Protein tyrosine phosphatases in signal transduction

Current Opinion in Cell Biology

Volumn 9, Issue 2, 1997, Pages 193-204

  Neel, Benjamin G ^a   Tonks, Nicholas K ^b  

^a BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

^b Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; PROTEIN TYROSINE PHOSPHATASE;

CELL INTERACTION; CRYSTAL STRUCTURE; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; REVIEW; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

EID: 0030953448     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80063-4     Document Type: Article

References (79)

1. Dixon JE, Zhang Z-Y: Protein tyrosine phosphatases: mechanism of catalysis and substrate specificity. Adv Enzymol Relat Areas Mol Biol 1994, 68:1-36.
2. Denu JE, Stuckey JA, Saper MA, Dixon JE: Form and function in protein dephosphorylation. Cell 1996, 87:361-364. This minireview covers recent developments in studies of the enzymology and structure of serine/threonine and tyrosine phosphatases.
3. Pulido R, Serra-Pages C, Tang M, Streuli M: The LAR/PTPδ/PTPσ subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTPδ, and PTPσ isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1. Proc Natl Acad Sci USA 1995, 92:11686-11690.
4. Serra-Pages C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M: The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein colocalize at focal adhesions. EMBO J 1995, 14:2827-2838.
5. Mondesert O, Moreno S, Russell P: Low molecular weight protein-tyrosine phosphatases are highly conserved between fission yeast and man. J Biol Chem 1994, 269:27996-27999.
6. Barford D, Flint AJ, Tonks NK: Crystal structure of human protein tyrosine phosphatase 1B. Science 1994, 263:1397-1404.
7. Stuckey JA, Schubert HL, Fauman EB, Zhang ZY, Dixon JE, Saper MA: Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Ȧ and the complex with tungstate. Nature 1994, 370:571-575.
8. Jia Z, Barford D, Flint AJ, Tonks NK: Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science 1995, 268:1754-1758. The authors of this paper describe the large conformational change that occurs in PTP-1B upon phosphotyrosyl peptide binding. This change results in the realignment of the aspartyl residue that serves as the general acid in the catalytic mechanism towards the active site of the enzyme.
9. Bilwes AM, Den Hertog J, Hunter T, Noel JP: Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization. Nature 1996, 382:555-559. This is the first report of a crystal structure for a receptor PTP. Domain 1 of RPTPα is revealed to form dimers in which the ammo-terminal helix-turn-helix of one monomer inserts into the mouth of the catalytic cleft of the other. The implication of this study is that dimerization of RPTPs would be expected to lead to inhibition of their catalytic activity.
10. Flint AJ, Tiganis T, Barford D, Tonks NK: Development of 'substrate trapping' mutants to identify physiological substrates of protein-tyrosine phosphatases. Proc Natl Acad Sci USA 1997, in press. This paper extends the authors' initial observations [14••] on the use of substrate-trapping mutants.
11. Zhang ZY, Wang Y, Dixon JE: Dissecting the catalytic mechanism of protein-tyrosine phosphatases. Proc Natl Acad Sci USA 1994, 91:1624-1627.
12. Bliska JB, Clemens JC, Dixon JE, Falkow S: The Yersinia tyrosine phosphatase: specificity of a bacterial virulence determinant for phosphoproteins in the J774A.1 macrophage. J Exp Med 1992, 176:1625-1630.
13. Sun H, Charles CH, Lau LF, Tonks NK: MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 1993, 75:487-493.
14. Garton AJ, Flint AJ, Tonks NK: Identification of p130cas as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. Mol Cell Biol 1996, 16:6408-6418. This paper describes the generation and use of mutants of the essential general acid residue of PTP-PEST to identify a specific protein substrate, p130cas, and discusses the general use of Asp→Ala mutants and Cys→Ser mutants as substrate traps.
15. Shiozaki K, Russell P: Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast. Nature 1995, 378:739-743. Together with [76••], this paper describes the regulation of the S. pombe Sty1/Spc1 pathway by two PTPs, Pyp1 and Pyp2, and the involvement of this pathway in response to stress and in mitotic control.
16. Desai DM, Sap J, Schlessinger J, Weiss A: Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell 1993, 73:541-554.
17. Zinn K: Drosophila protein tyrosine phosphatases. Semin Cell Biol 1993, 4:397-401.
18. Desai CJ, Gindhart JG Jr, Goldstein LS, Zinn K: Receptor tyrosine phosphatases are required for motor axon guidance in the Drosophila embryo. Cell 1996, 84:599-609. Together with [19••], this paper presents genetic evidence for the involvement of RPTPs in neuron guidance in Drosophila.
19. Krueger NX, Van Vactor D, Wan HI, Gelbart WM, Goodman CS, Saito H: The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila. Cell 1996, 84:611-622. Together with [18••], this paper presents genetic evidence for the involvement of RPTPs in neuron guidance in Drosophila.
20. Lin DM, Goodman CS: Ectopic and increased expression of fasiculin III alters motoneuron growth cone guidance. Neuron 1994, 13:507-523.
21. Peles E, Nativ M, Campbell PL, Sajurai T, Martinez R, Lev S, Clary DO, Schilling J, Barnea G, Plowman GD et al.: The carbonic anhydrase domain of receptor tyrosine phosphatase β is a functional ligand for the axonal recognition molecule contactin. Cell 1995, 82:251-260. This paper identifies the ectodomain of RPTPβ/ζ as a ligand for the neuronal recognition molecule contactin and the ectodomain of contactin as a putative ligand for RPTPβ/ζ.
22. Gebbink MFBG, Zondag GCM, Wubbolts RW, Beijersbergen RL, Van Etten I, Moolenaar WH: Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase. J Biol Chem 1993, 268:16101-16104.
23. Sap J, Jiang Y-P, Friedlander D, Grumet M, Schlessinger J: Receptor tyrosine phosphatase R-PTPκ mediates homophilic binding. Mol Cell Biol 1994, 14:1-9.
24. Brady-Kalnay SM, Tonks NK: Protein tyrosine phosphatases as adhesion receptors. Curr Opin Cell Biol 1995, 7:650-657.
25. Brady-Kalnay S, Tonks NK: Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTPμ. J Biol Chem 1994, 269:28472-28477.
26. Zondag GCM, Koningstein GM, Jiang Y-P, Sap J, Moolenaar WH, Gebbink MFBG: Homophilic interactions mediated by receptor tyrosine phosphatases μ and κ. J Biol Chem 1995, 270:14247-14250.
27. Fuchs M, Mueller T, Lerch MM, Ullrich A: Association of human protein tyrosine phosphatase κ with members of the armadillo family. J Biol Chem 1996, 271:16712-16719.
28. Kypta RM, Su H, Reichardt LF: Association between a transmembrane protein-tyrosine phosphatase and the cadherin-catenin complex. J Cell Biol 1996, 134:1519-1529.
29. Gumbiner BM: Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell 1996, 84:345-357.
30. Yi T, Mui AL-F, Krystal G, Ihle JN: Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor β chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis. Mol Cell Biol 1993, 13:7577-7586.
31. 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. Cell 1995, 80:729-738. Together with [32], this paper provides the first evidence that SHP-1 negatively regulates cytokine receptor signaling by dephosphorylating and inactivating cytokine receptor associated Janus family PTKs.
32. David M, Chen HE, Ling L, Goelz S, Larner AC, Neel BG: Differential regulation of the α/β interferon-stimulated Jak/Stat pathway by the SH2-domain containing tyrosine phosphatase SHPTP1. Mol Cell Biol 1995, 15:7050-7058.
33. Lorenz U, Bergemann AD, Steinberg HN, Flanagan JG, Li X, Galli SJ, Neel BG: Genetic analysis reveals cell type-specific regulation of receptor tyrosine kinase c-Kit by the protein tyrosine phosphatase SHP1. J Exp Med 1996, 184:1111-1126. Together with [56••], this paper uses a genetic approach to evaluate the biological significance of interactions between c-Kit and SHP-1. These studies conclude that SHP-1 does, indeed, negatively regulate c-Kit in vivo, but, unexpectedly, in a tissue-specific manner.
34. Ravetch JV: Fc receptors: rubor redux. Cell 1994, 78:553-560.
35. Muta T, Kurosaki T, Misulovin Z, Sanchez M, Nussenzweig MC, Ravetch JV: A 13-amino-acid motif in the cytoplasmic domain of Fc gamma RIIB modulates B-cell receptor signalling. Nature 1994, 368:70-73.
36. D'Ambrosio D, Hippen KL, Minskoff SA, Mellman I, Pani G, Siminovitch KA, Cambier JC: Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RIIB1. Science 1995, 268:293-297. This paper provides evidence for the involvement of SHP-1 in the negative regulation of BCR activation pathways via the inhibitory Fc receptor, FcγRIIB.
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 FcγRIIB. Nature 1996, 383:263-266. This paper shows that SHP-1 is not required for signaling through FcγRIIB in mast cells, and instead suggests the involvement of the inositol monophosphatase SHIP.
38. Sarkar S, Schlottmann K, Clooney D, Coggeshall KM: Negative signaling via FcγRIIB1 in B cells blocks phospholipase Cγ2 tyrosine phosphorylation but not Syk or Lyn activation. J Biol Chem 1996, 271:20182-20186.
39. Diegel ML, Rankin BM, Bolen JB, Dubois PM, Kiener PA: Cross-linking of Fc gamma receptor to surface immunoglobulin on B cells provides an inhibitory signal that closes the plasma membrane calcium channel. J Biol Chem 1994, 269:11409-11416.
40. Burshtyn DN, Scharenberg AM, Wagtmann N, Rajagopalan S, Berrada K, Yi T, Kinet J-P, Long EO: Recruitment of tyrosine phosphatase HCP by the killer cell inhibitory receptor. Immunity 1996, 4:77-85. This paper provides evidence for the involvement of SHP-1 in negative regulation of activating receptors by KIRs, and defines ITIM sequence features.
41. Campbell KS, Dessing M, Lopez-Botet M, Cella M, Colonna M: Tyrosine phosphorylation of human killer inhibitory receptor recruits protein tyrosine phosphatase 1C. J Exp Med 1996, 184:93-100.
42. Fry AM, Lanier LL, Weiss A: Phosphotyrosines in the killer cell inhibitory receptor motif of NFKB1 are required for negative signaling and for association with protein tyrosine phosphatase 1C. J Exp Med 1996, 184:295-300.
43. Olcese L, Lang P, Vely F, Cambiaggi A, Marguet D, Blery M, Hippen KL, Biassoni R, Moretta A et al.: Human and mouse killer-cell inhibitory receptors recruit PTP1C and PTP1D protein tyrosine phosphatases. J Immunol 1996, 156:4531-4534.
44. 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. Science 1995, 269:242-244. This paper demonstrates that SHP-1 associates with CD22 upon B-cell activation, and suggests that CD22 acts as a negative regulator of BCR signaling.
45. Campbell M-A, Klinman NR: Phosphotyrosine-dependent association between CD22 and protein-tyrosine phosphatase 1C. Eur J Immunol 1995, 25:1573-1579.
46. Lankester AC, Van Schijndel GMW, Van Lier RAW: Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation. J Biol Chem 1995, 270:20305-20308.
47. Law CL, Sidorenko SP, Chandran KA, Zhao Z, Shen S-H, Fischer EH, Clark EA: CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-γ1 upon B cell activation. J Exp Med 1996, 183:547-560.
48. Cyster JG, Goodnow CC: Protein tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection. Immunity 1995, 2:1-20. An elegant genetic analysis of the role of SHP-1 in setting the BCR activation threshold. The authors explored the effect of superimposing loss of SHP-1 on clonal selection and deletion in transgenic mice expressing specific B-cell receptors. They conclude that loss of SHP-1 decreases the BCR activation threshold.
49. -/- mice are hyperresponsive to BCR stimulation and that such mice exhibit a phenotype that is qualitatively similar to (although quantitatively less severe than) that of melme mice.
50. Sato S, Miller AS, Inaoki M, Bock CB, Jansen PJ, Tang LK, Tedder TF: CD22 is both a postitive and negative regulator of lymphocyte antigen receptor signal transduction: altered signaling in CD22-deficient mice. Immunity 1996, 5:551-562. See annotation [49••].
51. Lorenz U, Ravichandran KS, Burakoff SJ, Neel BG: Lack of SHPTP1 results in src-family kinase hyperactivation and thymocyte hyperresponsiveness. Proc Natl Acad Sci USA 1996, 93:9624-9629.
52. Pani G, Fischer K-D, Rascan IM, Siminovitch KA: Signaling capacity of the T cell antigen receptor is negatively regulated by the PTP1C tyrosine phosphatase. J Exp Med 1996, 184:839-852. The authors of this paper provide evidence that SHP-1 is a negative regulator of activation of thymocytes and peripheral T cells, and that SHP-1 possibly acts through CD5.
53. 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. Science 1996, 272:1173-1176. This paper suggests that SHP-1 directly binds to and inactivates ZAP-70 in T-cell lines.
54. Lorenz U, Ravichandran KS, Pei D, Walsh CT, Burakoff SJ, Neel BG: Lck-dependent tyrosyl phosphorylation of the phosphotyosine phosphatase SH-PTP1 in murine T cells. Mol Cell Biol 1994, 14:1824-1834.
55. Tarakhovsky A, Kanner SB, Hombach J, Ledbetter JA, Muller W, Killeen N, Rajewsky K: A role for CD5 in TCR-mediated signal transduction and thymocyte selection. Science 1995, 269:535-537.
56. Paulson RF, Vesely S, Siminovitch KA, Bernstein A: Signalling by the W/Kit receptor tyrosine kinase is negatively regulated in vivo by the protein tyrosine phosphatase Shp1. Nat Genet 1996, 13:309-315. See annotation [33••].
57. Yi T, Ihle JN: Association of hematopoietic cell phosphatase with c-kit after stimulation with c-kit ligand. Mol Cell Biol 1993, 13:3350-3358.
58. Perkins LA, Larsen I, Perrimon N: The Drosophila corkscrew gene encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso. Cell 1992, 70:225-236.
59. Perkins LA, Johnson MR, Melnick MB, Perrimon N: The non-receptor protein tyrosine phosphatase Corkscrew functions in multiple receptor tyrosine kinase pathways in Drosophila. Dev Biol 1997, in press. This paper provides evidence for the involvement of Corkscrew in multiple RTK pathways in Drosophila (in addition to its involvement in the Torso pathway, which was first described by these authors).
60. Allard JD, Chang HC, Herbst R, McNeill H, Simon MA: The SH2-containing tyrosine phosphatase corkscrew is required during signaling by sevenless, Ras1 and Raf. Development 1996, 122:1137-1146. This paper provides genetic evidence for the involvement of Corkscrew in Sevenless signal transduction and places Corkscrew either parallel to, or both upstream and downstream of, Ras in this pathway.
61. Herbst R, Carroll PM, Allard JD, Schilling J, Raabe T, Simon MA: Daughter of Sevenless is a substrate of the phosphotyrosine phosphatase corkscrew and functions during Sevenless signaling. Cell 1996, 85:899-909. This paper, together with [62••], provides biochemical and genetic evidence supporting the identification of Dos as a substrate for Corkscrew.
62. Raabe T, Riesgo-Escovar J, Liu X, Bausenwein BS, Deak P, Maroy P, Hafen E: DOS, a novel pleckstrin homology domain-containing protein required for signal transduction between sevenless and Ras1 in Drosophila. Cell 1996, 85:911-920. This paper reports the cloning of the dos gene, the initial characterization of the Dos protein, and the position of the Dos protein relative to Corkscrew in the Sevenless pathway.
63. Milarski KL, Saltiel AR: Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin. J Biol Chem 1994, 269:21239-21243.
64. Noguchi T, Matozaki T, Horita K, Fujioka Y, Kasuga M: Role of SH-PTP2, a protein-tyrosine phosphatase with src homology 2 domains, in insulin-stimulated ras activation. Mol Cell Biol 1994, 14:6674-6682.
65. Yamauchi K, Milarski KL, Saltiel AR, Pessin JE: Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling. Proc Natl Acad Sci USA 1995, 92:664-668.
66. Bennett AM, Hausdorff SF, O'Reilly AM, Freeman RM Jr, Neel BG: Multiple requirements for SHPTP2 in epidermal growth factor-mediated cell cycle progression. Mol Cell Biol 1995, 16:1189-1202.
67. Tang TL, Freeman RM, O'Reilly AM, Neel BG, Sokol SY: The SH2-containing protein tyrosine phosphatase SH-PTP2 is required upstream of MAP kinase for early Xenopus development Cell 1995, 80:473-483. Demonstrates that vertebrate SHP-2, like Corkscrew, is required for early embryonic development.
68. Yamauchi K, Pessin JE: Epidermal growth factor-induced association of the SHPTP2 protein tyrosine phosphatase with a 115-kDa phosphotyrosine protein. J Biol Chem 1995, 270:14871-14874.
69. Yamauchi K, Ribon V, Saltiel AR, Pessin JE: Identification of the major SHPTP2-binding protein that is tyrosine-phosphorylated in response to insulin. J Biol Chem 1995, 270:17716-17722.
70. Noguchi T, Matozaki T, Fujioka Y, Yamao T, Tsuda M, Takada T, Kasuga M: Characterization of a 115-kDa protein that binds to SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in Chinese hamster ovary cells. J Biol Chem 1996, 271:27652-27658. Provides a detailed biochemical characterization of the SH PS-1 protein, whose encoding gene was later cloned by these investigators (see [71••]).
71. Fujioka Y, Matozaki T, Noguchi T, Iwamatsu A, Yamao T, Takahashi N, Tsuda M, Takada T, Kasuga M: A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion. Mol Cell Biol 1996, 16:6887-6899. Describes the purification of a novel SHP-2-binding protein/potential substrate, and also describes the molecular cloning of the gene encoding this protein.
72. Marengere LEM, Waterhouse P, Duncan GS, Mittrucker H-W, Feng G-S, Mak TW: Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4. Science 1996, 272:1170-1173. Provides evidence suggesting that SHP-2 may be a negative regulator of T-cell signaling, acting through the CTLA-4 pathway.
73. Tonks NK: Protein tyrosine phosphatases and the control of cellular signaling responses. Adv Pharmacol 1996, 36:91-119.
74. Maeda T, Wurgler-Murphy SM, Saito H: A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 1994, 369:242-245.
75. Maeda T, Tsai AY, Saito H: Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cereviasae. Mol Cell Biol 1993, 13:5409-5417.
76. Millar JB, Buck V, Wilkinson MG: Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell size at division in fission yeast. Genes Dev 1995, 9:2117-2130. Together with [15••], this paper implicates Pyp1 and Pyp2 as negative regulators of the Spc1/Sty1 pathway in S. pombe. This pathway functions in the response to cell stress and in mitotic control.
77. Wilkinson MG, Samuels M, Takeda T, Toone WM, Shieh J-C, Toda T, Millar JBA, Jones N: The Atf transcription factor is a target for the Sty1 stress-activated MAP kinase pathway in fission yeast. Genes Dev 1996, 10:2289-2301. Together with [78••], this paper provides additional details about the S. pombe Sty1/Spc1 pathway and its involvement in the regulation of multiple physiological functions.
78. Shiozaki K, Russell P: Conjugation, meiosis, and the osmotic stress response are regulated by Spc1 kinase through Atf1 transcription factor in fission yeast. Genes Dev 1996, 10:2276-2288. See annotation [77••].
79. Shifrin VI, Davis RJ, Neel BG: Phosphorylation of protein-tyrosine phosphatase PTP-1B on identical sites suggests activation of a common signaling pathway during mitosis and stress reponse in mammalian cells. J Biol Chem 1997, 272:2957-2962.