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. 1996 Nov;16(11):5955–5963. doi: 10.1128/mcb.16.11.5955

Involvement of the protein tyrosine phosphatase SHP-1 in Ras-mediated activation of the mitogen-activated protein kinase pathway.

S Krautwald 1, D Büscher 1, V Kummer 1, S Buder 1, M Baccarini 1
PMCID: PMC231598  PMID: 8887625

Abstract

Ubiquitously expressed SH2-containing tyrosine phosphatases interact physically with tyrosine kinase receptors or their substrates and relay positive mitogenic signals via the activation of the Ras-mitogen-activated protein kinase (MAPK) pathway. Conversely, the structurally related phosphatase SHP-1 is predominantly expressed in hemopoietic cells and becomes tyrosine phosphorylated upon colony-stimulating factor 1 treatment of macrophages without associating with the colony-stimulating factor 1 receptor tyrosine kinase. Mice lacking functional SHP-1 (me/me and me(v)/me(v)) develop systemic autoimmune disease with accumulation of macrophages, suggesting that SHP-1 may be a negative regulator of hemopoietic cell growth. By using macrophages expressing dominant negative Ras and the me(v)/me(v) mouse mutant, we show that SHP-1 is activated in the course of mitogenic signal transduction in a Ras-dependent manner and that its activity is necessary for the Ras-dependent activation of the MAPK pathway but not of the Raf-1 kinase. Consistent with a role for SHP-1 as an intermediate between Ras and the MEK-MAPK pathway, Ras-independent activation of the latter kinases by bacterial lipopolysaccharide occurred normally in me(v)/me(v) cells. Our results sharply accentuate the diversity of signal transduction in mammalian cells, in which the same signaling intermediates can be rearranged to form different pathways.

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Selected References

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  1. Alessi D. R., Cohen P., Ashworth A., Cowley S., Leevers S. J., Marshall C. J. Assay and expression of mitogen-activated protein kinase, MAP kinase kinase, and Raf. Methods Enzymol. 1995;255:279–290. doi: 10.1016/s0076-6879(95)55031-3. [DOI] [PubMed] [Google Scholar]
  2. Avruch J., Zhang X. F., Kyriakis J. M. Raf meets Ras: completing the framework of a signal transduction pathway. Trends Biochem Sci. 1994 Jul;19(7):279–283. doi: 10.1016/0968-0004(94)90005-1. [DOI] [PubMed] [Google Scholar]
  3. Baccarini M., Li W., Dello Sbarba P., Stanley E. R. Increased phosphorylation of the colony stimulating factor-1 receptor following transmembrane signaling. Receptor. 1991;1(4):243–259. [PubMed] [Google Scholar]
  4. Baccarini M., Sabatini D. M., App H., Rapp U. R., Stanley E. R. Colony stimulating factor-1 (CSF-1) stimulates temperature dependent phosphorylation and activation of the RAF-1 proto-oncogene product. EMBO J. 1990 Nov;9(11):3649–3657. doi: 10.1002/j.1460-2075.1990.tb07576.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bignon J. S., Siminovitch K. A. Identification of PTP1C mutation as the 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. 1994 Nov;73(2):168–179. doi: 10.1006/clin.1994.1185. [DOI] [PubMed] [Google Scholar]
  6. Binari R., Perrimon N. Stripe-specific regulation of pair-rule genes by hopscotch, a putative Jak family tyrosine kinase in Drosophila. Genes Dev. 1994 Feb 1;8(3):300–312. doi: 10.1101/gad.8.3.300. [DOI] [PubMed] [Google Scholar]
  7. Blenis J. Signal transduction via the MAP kinases: proceed at your own RSK. Proc Natl Acad Sci U S A. 1993 Jul 1;90(13):5889–5892. doi: 10.1073/pnas.90.13.5889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Büscher D., Dello Sbarba P., Hipskind R. A., Rapp U. R., Stanley E. R., Baccarini M. v-raf confers CSF-1 independent growth to a macrophage cell line and leads to immediate early gene expression without MAP-kinase activation. Oncogene. 1993 Dec;8(12):3323–3332. [PubMed] [Google Scholar]
  9. Büscher D., Hipskind R. A., Krautwald S., Reimann T., Baccarini M. Ras-dependent and -independent pathways target the mitogen-activated protein kinase network in macrophages. Mol Cell Biol. 1995 Jan;15(1):466–475. doi: 10.1128/mcb.15.1.466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Cai H., Szeberényi J., Cooper G. M. Effect of a dominant inhibitory Ha-ras mutation on mitogenic signal transduction in NIH 3T3 cells. Mol Cell Biol. 1990 Oct;10(10):5314–5323. doi: 10.1128/mcb.10.10.5314. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Catling A. D., Reuter C. W., Cox M. E., Parsons S. J., Weber M. J. Partial purification of a mitogen-activated protein kinase kinase activator from bovine brain. Identification as B-Raf or a B-Raf-associated activity. J Biol Chem. 1994 Nov 25;269(47):30014–30021. [PubMed] [Google Scholar]
  12. Chao T. S., Byron K. L., Lee K. M., Villereal M., Rosner M. R. Activation of MAP kinases by calcium-dependent and calcium-independent pathways. Stimulation by thapsigargin and epidermal growth factor. J Biol Chem. 1992 Oct 5;267(28):19876–19883. [PubMed] [Google Scholar]
  13. Chao T. S., Foster D. A., Rapp U. R., Rosner M. R. Differential Raf requirement for activation of mitogen-activated protein kinase by growth factors, phorbol esters, and calcium. J Biol Chem. 1994 Mar 11;269(10):7337–7341. [PubMed] [Google Scholar]
  14. Chen H. E., Chang S., Trub T., Neel B. G. Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol Cell Biol. 1996 Jul;16(7):3685–3697. doi: 10.1128/mcb.16.7.3685. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Chen J., Martin B. L., Brautigan D. L. Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation. Science. 1992 Aug 28;257(5074):1261–1264. doi: 10.1126/science.1325671. [DOI] [PubMed] [Google Scholar]
  16. Courtneidge S. A., Dhand R., Pilat D., Twamley G. M., Waterfield M. D., Roussel M. F. Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor. EMBO J. 1993 Mar;12(3):943–950. doi: 10.1002/j.1460-2075.1993.tb05735.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Cyster J. G., Goodnow C. C. Protein tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection. Immunity. 1995 Jan;2(1):13–24. doi: 10.1016/1074-7613(95)90075-6. [DOI] [PubMed] [Google Scholar]
  18. D'Ambrosio D., Hippen K. L., Minskoff S. A., Mellman I., Pani G., Siminovitch K. A., Cambier J. C. Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RIIB1. Science. 1995 Apr 14;268(5208):293–297. doi: 10.1126/science.7716523. [DOI] [PubMed] [Google Scholar]
  19. David M., Chen H. E., Goelz S., Larner A. C., Neel B. G. Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol Cell Biol. 1995 Dec;15(12):7050–7058. doi: 10.1128/mcb.15.12.7050. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Decker T., Lohmann-Matthes M. L., Baccarini M. Heterogeneous activity of immature and mature cells of the murine monocyte-macrophage lineage derived from different anatomical districts against yeast-phase Candida albicans. Infect Immun. 1986 Nov;54(2):477–486. doi: 10.1128/iai.54.2.477-486.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Doody G. M., Justement L. B., Delibrias C. C., Matthews R. J., Lin J., Thomas M. L., Fearon D. T. A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP. Science. 1995 Jul 14;269(5221):242–244. doi: 10.1126/science.7618087. [DOI] [PubMed] [Google Scholar]
  22. Egan S. E., Weinberg R. A. The pathway to signal achievement. Nature. 1993 Oct 28;365(6449):781–783. doi: 10.1038/365781a0. [DOI] [PubMed] [Google Scholar]
  23. Farnsworth C. L., Feig L. A. Dominant inhibitory mutations in the Mg(2+)-binding site of RasH prevent its activation by GTP. Mol Cell Biol. 1991 Oct;11(10):4822–4829. doi: 10.1128/mcb.11.10.4822. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Feig L. A., Cooper G. M. Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP. Mol Cell Biol. 1988 Aug;8(8):3235–3243. doi: 10.1128/mcb.8.8.3235. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Feng G. S., Pawson T. Phosphotyrosine phosphatases with SH2 domains: regulators of signal transduction. Trends Genet. 1994 Feb;10(2):54–58. doi: 10.1016/0168-9525(94)90149-x. [DOI] [PubMed] [Google Scholar]
  26. Gallego C., Gupta S. K., Heasley L. E., Qian N. X., Johnson G. L. Mitogen-activated protein kinase activation resulting from selective oncogene expression in NIH 3T3 and rat 1a cells. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7355–7359. doi: 10.1073/pnas.89.16.7355. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Hanratty W. P., Dearolf C. R. The Drosophila Tumorous-lethal hematopoietic oncogene is a dominant mutation in the hopscotch locus. Mol Gen Genet. 1993 Apr;238(1-2):33–37. doi: 10.1007/BF00279527. [DOI] [PubMed] [Google Scholar]
  28. Harrison D. A., Binari R., Nahreini T. S., Gilman M., Perrimon N. Activation of a Drosophila Janus kinase (JAK) causes hematopoietic neoplasia and developmental defects. EMBO J. 1995 Jun 15;14(12):2857–2865. doi: 10.1002/j.1460-2075.1995.tb07285.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Hibi S., Löhler J., Friel J., Stocking C., Ostertag W. Induction of monocytic differentiation and tumorigenicity by v-Ha-ras in differentiation arrested hematopoietic cells. Blood. 1993 Apr 1;81(7):1841–1848. [PubMed] [Google Scholar]
  30. Hipskind R. A., Büscher D., Nordheim A., Baccarini M. Ras/MAP kinase-dependent and -independent signaling pathways target distinct ternary complex factors. Genes Dev. 1994 Aug 1;8(15):1803–1816. doi: 10.1101/gad.8.15.1803. [DOI] [PubMed] [Google Scholar]
  31. Hofer F., Fields S., Schneider C., Martin G. S. Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator. Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):11089–11093. doi: 10.1073/pnas.91.23.11089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Jaiswal R. K., Moodie S. A., Wolfman A., Landreth G. E. The mitogen-activated protein kinase cascade is activated by B-Raf in response to nerve growth factor through interaction with p21ras. Mol Cell Biol. 1994 Oct;14(10):6944–6953. doi: 10.1128/mcb.14.10.6944. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Jin D. I., Jameson S. B., Reddy M. A., Schenkman D., Ostrowski M. C. Alterations in differentiation and behavior of monocytic phagocytes in transgenic mice that express dominant suppressors of ras signaling. Mol Cell Biol. 1995 Feb;15(2):693–703. doi: 10.1128/mcb.15.2.693. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Kazlauskas A., Feng G. S., Pawson T., Valius M. The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp. Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):6939–6943. doi: 10.1073/pnas.90.15.6939. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Kikuchi A., Demo S. D., Ye Z. H., Chen Y. W., Williams L. T. ralGDS family members interact with the effector loop of ras p21. Mol Cell Biol. 1994 Nov;14(11):7483–7491. doi: 10.1128/mcb.14.11.7483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Kikuchi A., Williams L. T. Regulation of interaction of ras p21 with RalGDS and Raf-1 by cyclic AMP-dependent protein kinase. J Biol Chem. 1996 Jan 5;271(1):588–594. doi: 10.1074/jbc.271.1.588. [DOI] [PubMed] [Google Scholar]
  37. Klingmüller U., Lorenz U., Cantley L. C., Neel B. G., Lodish H. F. Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signals. Cell. 1995 Mar 10;80(5):729–738. doi: 10.1016/0092-8674(95)90351-8. [DOI] [PubMed] [Google Scholar]
  38. Kon-Kozlowski M., Pani G., Pawson T., Siminovitch K. A. The tyrosine phosphatase PTP1C associates with Vav, Grb2, and mSos1 in hematopoietic cells. J Biol Chem. 1996 Feb 16;271(7):3856–3862. doi: 10.1074/jbc.271.7.3856. [DOI] [PubMed] [Google Scholar]
  39. Krautwald S., Baccarini M. Bacterially expressed murine CSF-1 possesses agonistic activity in its monomeric form. Biochem Biophys Res Commun. 1993 Apr 30;192(2):720–727. doi: 10.1006/bbrc.1993.1474. [DOI] [PubMed] [Google Scholar]
  40. Krautwald S., Büscher D., Dent P., Ruthenberg K., Baccarini M. Suppression of growth factor-mediated MAP kinase activation by v-raf in macrophages: a putative role for the MKP-1 phosphatase. Oncogene. 1995 Mar 16;10(6):1187–1192. [PubMed] [Google Scholar]
  41. Kuhné M. R., Pawson T., Lienhard G. E., Feng G. S. The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J Biol Chem. 1993 Jun 5;268(16):11479–11481. [PubMed] [Google Scholar]
  42. Lange-Carter C. A., Johnson G. L. Ras-dependent growth factor regulation of MEK kinase in PC12 cells. Science. 1994 Sep 2;265(5177):1458–1461. doi: 10.1126/science.8073291. [DOI] [PubMed] [Google Scholar]
  43. Lange-Carter C. A., Pleiman C. M., Gardner A. M., Blumer K. J., Johnson G. L. A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf. Science. 1993 Apr 16;260(5106):315–319. doi: 10.1126/science.8385802. [DOI] [PubMed] [Google Scholar]
  44. Lankester A. C., van Schijndel G. M., van Lier R. A. Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation. J Biol Chem. 1995 Sep 1;270(35):20305–20308. doi: 10.1074/jbc.270.35.20305. [DOI] [PubMed] [Google Scholar]
  45. Lechleider R. J., Sugimoto S., Bennett A. M., Kashishian A. S., Cooper J. A., Shoelson S. E., Walsh C. T., Neel B. G. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor. J Biol Chem. 1993 Oct 15;268(29):21478–21481. [PubMed] [Google Scholar]
  46. Li W., Nishimura R., Kashishian A., Batzer A. G., Kim W. J., Cooper J. A., Schlessinger J. A new function for a phosphotyrosine phosphatase: linking GRB2-Sos to a receptor tyrosine kinase. Mol Cell Biol. 1994 Jan;14(1):509–517. doi: 10.1128/mcb.14.1.509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Lioubin M. N., Algate P. A., Tsai S., Carlberg K., Aebersold A., Rohrschneider L. R. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev. 1996 May 1;10(9):1084–1095. doi: 10.1101/gad.10.9.1084. [DOI] [PubMed] [Google Scholar]
  48. Lioubin M. N., Myles G. M., Carlberg K., Bowtell D., Rohrschneider L. R. Shc, Grb2, Sos1, and a 150-kilodalton tyrosine-phosphorylated protein form complexes with Fms in hematopoietic cells. Mol Cell Biol. 1994 Sep;14(9):5682–5691. doi: 10.1128/mcb.14.9.5682. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Luo H., Hanratty W. P., Dearolf C. R. An amino acid substitution in the Drosophila hopTum-l Jak kinase causes leukemia-like hematopoietic defects. EMBO J. 1995 Apr 3;14(7):1412–1420. doi: 10.1002/j.1460-2075.1995.tb07127.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Medema R. H., de Laat W. L., Martin G. A., McCormick F., Bos J. L. GTPase-activating protein SH2-SH3 domains induce gene expression in a Ras-dependent fashion. Mol Cell Biol. 1992 Aug;12(8):3425–3430. doi: 10.1128/mcb.12.8.3425. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Milarski K. L., Saltiel A. R. Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin. J Biol Chem. 1994 Aug 19;269(33):21239–21243. [PubMed] [Google Scholar]
  52. Morgan C., Pollard J. W., Stanley E. R. Isolation and characterization of a cloned growth factor dependent macrophage cell line, BAC1.2F5. J Cell Physiol. 1987 Mar;130(3):420–427. doi: 10.1002/jcp.1041300316. [DOI] [PubMed] [Google Scholar]
  53. 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 Oct;14(10):6674–6682. doi: 10.1128/mcb.14.10.6674. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Pagès G., Lenormand P., L'Allemain G., Chambard J. C., Meloche S., Pouysségur J. Mitogen-activated protein kinases p42mapk and p44mapk are required for fibroblast proliferation. Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8319–8323. doi: 10.1073/pnas.90.18.8319. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Pani G., Kozlowski M., Cambier J. C., Mills G. B., Siminovitch K. A. Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signaling. J Exp Med. 1995 Jun 1;181(6):2077–2084. doi: 10.1084/jem.181.6.2077. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Perkins L. A., 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. 1992 Jul 24;70(2):225–236. doi: 10.1016/0092-8674(92)90098-w. [DOI] [PubMed] [Google Scholar]
  57. Polakis P., McCormick F. Structural requirements for the interaction of p21ras with GAP, exchange factors, and its biological effector target. J Biol Chem. 1993 May 5;268(13):9157–9160. [PubMed] [Google Scholar]
  58. Reuter C. W., Catling A. D., Jelinek T., Weber M. J. Biochemical analysis of MEK activation in NIH3T3 fibroblasts. Identification of B-Raf and other activators. J Biol Chem. 1995 Mar 31;270(13):7644–7655. doi: 10.1074/jbc.270.13.7644. [DOI] [PubMed] [Google Scholar]
  59. Rodriguez-Viciana P., Warne P. H., Dhand R., Vanhaesebroeck B., Gout I., Fry M. J., Waterfield M. D., Downward J. Phosphatidylinositol-3-OH kinase as a direct target of Ras. Nature. 1994 Aug 18;370(6490):527–532. doi: 10.1038/370527a0. [DOI] [PubMed] [Google Scholar]
  60. Samuels M. L., Weber M. J., Bishop J. M., McMahon M. Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human raf-1 protein kinase. Mol Cell Biol. 1993 Oct;13(10):6241–6252. doi: 10.1128/mcb.13.10.6241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Sawada T., Milarski K. L., Saltiel A. R. Expression of a catalytically inert Syp blocks activation of MAP kinase pathway downstream of p21ras. Biochem Biophys Res Commun. 1995 Sep 14;214(2):737–743. doi: 10.1006/bbrc.1995.2347. [DOI] [PubMed] [Google Scholar]
  62. Schultz A. M., Copeland T. D., Mark G. E., Rapp U. R., Oroszlan S. Detection of the myristylated gag-raf transforming protein with raf-specific antipeptide sera. Virology. 1985 Oct 15;146(1):78–89. doi: 10.1016/0042-6822(85)90054-6. [DOI] [PubMed] [Google Scholar]
  63. Shultz L. D. Pleiotropic effects of deleterious alleles at the "motheaten" locus. Curr Top Microbiol Immunol. 1988;137:216–222. doi: 10.1007/978-3-642-50059-6_32. [DOI] [PubMed] [Google Scholar]
  64. Shultz L. D., Schweitzer P. A., Rajan T. V., Yi T., Ihle J. N., Matthews R. J., Thomas M. L., Beier D. R. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell. 1993 Jul 2;73(7):1445–1454. doi: 10.1016/0092-8674(93)90369-2. [DOI] [PubMed] [Google Scholar]
  65. Skorski T., Szczylik C., Ratajczak M. Z., Malaguarnera L., Gewirtz A. M., Calabretta B. Growth factor-dependent inhibition of normal hematopoiesis by N-ras antisense oligodeoxynucleotides. J Exp Med. 1992 Mar 1;175(3):743–750. doi: 10.1084/jem.175.3.743. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Smith M. R., Ramsburg E. A., Kung H. F., Durum S. K. Components of the protein kinase C pathway induce Ia expression after injection into macrophages. J Immunol. 1992 Aug 15;149(4):1304–1310. [PubMed] [Google Scholar]
  67. Spaargaren M., Bischoff J. R. Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12609–12613. doi: 10.1073/pnas.91.26.12609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Stanley E. R. The macrophage colony-stimulating factor, CSF-1. Methods Enzymol. 1985;116:564–587. doi: 10.1016/s0076-6879(85)16044-1. [DOI] [PubMed] [Google Scholar]
  69. Su L., Zhao Z., Bouchard P., Banville D., Fischer E. H., Krebs E. G., Shen S. H. Positive effect of overexpressed protein-tyrosine phosphatase PTP1C on mitogen-activated signaling in 293 cells. J Biol Chem. 1996 Apr 26;271(17):10385–10390. doi: 10.1074/jbc.271.17.10385. [DOI] [PubMed] [Google Scholar]
  70. Sun H., Tonks N. K. The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. Trends Biochem Sci. 1994 Nov;19(11):480–485. doi: 10.1016/0968-0004(94)90134-1. [DOI] [PubMed] [Google Scholar]
  71. Tang T. L., Freeman R. M., Jr, O'Reilly A. M., Neel B. G., Sokol S. Y. The SH2-containing protein-tyrosine phosphatase SH-PTP2 is required upstream of MAP kinase for early Xenopus development. Cell. 1995 Feb 10;80(3):473–483. doi: 10.1016/0092-8674(95)90498-0. [DOI] [PubMed] [Google Scholar]
  72. Tsui H. W., Siminovitch K. A., de Souza L., Tsui F. W. Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nat Genet. 1993 Jun;4(2):124–129. doi: 10.1038/ng0693-124. [DOI] [PubMed] [Google Scholar]
  73. Uchida T., Matozaki T., Matsuda K., Suzuki T., Matozaki S., Nakano O., Wada K., Konda Y., Sakamoto C., Kasuga M. Phorbol ester stimulates the activity of a protein tyrosine phosphatase containing SH2 domains (PTP1C) in HL-60 leukemia cells by increasing gene expression. J Biol Chem. 1993 Jun 5;268(16):11845–11850. [PubMed] [Google Scholar]
  74. Varticovski L., Druker B., Morrison D., Cantley L., Roberts T. The colony stimulating factor-1 receptor associates with and activates phosphatidylinositol-3 kinase. Nature. 1989 Dec 7;342(6250):699–702. doi: 10.1038/342699a0. [DOI] [PubMed] [Google Scholar]
  75. Wang Y., Yeung Y. G., Langdon W. Y., Stanley E. R. c-Cbl is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages. J Biol Chem. 1996 Jan 5;271(1):17–20. doi: 10.1074/jbc.271.1.17. [DOI] [PubMed] [Google Scholar]
  76. Xiao S., Rose D. W., Sasaoka T., Maegawa H., Burke T. R., Jr, Roller P. P., Shoelson S. E., Olefsky J. M. Syp (SH-PTP2) is a positive mediator of growth factor-stimulated mitogenic signal transduction. J Biol Chem. 1994 Aug 19;269(33):21244–21248. [PubMed] [Google Scholar]
  77. Xu X. X., Tessner T. G., Rock C. O., Jackowski S. Phosphatidylcholine hydrolysis and c-myc expression are in collaborating mitogenic pathways activated by colony-stimulating factor 1. Mol Cell Biol. 1993 Mar;13(3):1522–1533. doi: 10.1128/mcb.13.3.1522. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Yamauchi K., Milarski K. L., Saltiel A. R., Pessin J. E. Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling. Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):664–668. doi: 10.1073/pnas.92.3.664. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Yatani A., Okabe K., Polakis P., Halenbeck R., McCormick F., Brown A. M. ras p21 and GAP inhibit coupling of muscarinic receptors to atrial K+ channels. Cell. 1990 Jun 1;61(5):769–776. doi: 10.1016/0092-8674(90)90187-j. [DOI] [PubMed] [Google Scholar]
  80. Yetter A., Uddin S., Krolewski J. J., Jiao H., Yi T., Platanias L. C. Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase. J Biol Chem. 1995 Aug 4;270(31):18179–18182. doi: 10.1074/jbc.270.31.18179. [DOI] [PubMed] [Google Scholar]
  81. Yeung Y. G., Berg K. L., Pixley F. J., Angeletti R. H., Stanley E. R. Protein tyrosine phosphatase-1C is rapidly phosphorylated in tyrosine in macrophages in response to colony stimulating factor-1. J Biol Chem. 1992 Nov 25;267(33):23447–23450. [PubMed] [Google Scholar]
  82. Yi T. L., Cleveland J. L., Ihle J. N. Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13. Mol Cell Biol. 1992 Feb;12(2):836–846. doi: 10.1128/mcb.12.2.836. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Yi T., Ihle J. N. Association of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand. Mol Cell Biol. 1993 Jun;13(6):3350–3358. doi: 10.1128/mcb.13.6.3350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Yi T., Mui A. L., Krystal G., Ihle J. N. 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. 1993 Dec;13(12):7577–7586. doi: 10.1128/mcb.13.12.7577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Zhao Z., Tan Z., Wright J. H., Diltz C. D., Shen S. H., Krebs E. G., Fischer E. H. Altered expression of protein-tyrosine phosphatase 2C in 293 cells affects protein tyrosine phosphorylation and mitogen-activated protein kinase activation. J Biol Chem. 1995 May 19;270(20):11765–11769. doi: 10.1074/jbc.270.20.11765. [DOI] [PubMed] [Google Scholar]

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