Genetic analysis of protein tyrosine phosphatases

Current Opinion in Genetics and Development

Volumn 8, Issue 1, 1998, Pages 112-126

  Van Vactor, David ^a   O'Reilly, Alana M ^b   Neel, Benjamin G ^b  

^a HARVARD MEDICAL SCHOOL   (United States)

^b H   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; MUTANT PROTEIN; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; RECEPTOR PROTEIN;

DROSOPHILA; ENZYME REGULATION; GENETIC ANALYSIS; GENETIC RECOMBINATION; HEMATOPOIESIS; HUMAN; HYPOPHYSIS; LIVER DEVELOPMENT; NERVE FIBER; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; REVIEW; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE; SIGNAL TRANSDUCTION;

EID: 0031886094     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(98)80070-1     Document Type: Article

References (143)

1. Pawson T, Bernstein A. Receptor tyrosine kinases: genetic evidence for their role in Drosophila and mouse development. Trends Genet. 6:1990;350-356.
2. Duffy JB, Perrimon N. The torso pathway in Drosophila: lessons on receptor tyrosine kinase signaling and pattern formation. Dev Biol. 166:1994;380-395.
3. Simon MA. Signal transduction during the development of the Drosophila R7 photoreceptor. Dev Biol. 166:1994;431-442.
4. Duffy JB, Perrimon N. Recent advances in understanding signal transduction pathways in worms and flies. of special interest Curr Opin Cell Biol. 8:1996;231-238 This recent review, together with [5], summarizes the state of knowledge of Drosophila and C. elegans RTK signaling pathways.
5. Perrimon N, Perkins LA. There must be 50 ways to rule the signal: the case of the Drosophila EGF receptor. of special interest Cell. 89:1997;13-16 See annotation [4].
6. Waskiewicz AJ, Cooper JA. Mitogen and stress-response pathways - MAP kinase cascades and phosphatase regulation in mammals and yeast. Curr Opin Cell Biol. 7:1995;798-805.
7. Perrimon N. Signalling pathways initiated by receptor tyrosine kinases in Drosophila. Curr Opin Cell Biol. 6:1994;260-266.
8. Stemberg PW, Lesa G, Lee J, Katz WS, Yoon C, Clandinin TR, Huang LS, Chamberlin HM, Jongeward G. Let-23-mediated signal transduction during Caenorhabditis elegans development. Mol Reprod Dev. 42:1995;523-528.
9. Denu JE, Stuckey JA, Saper MA, Dixon JE. Form and function in protein dephosphorylation. of outstanding interest Cell. 87:1996;361-364 This review, together with [10-12] reviews recent data on the biochemistry and structure of PTPs and their implications for signal transduction studies.
10. Tonks NK, Neel BG. From form to function: signaling by protein tyrosine phosphatases. of outstanding interest Cell. 87:1996;365-368 See annotation [9].
11. Streuli M. Protein tyrosine phosphatases in signaling. of outstanding interest Curr Opin Cell Biol. 8:1996;182-188 See annotation [9].
12. Neel BG, Tonks NK. Protein tyrosine phosphatases in signal transduction. of outstanding interest Curr Opin Cell Biol. 9:1997;193-204 See annotation [9].
13. Pulido R, Serra-Pages C, Tang M, Streuli M. The LAR/PTPd/PTPs subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTPd, and PTPs isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1. Proc Natl Acad Sci USA. 92:1995;11686-11690.
14. 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. 14:1995;2827-2838.
15. Garton AJ, Flint AJ, Tonks NK. Identification of p130cas as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. of outstanding interest Mol Cell Biol. 16:1996;6408-6418 Together with [16] this paper describes the design and use of 'substrate-trapping' mutants of PTPs. Using PTP trapping mutants, the authors show that p130cas is a specific substrate for PTP-PEST, implicating this PTP in signaling through the cytoskeleton. Analagous mutants in other PTPs have also been useful in identifying substrates (see [16]).
16. Flint AJ, Tiganis T, Barford D, Tonks NK. Development of "substrate trapping" mutants to identify physiological substrates of protein-tyrosine phosphatases. of outstanding interest Proc Natl Acad Sci USA. 94:1997;1680-1685 See annotation [15].
17. 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. 75:1993;487-493.
18. Shiozaki K, Russell P. Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast. Nature. 378:1995;739-743.
19. of special interest Zhan X-L, Deschenes RJ, Guan K-L. Differential regulation of FUS3 MAP kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase MSG5 in Saccharomyces cerevesiae. of outstanding interest Genes Dev. 11:1997;1690-1702 Describes the exquisite regulation of the S. cerevesiae FUS3 MAPK pathway by two PTPs (PTP2 and PTP3) together with the DSP MSG-5. The demonstration that a MAPK family member can be regulated independently by PTPs and DSPs here may have important implications for MAPK control in mammalian cells. Additionally, the hierarchy of regulation demonstrated here and in references [20,27] may provide a model for generation of diverse biological events through differential regulation of MAPK pathways.
20. Wurgler-Murphy SM, Maeda T, Witten EA, Saito H. Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases. of outstanding interest Mol Cell Biol. 17:1997;1289-1297 Together with [27], this paper provides a detailed analysis of the regulation of the Hog1 MAPK pathway by PTP2 and PTP3. The authors demonstrate that Hog1 is a direct substrate of PTP2 using a PTP2 'trapping' mutant, and that PTP2 and PTP3 act together to regulate tyrosyl phosphorylation of Hog1, with PTP3 playing a supportive role.
21. Tonks NK. Protein tyrosine phosphatases and the control of cellular signaling responses. Adv Pharmacol. 36:1996;91-119.
22. 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 cerevisiae. Mol Cell Biol. 13:1993;5409-5417.
23. Maeda T, Wurgler-Murphy SM, Saito H. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature. 369:1994;242-245.
24. Ota I, Varshavsky A. A yeast protein similar to bacterial two-component regulators. Science. 262:1993;566-569.
25. Maeda T, Tsai AYM, Saito H. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Science. 269:1995;554-558.
26. Posas F, Wurgler-Murphy SM, Maeda T, Witten EA, Thai TC, Saito H. Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor. of special interest Cell. 86:1996;865-875 This paper elucidates the components of the HOG1 osmoregulatory pathway, which is in turn regulated at the level of HOG1 by PTP2 and PTP3.
27. Jacoby T, Flanagan H, Faykin A, Seto AG, Mattison C, Ota I. Two protein-tyrosine phosphtases inactivate the osmotic stress response pathway in yeast by targeting the mitogen-activated protein kinase, Hog1. of special interest J Biol Chem. 272:1997;17749-17755 See annotation [20].
28. Doi K, Gartner A, Ammerer G, Errede B, Shinkawa H, Sugimoto K, Matsumoto K. MSG5, a novel protein phosphatase promotes adaptation to pheromone response in S. cerevisiae. EMBO J. 13:1994;61-70.
29. Park HD, Beeser AE, Clancy MJ, Cooper TJ. The Saccharomyces cerevisiae nitrogen starvation-induced YVH1P and PTP2P phosphatases play a role in control of sporulation. of special interest Yeast. 12:1996;1135-1151 Provides genetic evidence suggesting that PTP2 and the DSP YVH1 may regulate sporulation in response to nutrient deprivation.
30. + encode protein tyrosine phosphatases that negatively regulates mistosis. Mol Cell Biol. 12:1992;5571-5580.
31. Millar JBA, Russel P, Dixon JE, Guan KL. Negative regulation of mitosis by two functionally overlapping PTPases in fission yeast. EMBO J. 11:1992;4943-4952.
32. 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. 9:1995;2117-2130.
33. Shiozaki K, Russell P. Counteractive roles of protein phosphatase 2C (PP2C) and a MAP kinase homolog in the osmoregulation of fission yeast. EMBO J. 14:1995;492-502.
34. Shiozaki K, Russell P. Conjugation, meiosis, and the osmotic stress response are regulated by Spc1 kinase through Atf1 transcription factor in fission yeast. of outstanding interest Genes Dev. 10:1996;2276-2288 Together with [35,36], these papers provide molecular details of the regulation and actions of the S. pombe Sty1/Spc1, including the demonstration that activation of the transcription factor Atf1, which is important for recovery from environmental stress, is negatively regulated by PTPs which dephosphorylate tyrosyl phosphorylated Sty1/Spc1.
35. Degols G, Shiozaki K, Russell P. Activation and regulation of the Spc1 stress-activated protein kinase in Schizosaccharomyces pombe. of outstanding interest Mol Cell Biol. 16:1996;2870-2877 See annotation [34].
36. 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. of outstanding interest Genes Dev. 10:1996;2289-2301 See annotation [34].
37. Alessi DR, Gomez N, Moorhead G, Lewis T, Keyse SM, Cohen P. Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100 in various cell lines. Curr Biol. 5:1995;283-295.
38. 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. of special interest J Biol Chem. 272:1997;2957-2962 Provides biochemical evidence implicating the non-transmembrane PTP, PTP-1B, in mammalian stress response pathways. PTP-1B is shown to be phosphorylated in response to various cellular stresses. The same sites are phosphorylated during normal mitosis but the functional significance of these modifications remain unclear.
39. Wilson LK, Benton BM, Zhou S, Thorner J, Martin GS. The yeast immunophilin Fpr3 is a physiological substrate of the tyrosine-specific phosphoprotein phosphatase Ptp1. of special interest J Biol Chem. 270:1995;25185-25193 This paper indicates that the immunophilin Fpr3 is a target of S. cerevesiae PTP1 but the physiological significance of this remains unclear, as PTP1 knockout yeast have no apparent phenotype.
40. Millar JBA, Lenaers G, Russel P. Pyp 3 PTPase acts as mitotic inducer in fission yeast. EMBO J. 11:1992;4933-4942.
41. Van Vactor D. Protein tyrosine phosphatases in the nervous system. of outstanding interest Curr Opin Cell Biol. 1998; This recent review is focussed on PTP expression patterns in the developing vertebrate nervous system, a topic not covered by other reviews [42,49].
42. Desai CJ, Sun Q, Zinn K. Tyrosine phosphorylation and axon guidance: of mice and flies. of outstanding interest Curr Opin Neurobiol. 7:1997;70-74 This recent review is focussed on RPTPase function during axon guidance in Drosophila, and explores complex functional interactions between RPTP family members.
43. Chien CB. PY in the fly receptor-like tyrosine phosphatases in axonal pathfinding. Neuron. 16:1996;1065-1068.
44. Desai CJ, Gindhart JG Jr, Goldstein LS, Zinn K. Receptor tyrosine phosphatases are required for motor axon guidance in the Drosophila embryo. of outstanding interest Cell. 84:1996;599-609 Together with [45,46], these papers analyze the phenotype of Drosophila both singly and multiply defective for RPTPs.
45. Krueger NX, Van Vactor D, Wan HI, Gelbart WM, Goodman CS, Saito H. The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila. of outstanding interest Cell. 84:1996;611-622 See annotation [44].
46. Desai CJ, Krueger NX, Saito H, Zinn K. Competition and cooperation among receptor tyrosine phosphatases control growth cone guidance in Drosophila. of outstanding interest Development. 124:1997;1941-1952 See annotation [44].
47. Saito H. Structural diversity of eukaryotic protein tyrosine phosphatases: functional and evolutionary implications. Semin Cell Biol. 4:1993;379-387.
48. Brady-Kalnay SM, Tonks NK. Protein tyrosine phosphatases as adhesion receptors. Curr Opin Cell Biol. 7:1995;650-657.
49. Van Vactor D. Adhesion and signaling in axonal fasciculation. of outstanding interest Curr Opin Neurobiol. 1998; This review examines recent genetic data that reveals important functional roles for cell adhesion molecules and signaling proteins in axon guidance and selective axonal fasciculation.
50. Lin DM, Goodman CS. Ectopic and increased expression of fasiculin III alters motoneuron growth cone guidance. Neuron. 13:1994;507-523.
51. Van Vactor D, Sink H, Fambrough D, Tsoo R, Goodman CS. Genes that control neuromuscular specificity in Drosophila. Cell. 73:1993;1137-1153.
52. Sink H, Van Vactor D, Robinson YM, Goodman CS. Genetic analysis of neuromuscular connectivity in Drosophila: a systematic screen of the 3rd chromosome. Soc Neurosci Abs. 19:1993;235.
53. Korey C, Bascom-Slack C, Scalice D, Percival B, Van Vactor D. X-chromosome genes provide further insight into embryonic motor axon guidance. Soc Neurosci Abs. 23:1997;1956.
54. Fambrough D, Goodman CS. The Drosophila beaten path gene encodes a novel secreted protein that regulates defasciculation at motor axon choice points. of special interest Cell. 87:1996;1049-1058 See annotation [56].
55. Mushegian AR. The Drosophila beat protein is related to adhesion proteins that contain immunoglobulin domains. of special interest Curr Biol. 7:1997;336-338 See annotation [56].
56. Bazan JF, Goodman CS. Molecular structure of the Drosophila beat protein. of special interest Curr Biol. 7:1997;R338-R339 These three papers [54-56] describe proteins the biological properties of which are compatible with being ligands for RPTPs.
57. Bilwes AM, den Hertog J, Hunter T, Noel JP. Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization. of outstanding interest Nature. 382:1996;555-559 A description of the crystal structure of domain 1 of RPTPα and a suggestion of a model in which RPTPs may be negatively regulated by dimerization (and potentially, by ligand binding).
58. Hoffmann KMV, Tonks NK, Barford D. The crystal structure of domain 1 of receptor protein-tyrosine phosphatase μ of outstanding interest J Biol Chem. 272:1997;27505-27508 This paper presents the structure of domain 1 of PTPμ. In so doing, it suggests that not all RPTPs are subject to the same negative regulatory mechanism proposed by Bilwes et al. [57] for PTPα.
59. Prokop A, Landgraf M, Rushton E, Broadie K, Bate M. Presynaptic development at the Drosophila neuromuscular junction: assembly and localization of presynaptic active zones. Neuron. 17:1996;617-626.
60. Yeo TT, Yang T, Massa SM, Zhang JS, Honkaniemi J, Butcher LL, Longo FM. Deficient LAR expression decreases basal forbrain cholinergic size and hippocampal cholinergic innervation. of special interest J Neurosci Res. 47:1997;348-360 A description of abnormal innervation in LAR knockout mice, which could be consistent with defective axonal guidance. Although this analysis is restricted to a partial loss-of-function, and it stops short of identifying the developmental origin of the observed defects in innervation, this is the first indication that vertebrate neuronal connections may rely upon LAR function.
61. Schaapveld RQJ, Schepens JTG, Robinson GW, Attema J, Oerlemans FTJJ, Fransen JAM, Streuli M, Wieringa B, Henninghausen L, Hendriks WJAJ. Impaired mammary gland development and function in mice lacking LAR receptor-like tyrosine phosphatase activity. of special interest Dev Biol. 188:1996;134-146 The authors of this report describe mammary gland abnormalities in LAR knockout mice. The precise etiology of these defects are still unclear at a cellular level.
62. Uetani N, Asano M, Mizuno K, Yakura H, Iwakura Y. Targeted disruption of the murine protein tyrosine phosphatase δ (MPTPδ) results in growth retardation and behavioral abnormalities. Yakura H. Kinases and Phosphatases in Lymphocyte and Neuronal Signalling. 1997;313-314 Springer-Verlag, Tokyo.
63. Sommer L, Rao M, Anderson DJ. RPTPd and the novel protein tyrosine phosphatase RPTPj are expressed in restricted regions of the developing central nervous system. Dev Dyn. 208:1997;48-61.
64. Kaufman N, Wills Z, Van Vactor D. Drosophila Rac1 controls motor axon guidance. of special interest Development. 125:1998;453-461 This paper implicates Drosophila Rac1 in motor axon guidance, which is of interest as LAR binds a protein that has Rac exchange activity [65].
65. Debant A, Serra-Pages C, Seipel K, O'Brien S, Tang M, Park S, Streuli M. The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains. of special interest Proc Natl Acad Sci USA. 93:1996;5466-5471 The authors of this paper describe the cloning and characterization of a novel, multi-domain protein that binds to mammalian LAR.
66. Brady-Kalnay SM, Rimm DL, Tonks NK. Receptor protein tyrosine phosphatase PTPμ associates with cadherins and catenins in vivo. J Cell Biol. 130:1995;977-986.
67. Kypta RM, Su H, Reichardt LF. Association between a transmembrane protein-tyrosine phosphatase and the cadherin-catenin complex. J Cell Biol. 134:1996;1519-1529.
68. Fuchs M, Mueller T, Lerch MM, Ullrich A. Association of human protein tyrosine phosphatase κ with members of the armadillo family. J Biol Chem. 271:1996;16712-16719.
69. Iwai Y, Usui T, Hirano S, Steward R, Takeichi M, Uemura T. Axon patterning requires DN-cadherin a novel neuronal adhesion receptor, in the Drosophila CNS. Neuron. 19:1997;77-89.
70. Baum PD, Garriga G. Neuronal migrations and axon fasciculation are disrupted in ina-1 integrin mutants. Neuron. 19:1997;51-62.
71. Tian S, Zinn K. An adhesion molecule-like protein the protein interacts with and is a substrate for a Drosophila receptor-linked protein tyrosine phosphatase. J Biol Chem. 269:1994;28478-28486.
72. Fashena SJ, Zinn K. Transmembrane glycoprotein gp150 is a substrate for receptor tyrosine phosphtase DPTP10D in Drosophila cells. of outstanding interest Mol Cell Biol. 17:1997;6859-6867 This study provides biochemical evidence in favor of the suggestion that gp150 is a direct substrate for DPTP10D, as well as providing information about possible kinases that phosphorylate this RPTP.
73. Callahan CA, Muralldhar MG, Lungren SE, Scully AL, Thomas JB. Control of neuronal pathway selection by a Drosophila receptor protein-tyrosine kinase family member. Nature. 376:1995;171-174.
74. Flanagan JG, Vanderhaegen P. The Ephrins and Eph receptors in neural development. Annu Rev Neurosci. 21:1998;309-345.
75. Saffell JL, Williams EJ, Mason IJ, Walsh FS, Doherty P. Expression of a dominant negative FGF receptor inhibits axonal growth and FGF receptor. Neuron. 18:1997;231-242.
76. Perkins LA, Larsen I, Perrimon N. corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso. Cell. 70:1992;225-236.
77. Gutch MJ, Flint AJ, Keller J, Tonks NK, Hengartner MO. The Caenorhabditis elegans SH2 domain-containing protein tyrosine phosphatase PTP-2 participates in signal transduction during oogenesis, embryogenesis and vulval development. of outstanding interest Genes Dev. 1998; A description of the identification, cloning and initial characterization of the C. elegans homolog of SHP-2. PTP2 is required for signaling downstream of let23 and for normal oocyte development.
78. Neel BG. Structure and function of SH2-domain containing tyrosine phosphatases. Semin Cell Biol. 4:1993;419-432.
79. Feng GS, Pawson T. Phosphotyrosine phosphatases with SH2 domains: regulators of signal transduction. Trends Genet. 10:1994;54-58.
80. 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. 180:1996;63-81 This report provides genetic evidence for the participation of Drosophila corkscrew in multiple RTK signaling pathways. Moreover, genetic analysis indicates that Csw mutants are less severely defective than null mutants in the respective RTK, arguing that Csw is required to set the full 'gain' through the pathway but not for some basal level of RTK signaling.
81. Bignon JS, Siminovitch KA. Identification of PTP1C mutation as a genetic defect in motheaten and viable motheaten mice: a step toward defining the roles of protein tyrosine phosphatases in the regulation of hemopoietic cell differentiation and function. Clin Immunol Immunopathol. 73:1994;168-179.
82. Scharenberg A, Kinet J. The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP? of outstanding interest Cell. 87:1996;961-964 Together with [83,84] this review covers various aspects of signaling involving SHP-1.
83. Neel BG. Role of phosphatases in lymphocyte activation. of outstanding interest Curr Opin Immunol. 9:1997;405-420 See annotation [82].
84. Burshtyn DN, Long EO. Regulation through inhibitory receptors: lessons from natural killer cells. of outstanding interest Trends Cell Biol. 1997; See annotation [82].
85. 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. of outstanding interest Development. 122:1996;1137-1146 Provides genetic evidence that Csw regulates Sevenless signaling and argues that Csw must exist either both upstream and downstream of Raf or lie in a parallel pathway.
86. Huang LS, Tzou P, Sternberg PW. The lin-15 locus encodes two negative regulators of Caenorhabditis elegans vulval development. Mol Biol Cell. 5:1994;395-411.
87. Carraway KLR, Cantley LC. A new acquaitance for erbB3 and erbB4: a role for receptor heterodimerization in growth signaling. Cell. 78:1994;5-8.
88. 2+-induced regulation of ion channel and MAP kinase functions. Nature. 376:1995;737-745.
89. Rosen LB, Greenberg ME. Stimulation of growth factor receptor signal transduction by activation of voltage-sensitive calcium channels. Proc Natl Acad Sci USA. 93:1996;1113-1118.
90. Van Biesen T, Hawes BE, Luttrell DK, Krueger KM, Touhara K, Porfiri E, Sakaue M, Luttrell LM, Lefkowitz RJ. Receptor-tyrosine kinase and G beta gamma-mediated MAP kinase activation by a common signalling pathway. Nature. 376:1995;781-784.
91. Dikic I, Tokiwa G, Lev S, Courtneidge SA, Schlessinger J. A role for Pyk2 and Src in linking G-coupled receptors with MAP kinase activation. Nature. 383:1996;547-550.
92. Daub H, Weiss FU, Wallasch C, Ullrich A. Role of transactivation of the EGF receptor in signalling by G-protein coupled receptors. Nature. 379:1996;557-560.
93. Yamauchi T, Ueki K, Tobe K, Tamemoto H, Sekine N, Wada M, Honjo M, Takahashi M, Takahashi T, Hirai H, et al. Tyrosine phosphorylation of the EGF receptor by the kinase Jak2 is induced by growth hormone. Nature. 390:1997;91-96.
94. 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. 80:1995;473-483.
95. -/- mice and characterization of insulin signaling in several tissues from heterozygotic animals.
96. -/- mice. (See main text for details.).
97. O'Reilly AM, Neel BG. Structural determinants of SHP-2 function and specificity in Xenopus mesoderm induction. of special interest Mol Cell Biol. 18:1998;161-177 This paper describes which domains of SHP-2 are required for its functions in early Xenopus development and furthermore shows that the PTP domains of the SHPs are essential for conferring specificity in vivo.
98. Pei D, Neel BG, Walsh CT. Overexpression, purification, and characterization of Src homology 2-containing protein tyrosine phosphatase. Proc Natl Acad Sci USA. 90:1993;1092-1096.
99. Townley R, Shen S-H, Banville D, Ramachandran C. Inhibition of the activity of protein tyrosine phosphatase 1C by its SH2 domains. Biochemistry. 32:1993;13414-13418.
100. Pei D, Lorenz U, Klingmuller U, Neel BG, Walsh CT. Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains. Biochemistry. 33:1994;15483-15493.
101. Dechert U, Adam M, Harder KW, Clark-Lewis I, Jirik F. Characterization of protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of SH2 domains. J Biol Chem. 269:1994;5602-5611.
102. Zhao Z, Larocque R, Ho WT, Fischer EH, Shen SH. Purification and characterization of PTP2C, a widely distributed protein tyrosine phosphatase containing two SH2 domains. J Biol Chem. 269:1994;8780-8785.
103. Zhao Z, Bouchard P, Diltz CD, Shen S, Fischer EH. Purification and characterization of a protein tyrosine phosphatase containing SH2 domains. J Biol Chem. 268:1993;2816-2820.
104. Sugimoto S, Wandless TJ, Shoelson SE, Neel BG, Walsh CT. Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine containing peptides derived from insulin receptor substrate-1. J Biol Chem. 268:1993;2733-2736.
105. -/- embryonal stem cells exhibit markedly defective hematopoietic differentiation.
106. 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. of outstanding interest Cell. 85:1996;899-909 This paper together with [107], provide biochemical and genetic evidence that DOS is a biologically relevant in vivo substrate for SHP-2.
107. 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. of outstanding interest Cell. 85:1996;911-920 See annotation [106].
108. Sun XJ, Pons S, Asano T, Myers MGJ, Glasheen E, White MF. The Fyn tyrosine kinase binds IRS-1 and forms a distinct signaling complex during insulin stimulation. J Biol Chem. 271:1996;10583-10587.
109. Mastick CC, Brady MJ, Saltiel AR. Insulin stimulates the tyrosine phosphorylation of caveolin. J Cell Biol. 129:1995;1523-1531.
110. Peng ZY, Cartwright CA. Regulation of the Src tyrosine kinase and Syp tyrosine phosphatase by their cellular association. Oncogene. 11:1995;1955-1962.
111. Takahashi F, Endo S, Kojima T, Saigo K. Regulation of cell-cell contacts in developing Drosophila eyes by Dsrc41, a new, close relative of vertebrate c-src. Genes Dev. 10:1996;1645-1656.
112. Cooper JA, Simon MA, Kussick SJ. Signaling by ectopically expressed Drosophila Src64 requires the protein-tyrosine-phosphatase corkscrew and the adapter downstream of receptor kinases. of special interest Cell Growth Differ. 7:1996;1435-1441 This paper provides genetic evidence suggesting that Csw may be downstream of c-Src.
113. Cleghon V, Gayko U, Copeland TD, Perkins LA, Perrimon N, Morrison DK. Drosophila terminal structure development is regulated by the compensatory activities of positive and gegative phosphotyrosine signaling sites on the Torso RTK. of outstanding interest Genes Dev. 10:1996;566-577 This paper shows that two different sites on the Torso RTK have mutually antagonistic signaling effects, and suggests that Csw (and by inference, SHP-2) may act to release an inhibitory molecule from RTKs to which it binds.
114. Klinghoffer RA, Kazlauskas A. Identification of a putative Syp substrate, the PDGFB receptor. J Biol Chem. 270:1995;22208-22217.
115. Rivard N, McKenzie FR, Brondello J-M, Pouyssegur J. The phosphotyrosine phosphatase PTP1D, but not PTP1C, is an essential mediator of fibroblast proliferation induced by tyrosine kinase and G protein-coupled receptors. J Biol Chem. 270:1995;11017-11024.
116. Bennett AM, Hausdorff SF, O'Reilly AM, Freeman RM Jr, Neel BG. Multiple requirements for SH-PTP2 in epidermal growth factor-mediated cell cycle progression. Mol Cell Biol. 16:1996;1189-1202.
117. Roche S, McGlade J, Jones M, Gish GD, Pawson T, Courtneidge SA. Requirement of phospholipase C gamma, the tyrosine phosphatase Syp and the adaptor proteins Shc and Nck for PDGF-induced DNA synthesis: evidence for the existence of Ras-dependent and Ras-independent pathways. EMBO J. 15:1996;4940-4948.
118. 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. 14:1994;6674-6682.
119. 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. 269:1994;21239-21243.
120. 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. 270:1995;17716-17722.
121. 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. of outstanding interest Mol Cell Biol. 16:1996;6887-6899 This is the first paper describing the purification, cloning and initial characterization of SHPS-1, a member of the SIRP family.
122. Kharitonenkov A, Chen Z, Sures I, Wang H, Schilling J, Ullrich A. A family of proteins that inhibit signaling though tyrosine kinase receptors. of outstanding interest Nature. 386:1997;181-186 This paper also describes the cloning of SHPS-1/SIRP1α (see [121]) along with the demonstration that this protein is part of a gene family and over-expression data that suggest that SIRPs may be signal-inhibitory receptors.
123. Ohnishi H, Kubota M, Ohtake A, Sato K, Sano S. Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule. of special interest J Biol Chem. 271:1996;25569-25574 A third paper (see [121,122]) describing the cloning of a SIRP family member.
124. Miyamoto S, Teramoto H, Coso OA, Gutkind JS, Burbelo PD, Akiyama SK, Yamada KM. Integrin function: molecular heirarchies of cytoskeletal and signaling molecules. J Cell Biol. 131:1995;791-805.
125. Vuori K, Rusolahti E. Association of insulin receptor substrate-1 with integrins. Science. 266:1994;1576-1578.
126. Xiao S, Rose DW, Sasaoka T, Maegawa H, Burke TRJ, Roller PP, Shoelson SE, Olefsky JM. Syp (SH-PTP2) is a positive mediator of growth factor-stimulated mitogenic signal transduction. J Biol Chem. 269:1994;21244-21248.
127. 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. 92:1995;664-668.
128. Yamauchi K, Pessin JE. Epidermal growth factor-induced association of the SHPTP2 protein tyrosine phosphatase with a 115-kDa phosphotyrosine protein. J Biol Chem. 270:1995;14871-14874.
129. Grammer TC, Blenis J. Evidence for MEK-independent pathways regulating the prolonged activation of the ERK-MAP kinases. Oncogene. 14:1997;1635-1642.
130. Duckworth BC, Cantley LC. Conditional inhibition of the mitogen-activated protein kinase cascade by wortmannin. J Biol Chem. 272:1997;27665-27670.
131. 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. of outstanding interest Science. 272:1996;1170-1173 Provides evidence that SHP-2 may be a negative regulator of T cell signaling, acting on the CTLA-4 pathway.
132. Symes A, Stahl N, Reeves SA, Farruggela T, Servidel T, Gearan T, Yancopoulos G, Fink JS. The protein tyrosine phosphatase SHP-2 negatively regulates cilliary neurotrophic factor induction of gene expression. of outstanding interest Curr Biol. 7:1997;687-700 Provides evidence that SHP-2 may act as a negative regulatory of gp130-linked signaling pathways.
133. Boulton TG, Stahl N, Yancopoulos GD. Ciliary neurotrphic factor/leukemia inhibitory factor/interleukin 6/oncostatin M family of cytokines induces tyrosine phosphorylation of a common set of proteins overlapping those induced
134. David M, Zhou G, Pine R, Dixon JE, Larner AC. The SH2 domain-containing tyrosine phosphatase PTP1D is required for interferon alpha/beta-induced gene expression. of outstanding interest J Biol Chem. 271:1996;15862-15865 This paper, together with [135-137] provide evidence that SHP-2 plays a positive role in several cytokine signaling pathways, acting upstream of both the MAPK and STAT pathways.
135. Tauchi T, Damen JE, Toyama K, Feng G-S, Broxmeyer HE, Krystal G. Tyrosine 425 within the activated erythropoietin receptor binds syp, reduces the erythropoietin required for syp tyrosine phosphorylation, and promotes mitogenesis. of outstanding interest Blood. 87:1996;4495-4501 See annotation [134].
136. Ali S, Chen Z, Lebrun J-J, Vogel W, Kharitonenkov A, Kelly Pa, Ullrich A. PTP1D is a positive regulator of the prolactin signal leading to β-casein promoter activation. of outstanding interest EMBO J. 15:1996;135-142 See annotation [134].
137. Pazdrak K, Adachi T, Alam R. Src homology 2 protein tyrosine phosphatase (SHPTP2)/Src homology 2 phosphatase 2 (SHP2) tyrosine phosphatase is a positive regulator of the interleukin 5 receptor signal transduction pathways leading to prolongation of eosinophil survival. of outstanding interest J Exp Med. 186:1997;561-568 See annotation [134].
138. Tenev T, Keilhack H, Tomic S, Stoyanov B, Stein-Gerlach M, Lammers R, Krivtsov AV, Ullrich A, Bohmer FD. Both SH2 domains are involved in interaction of SHP-1 with the epidermal growth factor receptor but cannot confer receptor-directed activity to SHP-1/SHP-2 chimera. J Biol Chem. 272:1997;5966-5973.
139. Songyang Z, Shoelson SE, Chaudhuri M, Gish G, Pawson T, Haser WG, King F, Roberts T, Ratnofsky S, Lechleider RJ, et al. SH2 domains recognize specific phosphopeptide sequences. Cell. 72:1993;767-778.
140. Songyang Z, Shoelson SE, McGlade J, Olivier P, Pawson T, Bustelo XR, Barbacid M, Sabe H, Hanafusa H, Yi T, et al. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fes/fps, GRB-2, HCP, SHC, Syk, and vav. Mol Cell Biol. 14:1994;2777-2785.
141. Huyer G, Li ZM, Adam M, Huckle WR, Ramachandran C. Direct determination of the sequence recognition requirements of the SH2 domains of SH-PTP2. Biochemistry. 34:1995;1040-1049.
142. Burshtyn DN, Yang W, Yi T, Long EO. A novel phosphotyrosine motif with a critical amino acid at position -2 for the SH2 domain-mediated activation of the tyrosine phosphatase SHP-1. J Biol Chem. 272:1997;13066-13072.
143. You-Ten KE, Muise ES, Itie A, Michaliszyn E, Wagner J, Jothy S, Lapp WS, Tremblay ML. Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice. of outstanding interest J Exp Med. 186:1997;683-693 This paper describes the phenotype of TC-PTP-deficient mice. The mice have multiple hematopoeiticand immune system defects, demonstrating the important role of this PTP in vivo.