nydegger S., et al. Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1. J Cell Biol. 137 (2006) 795-807
75. McNicol A., and Israels S.J. Platelet dense granules: structure, function and implications for haemostasis. Thromb. Res. 95 (1999) 1-18
76. Peters P.J., et al. Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments. Nature 349 (1991) 669-676
77. Gullberg U., et al. Biosynthesis, processing and sorting of neutrophil proteins: insight into neutrophil granule development. Eur. J. Haematol. 58 (1997) 137-153
78. Raposo G., et al. Accumulation of major histocompatibility complex class II molecules in mast cell secretory granules and their release upon degranulation. Mol. Biol. Cell 8 (1997) 2631-2645
79. Dragonetti A., et al. The lysosomal protease cathepsin D is efficiently sorted to and secreted from regulated secretory compartments in the rat basophilic/mast cell line RBL. J. Cell Sci. 113 (2000) 3289-3298
80. Persson T., et al. Specific granules of human eosinophils have lysosomal characteristics: presence of lysosome-associated membrane proteins and acidification upon cellular activation. Biochem. Biophys. Res. Commun. 291 (2002) 844-854