Inhibitory receptors, ITIM sequences and phosphatases

Current Opinion in Immunology

Volumn 9, Issue 3, 1997, Pages 338-343

  Unkeless, Jay C ^a   Jin, Jie ^a  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL RECEPTOR; FC RECEPTOR; PROTEIN TYROSINE PHOSPHATASE; T LYMPHOCYTE RECEPTOR; TYROSINE;

CYTOTOXIC T LYMPHOCYTE; PHOSPHORYLATION; REVIEW;

EID: 0030873248     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(97)80079-9     Document Type: Article

References (42)

1. Reth M. Antigen receptor tail clue. Nature. 338:1989;383-384.
2. Chan AC, Shaw AS. Regulation of antigen receptor signal transduction by protein tyrosine kinases. of special interest Curr Opin Immunol. 8:1996;394-401 A concise review describing the kinases and phosphorylation events involved during ITAM-mediated antigen-receptor signaling in T cells.
3. Muta T, Kurosaki T, Misulovin Z, Sanchez M, Nussenzweig MC, Ravetch JV. A 13-amino-acid motif in the cytoplasmic domain of FcgammaRIIB modulates B-cell receptor signalling. Nature. 368:1994;70-73.
4. Burshtyn DN, Scharenberg AM, Wagtmann N, Rajagopalan S, Berrada K, Yi T, Kinet JP, Long EO. Recruitment of tyrosine phosphatase HCP by the killer cell inhibitor receptor. of outstanding interest Immunity. 4:1996;77-85 This report describes how, after cross-linking the NK cell KIR p58, the cytoplasmic tail of p58 is tyrosine-phosphorylated and associates with SHP-1 which activates the enzyme. Overexpression of a dominant negative SHP-1 mutant in NK cell clones prevents MHC class I mediated inhibition of NK-cell lysis. These results suggest that SHP-1 is essential in mediating the inhibitory signal. See also annotations [26,27].
5. + IL-2-activated natural killer cells. Nature. 358:1992;66-70.
6. Sgroi D, Varki A, Braesch-Andersen S, Stamenkovic I. CD22, a B cell-specific immunoglobulin superfamily member, is a sialic acid-binding lectin. J Biol Chem. 268:1993;7011-7018.
7. Tuscano J, Engel P, Tedder TF, Kehrl JH. Engagement of the adhesion receptor CD22 triggers a potent stimulatory signal for B cells and blocking CD22/CD22L interactions impairs T-cell proliferation. of special interest Blood. 87:1996;4723-4730 This paper reports that the anti-CD22 monoclonal antibody HB22.7 blocks the binding of CD22 to its ligand(s) and directly stimulates B-cell proliferation, suggesting an inhibitory role for CD22 in B-cell activation.
8. Doody GM, Justement LB, Delibrias CC, Matthews RJ, Lin J, Thomas ML, Fearon DT. A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP. of outstanding interest Science. 269:1995;242-244 This paper describes the functional association of CD22 with SHP-1 and the augmentation of antigen-receptor signaling following ligation of CD22. This implies an inhibitory role for CD22 in B-cell signaling.
9. Walunas TL, Bakker CY, Bluestone JA. CTLA-4 ligation blocks CD28-dependent T cell activation. of special interest J Exp Med. 183:1996;2541-2550 This report, along with [10], shows that CTLA-4 ligation inhibits T-cell activation by blocking CD28-mediated IL-2 production and the cell cycle progression of activated T cells.
10. Krummel MF, Allison JP. CTLA-4 engagement inhibits IL-2 accumulation and cell cycle progression upon activation of resting T cells. of special interest J Exp Med. 183:1996;2533-2540 See annotation [9].
11. Marengere LE, Waterhouse P, Duncan GS, Mittrucker HW, Feng GS, Mak TW. Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4. of outstanding interest Science. 272:1996;1170-1173 The authors show that CTLA-4 specifically associates with Syp (SHP-2). The interaction is mediated by the SH2 domain of Syp and the phosphotyrosine sequence YVKM (single-letter amino acid code) in the CTLA-4 cytoplasmic tail. The CTLA-4-recruited Syp has phosphatase activity and may play a role in inhibiting T-cell activation.
12. Phillips NE, Parker DC. Subclass specificity of Fc gamma receptor-mediated inhibition of mouse B cell activation. J Immunol. 134:1985;2835-2838.
13. 2+ mobilization and B-cell proliferation following co-ligation of membrane immunoglobulin with FcγRIIB1. The presence of a second protein, later identified as SHIP [37,38], was noted.
14. Tsui HW, Siminovitch KA, De Souza L, Tsui FW. Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nat Genet. 4:1993;124-129.
15. Kozlowski M, Mlinaric-Rascan I, Feng GS, Shen R, Pawson T, Siminovitch KA. Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice. J Exp Med. 178:1993;2157-2163.
16. Shultz LD, Schweitzer PA, Rajan TV, Yi T, Ihle JN, Matthews RJ, Thomas ML, Beier DR. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph). Cell. 73:1993;1445-1454.
17. Yi T, Mui AL, Krystal G, Ihle JN. Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis. Mol Cell Biol. 13:1993;7577-7586.
18. Klingmuller U, Lorenz U, Cantley LC, Neel BG, Lodish HF. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. of special interest Cell. 80:1995;729-738 Reports that the tyrosine-phosphorylated erythropoietin receptor recruits SHP-1 which terminates erythropoietin receptor signaling by dephosphorylating and inactivating Jak2.
19. David M, Chen HE, Goelz S, Larner AC, Neel BG. Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol Cell Biol. 15:1995;7050-7058.
20. Jiao HY, Berrada K, Yang WT, Tabrizi M, Platanias LC, Yi TL. Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1. of special interest Mol Cell Biol. 16:1996;6985-6992 Demonstates that SHP-1 directly associates with and dephosphorylates Jak2, showing the generality of SHP-1 activity as an inhibitory modulator.
21. Yu CC, Tsui HW, Ngan BY, Shukman MJ, Wu GE, Tsui FW. B and T cells are not required for the viable motheaten phenotype. J Exp Med. 183:1996;371-380.
22. v B-cell activation establish a role for SHP-1 in negative signaling in B-cells. SHP-1 associates with the resting BCR complex but dissociates from the complex upon BCR stimulation.
23. Daeron M, Latour S, Malbec O, Espinosa E, Pina P, Pasmans S, Fridman WH. The same tyrosine-based inhibition motif, in the intracytoplasmic domain of Fc γRIIB, regulates negatively BCR-, TCR-, and FcR-dependent cell activation. of special interest Immunity. 3:1995;635-646 In T-cell lines and basophilic leukemia cells transfected with FcγRIIB isoforms, the same ITIM is shown to inhibit TCR-, FcγR-, and BCR-dependent cell activation.
24. Takai T, Ono M, Hikida M, Ohmori H, Ravetch JV. Augmented humoral and anaphylactic responses in Fc gamma RII-deficient mice. of outstanding interest Nature. 379:1996;346-349 Analysis of FcγRII-deficient mice confirms the negative regulatory role of this receptor in immune complex initiated signaling.
25. Colonna M, Samaridis J. Cloning of immunoglobulin-superfamily members associated with HLA-C and HLA-B recognition by human natural killer cells. of special interest Science. 268:1995;405-408 This paper describes the molecular cloning and sequencing of the genes encoding members of the KIR family, showing that human KIRs are members of the Ig superfamily and that the cytoplasmic domains of KIRs contain ITAM-like motifs, now termed ITIMs.
26. Fry AM, Lanier LL, Weiss A. Phosphotyrosines in the killer cell inhibitory receptor motif of NKB1 are required for negative signaling and for association with protein tyrosine phosphatase 1C. of outstanding interest J Exp Med. 184:1996;295-300 The chimeric receptor CD8-NKB1 is found to be capable of inhibiting T-cell activation in Jurkat cells. The tyrosine phosphorylation of the NKB1 ITIM induces its association with SHP-1. Mutation of both tyrosines in the ITIM abolishes SHP-1 association and the inhibitory functions of NKB1. The membrane-proximal tyrosine is suggested to play a crucial role in mediating the inhibitory signal.
27. Campbell KS, Dessing M, Lopez Botet M, Cella M, Colonna M. Tyrosine phosphorylation of a human killer inhibitory receptor recruits protein tyrosine phosphatase 1C. of outstanding interest J Exp Med. 184:1996;93-100 Demonstrates that tyrosine phosphorylation of the ITIM of the human KIR p58 recruits SHP-1.
28. Binstadt BA, Brumbaugh KM, Dick CJ, Scharenberg AM, Williams BD, Collona M, Lanier LL, Kinet J-P, Abraham RT, Leibson PJ. Sequential involvement of Lck and Shp-1 with MHC-recognizing receptors on NK cells inhibits FcR-initiated tyrosine kinase activation. of outstanding interest Immunity. 5:1996;629-638 The authors show that the Src family kinase Lck is required for tyrosine phosphorylation of KIRs. KIR ligation inhibits the FcR-induced tyrosine phosphorylation of the ζ chain, ZAP70 and PLC-γ. Expression of dominant negative mutant SHP-1 restores the tyrosine phosphorylation of these molecules and reverses the KIR-mediated inhibition.
29. Ting AT, Karnitz LM, Schoon RA, Abraham RT, Leibson PJ. Fc gamma receptor activation induces the tyrosine phosphorylation of both phospholipase C (PLC)-gamma 1 and PLC-γ amma 2 in natural killer cells. J Exp Med. 176:1992;1751-1755.
30. Kanakaraj P, Duckworth B, Azzoni L, Kamoun M, Cantley LC, Perussia B. Phosphatidylinositol-3 kinase activation induced upon Fc gamma RIIIA-ligand interaction. J Exp Med. 179:1994;551-558.
31. Azzoni L, Kamoun M, Salcedo TW, Kanakaraj P, Perussia B. Stimulation of Fc gamma RIIIA results in phospholipase C-gamma 1 tyrosine phosphorylation and p56lck activation. J Exp Med. 176:1992;1745-1750.
32. Bonnema JD, Karnitz LM, Schoon RA, Abraham RT, Leibson PJ. Fc receptor stimulation of phosphatidylinositol 3-kinase in natural killer cells is associated with protein kinase C-independent granule release and cell-mediated cytotoxicity. J Exp Med. 180:1994;1427-1435.
33. Ting AT, Dick CJ, Schoon RA, Kamitz LM, Abraham RT, Leibson PJ. Interaction between lck and syk family tyrosine kinases in Fc gamma receptor-initiated activation of natural killer cells. J Biol Chem. 270:1995;16415-16421.
34. Kaufman DS, Schoon RA, Robertson MJ, Leibson PJ. Inhibition of selective signaling events in natural killer cells recognizing major histocompatibility complex class I. Proc Natl Acad Sci USA. 92:1995;6484-6488.
35. Plas DR, Johnson R, Pingel JT, Matthews RJ, Dalton M, Roy G, Chan AC, Thomas ML. Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling. of outstanding interest Science. 272:1996;1173-1176 SHP-1 binds to activated ZAP-70, resulting in activation of SHP-1 and inactivation of ZAP-70.
36. Lck, ZAP70 and the TCR ζ chain into insect cells, that SHP-1 dephosphorylates these molecules.
37. Ono M, Bolland S, Tempst P, Ravetch JV. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB. of outstanding interest Nature. 383:1996;263-266 This paper reports that FcγRIIB inhibitory signaling does not require SHP-1 in mast cells. The FcγRIIB ITIM recruits SHIP in B cells and mast cells, and SHIP is suggested to play a dominant role in negative signaling in these cell types.
38. Osborne MA, Zenner G, Lubinus M, Zhang XL, Songyang Z, Cantley LC, Majerus P, Burn P, Kochan JP. The inositol 5'-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation. of outstanding interest J Biol Chem. 271:1996;29271-29278 This paper reports that the FcεRI ITAM, as well as the ITAM motifs of the TCR ζ, ε, and δ chains, recruits SHIP. SHIP activity is inhibited by Lck phosphorylation, suggesting that maximal TCR or FcεRI stimulation inactivates SHIP.
39. 2+ channels.
40. Luckhoff A, Clapham DE. Inositol 1,3,4,5-tetrakisphosphate activates an endothelial Ca(2+)-permeable channel. Nature. 355:1992;356-358.
41. Franke TF, Yang SI, Chan TO, Datta K, Kazlauskas A, Morrison DK, Kaplan DR, Tsichlis PN. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell. 81:1995;727-736.
42. Burgering BM, Coffer PJ. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature. 376:1995;599-602.