Cited by 397Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingCytokine Signaling Pathways and Interactions

The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.

Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.

Open access

Bennett, A M, Tang, T L, Sugimoto, S, Walsh, C T, Neel, B G·1994·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.91.15.7335PMC PMC44394

Open this paper in CoChat — free account

Abstract

Protein-tyrosine-phosphatase SHPTP2 (Syp/PTP-1D/PTP2C) is the homologue of the Drosophila corkscrew (csw) gene product, which transmits positive signals from receptor tyrosine kinases. Likewise, SHPTP2 has been implicated in positive signaling from platelet-derived growth factor receptor beta (PDGFR). Upon PDGF stimulation, SHPTP2 binds to the PDGFR and becomes tyrosine-phosphorylated. We have identified tyrosine-542 (pY542TNI) as the major in vivo site of SHPTP2 tyrosine phosphorylation. The pY542TNI sequence conforms to the consensus binding site for the SH2 domain of Grb2, which, by association with Sos1, couples some growth factor receptors to Ras. Following PDGF stimulation, Grb2 binds tyrosine-phosphorylated SHPTP2. Moreover, a mutant PDGFR lacking its SHPTP2 binding site displays markedly reduced Grb2 binding. These data indicate that phosphorylation of SHPTP2 couples Grb2 to PDGFR in vivo, providing a mechanism for Ras activation by PDGFR and for positive signaling via SHPTP2 and Csw.

Integrity signals

Registry

Crossref · 10.1073/pnas.91.15.7335

Cites

43 of 43 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Signal transduction by receptors with tyrosine kinase activity
Ullrich, A., & Schlessinger, J. (1990) · Cell · doi:10.1016/0092-8674(90)90801-k · Cited by 5,435
Gene Splicing by Overlap Extension: Tailor-Made Genes Using the Polymerase Chain Reaction
Horton, R. M., Cai, Z., Ho, S. N., & Pease, L. R. (2013) · BioTechniques · doi:10.2144/000114017 · Cited by 1,292
Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
Egan, S. E., Giddings, B. W., Brooks, M. W., Buday, L., Sizeland, A. M., & Weinberg, R. A. (1993) · Nature · doi:10.1038/363045a0 · Cited by 1,200
[42] Detection and quantification of phosphotyrosine in proteins
Cooper, J. A., Sefton, B. M., & Hunter, T. R. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)99075-4 · Cited by 1,109
Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
Buday, L., & Downward, J. (1993) · Cell · doi:10.1016/0092-8674(93)90146-h · Cited by 1,064
The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
Rozakis-Adcock, M., Fernley, R. T., Wade, J. D., Pawson, T. J., & Bowtell, D. D. L. (1993) · Nature · doi:10.1038/363083a0 · Cited by 1,009
Phosphatidylinositol 3′‐kinase is activated by association with IRS‐1 during insulin stimulation.
Backer, J., Myers, M. G., Shoelson, S. E., Chin, D. J., Sun, X., Miralpeix, M., Hu, P. J., Margolis, B. L., Skolnik, E. Y., & Schlessinger, J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05426.x · Cited by 1,000
Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
Rozakis-Adcock, M., McGlade, J. C., Mbamalu, G., Pelicci, G., Daly, R. J., Li, W., Batzer, A., Thomas, S. Μ., Brugge, J. S., Pelicci, P. G., et al. (1992) · Nature · doi:10.1038/360689a0 · Cited by 973
SH2 and SH3 domains: From structure to function
Pawson, T. J., & Gish, G. D. (1992) · Cell · doi:10.1016/0092-8674(92)90504-6 · Cited by 940
Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling
Li, N., Batzer, A., Daly, R. J., Yajnik, V., Skolnik, E. Y., Chardin, P., Bar‐Sagi, D., Margolis, B. L., & Schlessinger, J. (1993) · Nature · doi:10.1038/363085a0 · Cited by 938

Flagged first, then by citations

Show all 43 references

Sorted by citations

Items 101–200 of 397

A THEMIS:SHP1 complex promotes T‐cell survival
Paster, W., Bruger, A. M., Katsch, K., Grégoire, C., Roncagalli, R., Fu, G., Gascoigne, N. R. J., Nika, K., Cohnen, A., Feller, S. M., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201387725 · Cited by 108
The Tyrosine Phosphatase Shp2 Interacts with NPM-ALK and Regulates Anaplastic Lymphoma Cell Growth and Migration
Voena, C., Conte, C., Ambrogio, C., Erba, E. B., Boccalatte, F. E., Mohammed, S., Jensen, O. N., Palestro, G., Inghirami, G., & Chiarle, R. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4350 · Cited by 103
Both Src-Dependent and -Independent Mechanisms Mediate Phosphatidylinositol 3-Kinase Regulation of Colony-Stimulating Factor 1-Activated Mitogen-Activated Protein Kinases in Myeloid Progenitors
Lee, A. W. ‐., & States, D. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6779-6798.2000 · Cited by 103
Direct Association of Grb2 with the p85 Subunit of Phosphatidylinositol 3-Kinase
Wang, J., Auger, K. R., Jarvis, L. A., Shi, Y., & Roberts, T. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12774 · Cited by 100
Growth Hormone Regulation of SIRP and SHP-2 Tyrosyl Phosphorylation and Association
Stofega, M. R., Wang, H., Ullrich, A., & Carter‐Su, C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.7112 · Cited by 100
SHP‐2 regulates the phosphatidylinositide 3′‐kinase/Akt pathway and suppresses caspase 3‐mediated apoptosis
Zito, C. I., Kontaridis, M. I., Fornaro, M., Feng, G. S., & Bennett, A. M. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10446 · Cited by 97
Self-citation
Peroxovanadate Induces Tyrosine Phosphorylation of Multiple Signaling Proteins in Mouse Liver and Kidney
Ruff-Jamison, S., Chen, K., & Cohen, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.1263 · Cited by 97
SHP-1 Associates with Both Platelet-derived Growth Factor Receptor and the p85 Subunit of Phosphatidylinositol 3-Kinase
Yu, Z., Su, L., Höglinger, O., Jaramillo, M., Banville, D., & Shen, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3687 · Cited by 96
Roles of Protein-tyrosine Phosphatases in Stat1α-mediated Cell Signaling
Haque, S. J., Flati, V., Deb, A., & Williams, B. R. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25709 · Cited by 95
Regulation of Insulin-like Growth Factor I Receptor Dephosphorylation by SHPS-1 and the Tyrosine Phosphatase SHP-2
Maile, L. A., & Clemmons, D. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109258200 · Cited by 95
Opposing Actions of CSW and RasGAP Modulate the Strength of Torso RTK Signaling in the Drosophila Terminal Pathway
Cleghon, V., Feldmann, P., Ghiglione, C., Copeland, T. D., Perrimon, N., Hughes, D. A., & Morrison, D. K. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80287-7 · Cited by 95
Receptor protein tyrosine phosphatase α participates in the m1 muscarinic acetylcholine receptor‐dependent regulation of Kv1.2 channel activity
Tsai, W., Morielli, A. D., Cachero, T. G., & Peralta, E. G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.109 · Cited by 93
The Phosphotyrosine Phosphatase PTP1D, but not PTP1C, Is an Essential Mediator of Fibroblast Proliferation Induced by Tyrosine Kinase and G Protein-coupled Receptors
Rivard, N., McKenzie, F. R., Brondello, J., & Pouysségur, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.18.11017 · Cited by 93
Transcriptional regulation of the AP-2α promoter by BTEB-1 and AP-2rep, a novel wt-1/egr-related zinc finger repressor
Imhof, A., Schuierer, M., Werner, O., Moser, M., Roth, C., Bauer, R., & Buettner, R. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.194 · Cited by 90
The docking molecule Gab2 is induced by lymphocyte activation and is involved in signaling by Interleukin-2 and Interleukin-15 but not other common gamma chain-using cytokines
Gadina, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004021200 · Cited by 92
Activation of Protein-tyrosine Phosphatase SH-PTP2 by a Tyrosine-based Activation Motif of a Novel Brain Molecule
Ohnishi, H., Kubota, M., Ohtake, A., Sato, K., & Sano, S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.41.25569 · Cited by 92
Src Homology Region 2-Containing Protein Tyrosine Phosphatase-2 (SHP-2) Can Play a Direct Role in the Inhibitory Function of Killer Cell Ig-Like Receptors in Human NK Cells
Yusa, S.-I., & Campbell, K. S. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.9.4539 · Cited by 91
Characterization of the Signaling Capacities of the Novel gp130-like Cytokine Receptor*
Dreuw, A., Radtke, S., Pflanz, S., Lippok, B., Heinrich, P., & Hermanns, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401122200 · Cited by 87
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 the Prolongation of Eosinophil Survival
Pazdrak, K., Adachi, T., & Alam, R. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.4.561 · Cited by 89
Granulocyte-macrophage Colony-stimulating Factor Provokes RAS Activation and Transcription of c-fos through Different Modes of Signaling
Itoh, T., Muto, A., Watanabe, S., Miyajima, A., Yokota, T., & Arai, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.13.7587 · Cited by 89
HCPTPA, a Protein Tyrosine Phosphatase That Regulates Vascular Endothelial Growth Factor Receptor-mediated Signal Transduction and Biological Activity
Huang, L., Sankar, S., Lin, C., Kontos, C. D., Schroff, A. D., Cha, E. H., Feng, S.-M., Li, S.-F., Yu, Z., Etten, R. L. V., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38183 · Cited by 88
Ras-GRF Activates Ha-Ras, but Not N-Ras or K-Ras 4B, Proteinin Vivo
Jones, M. K., & Jackson, J. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1782 · Cited by 88
Protein tyrosine phosphorylation in T cell signaling
Mustelin, T. (2002) · Frontiers in bioscience · doi:10.2741/a821 · Cited by 87
Gab-Family Adapter Molecules in Signal Transduction of Cytokine and Growth Factor Receptors, and T and B Cell Antigen Receptors
Hibi, M., & Hirano, T. (2000) · Leukemia and Lymphoma · doi:10.3109/10428190009089430 · Cited by 94
Specific SHP-2 partitioning in raft domains triggers integrin-mediated signaling via Rho activation
Lacalle, R. A., Mira, E., Gómez‐Moutón, C., Jiménez-Baranda, S., Martínez‐A, C., & Mañes, S. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200109031 · Cited by 82
Structure of the noncompetitive antagonist-binding site of the Torpedo nicotinic acetylcholine receptor. [3H]meproadifen mustard reacts selectively with alpha-subunit Glu-262.
Pedersen, S. E., Sharp, S. D., Liu, W., & Cohen, J. B. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50044-8 · Cited by 81
Altered Expression of Protein-tyrosine Phosphatase 2C in 293 Cells Affects Protein Tyrosine Phosphorylation and Mitogen-activated Protein Kinase Activation
Zhao, Z. J., Tan, Z., Wright, J. H., Diltz, C. D., Shen, S., Krebs, E. G., & Fischer, E. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11765 · Cited by 81
MAPK and PI3K signaling: At the crossroads of neural crest development
Dinsmore, C. J., & Soriano, P. M. (2018) · Developmental Biology · doi:10.1016/j.ydbio.2018.02.003 · Cited by 82
SHP-2 binds to Tyr763 and Tyr1009 in the PDGF β-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis
Rönnstrand, L., Arvidsson, A., Kallin, A., Rorsman, C., Hellman, U., Engström, U., Wernstedt, C., & Heldin, C. (1999) · Oncogene · doi:10.1038/sj.onc.1202705 · Cited by 79
Integrins Enhance Platelet-derived Growth Factor (PDGF)-dependent Responses by Altering the Signal Relay Enzymes That Are Recruited to the PDGF β Receptor
DeMali, K. A., Balciunaite, E., & Kazlauskas, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19551 · Cited by 79
The Next Wave
Mustelin, T., Brockdorff, J. L., Rudbeck, L., Wingren, A. G., Han, S., Wang, X., Tailor, P., & Saxena, M. (1999) · Cellular Signalling · doi:10.1016/s0898-6568(99)00016-9 · Cited by 78
The Shp-2 tyrosine phosphatase activates the Src tyrosine kinase by a non-enzymatic mechanism
Walter, A. O., Peng, Z.-Y., & Cartwright, C. A. (1999) · Oncogene · doi:10.1038/sj.onc.1202513 · Cited by 78
Non-redundant Signal Transduction of Interleukin-6-type Cytokines
Hermanns, H. M., Radtke, S., Schaper, F., Heinrich, P. C., & Behrmann, I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005408200 · Cited by 79
Shp-2 mediates v-Src-induced morphological changes and activation of the anti-apoptotic protein kinase Akt
Hakak, Y., Hsu, Y. S., & Martin, G. S. (2000) · Oncogene · doi:10.1038/sj.onc.1203655 · Cited by 77
Specific involvement of tyrosine 764 of human granulocyte colony- stimulating factor receptor in signal transduction mediated by p145/Shc/GRB2 or p90/GRB2 complexes
de Koning, J. P., Schelen, A. M., Dong, F., van Buitenen, C., Burgering, B. M. T., Bos, J. L., Löwenberg, B., & Touw, I. (1996) · Blood · doi:10.1182/blood.v87.1.132.132 · Cited by 77
Interleukin-3 Induces the Association of the Inositol 5-Phosphatase SHIP with SHP2
Liu, L., Damen, J. E., Ware, M. D., & Krystal, G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.10998 · Cited by 73
SHP2 Inhibition Sensitizes Diverse Oncogene-Addicted Solid Tumors to Re-treatment with Targeted Therapy
Drilon, A. E. D. C., Sharma, M. R., Johnson, M. L., Yap, T. A., Gadgeel, S. M., Nepert, D. L., Feng, G., Reddy, M. B., Harney, A. S., Elsayed, M., et al. (2023) · Cancer Discovery · doi:10.1158/2159-8290.cd-23-0361 · Cited by 75
The low Mr phosphotyrosine protein phosphatase behaves differently when phosphorylated at Tyr131 or Tyr132 by Src kinase
Bucciantini, M., Chiarugi, P., Cirri, P., Taddei, L., Stefani, M., Raugei, G., Nordlund, P., & Ramponi, G. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00828-5 · Cited by 75
Expression of a Dominant Negative SHP-2 in Transgenic Mice Induces Insulin Resistance
Maegawa, H., Hasegawa, M., Sugai, S., Obata, T., Ugi, S., Morino, K., Egawa, K., Fujita, T., Sakamoto, T., Nishio, Y., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.30236 · Cited by 75
Adapter Function of Protein-tyrosine Phosphatase 1D in Insulin Receptor/Insulin Receptor Substrate-1 Interaction
Kharitonenkov, A., Schnekenburger, J., Chen, Z., Knyazev, P. G., Ali, S., Zwick, E., White, M. F., & Ullrich, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.49.29189 · Cited by 75
Functions of Tie1 and Tie2 Receptor Tyrosine Kinases in Vascular Development
Partanen, J. M., & Dumont, D. (1999) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-59953-8_8 · Cited by 74
The Docking Molecule Gab2 Is Induced by Lymphocyte Activation and Is Involved in Signaling by Interleukin-2 and Interleukin-15 but Not Other Common γ Chain-using Cytokines
Gadina, M., Sudarshan, C., Visconti, R., Zhou, Y., Gu, H., Neel, B. G., & O’Shea, J. J. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61466-3 · Cited by 75
Self-citation
Role of protein tyrosine phosphatases in the modulation of insulin signaling and their implication in the pathogenesis of obesity-linked insulin resistance
Xu, E., Schwab, M. G., & Marette, A. (2013) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-013-9282-4 · Cited by 76
Definition of the Role of Tyrosine Residues of the Common β Subunit Regulating Multiple Signaling Pathways of Granulocyte-Macrophage Colony-Stimulating Factor Receptor
Itoh, T., Liu, R., Yokota, T., Arai, K., & Watanabe, S. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.742 · Cited by 74
Selective Inhibition of Growth Factor-stimulated Mitogenesis by a Cell-permeable Grb2-binding Peptide
Williams, E. J., Dunican, D. J., Green, P. J., Howell, F. V., Derossi, D., Walsh, F. S., & Doherty, P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22349 · Cited by 74
Octapeptide somatostatin analog SMS 201-995 induces translocation of intracellular PTP1C to membranes in MCF-7 human breast adenocarcinoma cells
Srikant, C. B., & Shen, S. H. (1996) · Endocrinology · doi:10.1210/en.137.8.3461 · Cited by 73
Alterations in the Global Proteome and Phosphoproteome in Third Generation EGFR TKI Resistance Reveal Drug Targets to Circumvent Resistance
Zhang, X., Maity, T. K., ROSS, K. E., Qi, Y. A., Cultraro, C. M., Bahta, M., Pitts, S. C., Keswani, M., Gao, S., Nguyen, K. D. P., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-2435 · Cited by 72
Phosphorylation of Tyrosine 720 in the Platelet-Derived Growth Factor α Receptor Is Required for Binding of Grb2 and SHP-2 but Not for Activation of Ras or Cell Proliferation
Bazenet, C. E., Gelderloos, J. A., & Kazlauskas, A. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.6926 · Cited by 72
Signaling by the Cytokine Receptor Superfamily in Normal and Transformed Hematopoietic Cells
Ihle, J. N. (1996) · Advances in cancer research · doi:10.1016/s0065-230x(08)60351-6 · Cited by 70
Catalytic-dependent and -independent roles of SHP-2 tyrosine phosphatase in interleukin-3 signaling
Yu, W.-M., Hawley, T. S., Hawley, R. G., & Qu, C. (2003) · Oncogene · doi:10.1038/sj.onc.1206846 · Cited by 71
Structure, Function, and Pathogenesis of SHP2 in Developmental Disorders and Tumorigenesis
Huang, W.-Q., Lin, Q., Zhuang, X., Cai, L., Ruan, R., Lu, Z., & Tzeng, C. (2014) · Current Cancer Drug Targets · doi:10.2174/1568009614666140717105001 · Cited by 70
Sprouty proteins are in vivo targets of Corkscrew/SHP-2 tyrosine phosphatases
Jarvis, L. A., Peters, S. T., Simon, M. A., Krasnow, M. A., & Smith-Bolton, R. K. (2006) · Development · doi:10.1242/dev.02255 · Cited by 69
Specificity and affinity motifs for Grb2 SH2-ligand interactions
Kessels, H. W. H. G., Ward, A. C., & Schumacher, T. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142224499 · Cited by 69
Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584.
Vogel, W. F., & Ullrich, A. (1996) · PubMed · Cited by 69
SHP2 promotes proliferation of breast cancer cells through regulating Cyclin D1 stability via the PI3K/AKT/GSK3β signaling pathway
Yuan, Y., Fan, Y., Gao, Z., Sun, X., Zhang, H., Wang, Z., Cui, Y., Song, W., Wang, Z., Zhang, F., et al. (2020) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2020.0056 · Cited by 69
Protein Tyrosine Phosphatases in Cancer
Labbé, D. P., Hardy, S., & Tremblay, M. L. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396456-4.00009-2 · Cited by 71
Protein kinase structure and function analysis with chemical tools
Shen, K., Hines, A. C., Schwarzer, D., Pickin, K. A., & Cole, P. A. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.08.020 · Cited by 68
Protein Tyrosine Phosphatases and the Control of Cellular Signaling Responses
Tonks, N. K. (1996) · Advances in pharmacology · doi:10.1016/s1054-3589(08)60578-5 · Cited by 68
Biochemical and genetic analysis of the Drk SH2/SH3 adaptor protein of Drosophila.
Raabe, T., Olivier, J. P., Dickson, B. J., Liu, X. J., Gish, G. D., Pawson, T. J., & Hafen, E. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07248.x · Cited by 67
SHP1 and SHP2 protein-tyrosine phosphatases associate with betac after interleukin-3-induced receptor tyrosine phosphorylation. Identification of potential binding sites and substrates.
Bone, H., Dechert, U., Jirik, F. R., Schrader, J. W., & Welham, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14470 · Cited by 72
Type I Collagen Limits VEGFR-2 Signaling by a SHP2 Protein-Tyrosine Phosphatase–Dependent Mechanism 1
Mitola, S. M. F., Brenchio, B., Piccinini, M., Tertoolen, L. G. J., Zammataro, L. A., Breier, G., RINAUDO, M. T., den Hertog, J., Arese, M., & Bussolino, F. (2005) · Circulation Research · doi:10.1161/01.res.0000199355.32422.7b · Cited by 66
The role of phosphotyrosine phosphatases in haematopoietic cell signal transduction
Frearson, J. A., & Alexander, D. R. (1997) · BioEssays · doi:10.1002/bies.950190509 · Cited by 66
Dopamine regulates phosphorylation of VEGF receptor 2 by engaging Src-homology-2-domain-containing protein tyrosine phosphatase 2
Sinha, S., Vohra, P. K., Bhattacharya, R., Dutta, S. K., Sinha, S., & Mukhopadhyay, D. (2009) · Journal of Cell Science · doi:10.1242/jcs.053124 · Cited by 63
Rapid Identification of Phosphopeptide Ligands for SH2 Domains
Müller, K., Gombert, F. O., Manning, U., Grossmüller, F., Graff, P., Zaegel, H., Zuber, J.-F., Freuler, F., Tschopp, C., & Baumann, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.28.16500 · Cited by 65
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
Noguchi, T., Matozaki, T., Fujioka, Y., Yamao, T., Tsuda, M., Takada, T., & Kasuga, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27652 · Cited by 64
Tryptophan 650 of human granulocyte colony-stimulating factor (G-CSF) receptor, implicated in the activation of JAK2, is also required for G- CSF-mediated activation of signaling complexes of the p21ras route
Barge, R., de Koning, J. P., Pouwels, K., Dong, F., Lowenberg, B., & Touw, I. (1996) · Blood · doi:10.1182/blood.v87.6.2148.bloodjournal8762148 · Cited by 64
Somatostatin receptor 1 (SSTR1)-mediated inhibition of cell proliferation correlates with the activation of the MAP kinase cascade: role of the phosphotyrosine phosphatase SHP-2
Florio, T., Thellung, S., Arena, S. K., Corsaro, A., Bajetto, A., Schettini, G., & Stork, P. A. (2000) · Journal of Physiology-Paris · doi:10.1016/s0928-4257(00)00214-x · Cited by 63
Tyrosine Phosphatase SHP-2 Is Involved in Regulation of Platelet-derived Growth Factor-induced Migration
Qi, J. H., Ito, N., & Claesson, L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.14455 · Cited by 63
Physiological Signaling Specificity by Protein Tyrosine Phosphatases
Soulsby, M., & Bennett, A. M. (2009) · Physiology · doi:10.1152/physiol.00017.2009 · Cited by 65
Self-citation
Molecular Mechanism for SHP2 in Promoting HER2-induced Signaling and Transformation
Zhou, X., & Agazie, Y. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900020200 · Cited by 62
Disruption of Gap Junctional Communication by the Platelet-derived Growth Factor Is Mediated via Multiple Signaling Pathways
Hossain, M. Z., Jagdale, A. B., Peng, A., Kazlauskas, A., & Boynton, A. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.15.10489 · Cited by 61
A role for the SHP-2 tyrosine phosphatase in nerve growth-induced PC12 cell differentiation.
Wright, J. H., Drueckes, P., Bartoe, J. L., Zhao, Z., Shen, S. H., & Krebs, E. G. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.8.1575 · Cited by 61
Association between Receptor Protein-tyrosine Phosphatase RPTPα and the Grb2 Adaptor
Su, J. D., Yang, L., & Sap, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.45.28086 · Cited by 58
Angiotensin II Stimulates Tyrosine Phosphorylation and Activation of Insulin Receptor Substrate 1 and Protein-tyrosine Phosphatase 1D in Vascular Smooth Muscle Cells
Ali, M., Schieffer, B., Delafontaine, P., Bernstein, K. E., Ling, B. N., & Marrero, M. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.19.12373 · Cited by 59
The Caenorhabditis elegans EGL-15 Signaling Pathway Implicates a DOS-Like Multisubstrate Adaptor Protein in Fibroblast Growth Factor Signal Transduction
Schutzman, J. L., Borland, C. Z., Newman, J. C., Robinson, M. K., Kokel, M., & Stern, M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.8104-8116.2001 · Cited by 58
Characterization of a Novel Tyrosine Phosphorylated 100-kDa Protein That Binds to SHP-2 and Phosphatidylinositol 3′-Kinase in Myeloid Cells
Carlberg, K., & Rohrschneider, L. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15943 · Cited by 56
PTPN11-Associated Mutations in the Heart: Has LEOPARD Changed Its RASpots?
Lauriol, J., & Kontaridis, M. I. (2011) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2012.03.006 · Cited by 55
SHP-2 in Lymphocytes' Cytokine and Inhibitory Receptor Signaling
Niogret, C., Birchmeier, W., & Guarda, G. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02468 · Cited by 58
Functional analysis of the cytoplastic domain of the human Mpl receptor for tyrosine‐phosphorylation of the signaling molecules, proliferation and differentiation
Morita, H., Tahara, T., Matsumoto, A., Kato, T., Miyazaki, H., & Ohashi, H. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)01047-2 · Cited by 55
Different Signaling Roles of SHPTP2 in Insulin-induced GLUT1 Expression and GLUT4 Translocation
Hausdorff, S. F., Bennett, A. M., Neel, B. G., & Birnbaum, M. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.12965 · Cited by 55
Self-citation
Nerve Growth Factor Stimulates Tyrosine Phosphorylation and Activation of Src Homology-containing Protein-tyrosine Phosphatase 1 in PC12 Cells
Vambutas, V., Kaplan, D. R., Sells, M. A., & Chernoff, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25629 · Cited by 55
Nitric Oxide–Induced Motility in Aortic Smooth Muscle Cells
Chang, Y., Ceacareanu, B., Dixit, M., Sreejayan, N., & Hassid, A. (2002) · Circulation Research · doi:10.1161/01.res.0000033524.92083.64 · Cited by 55
Off‐target inhibition by active site‐targeting SHP 2 inhibitors
Tsutsumi, R., Ran, H., & Neel, B. G. (2018) · FEBS Open Bio · doi:10.1002/2211-5463.12493 · Cited by 54
Self-citation
Phosphorylation of Grb2-Associated Binder 2 on Serine 623 by ERK MAPK Regulates Its Association with the Phosphatase SHP-2 and Decreases STAT5 Activation
Arnaud‐Arnould, M., Crouin, C., Déon, C., Loyaux, D., & Bertoglio, J. H. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.6.3962 · Cited by 54
Prediction of phosphotyrosine signaling networks using a scoring matrix-assisted ligand identification approach
Li, L., Wu, C., Huang, H., Zhang, K., Gan, J., & Li, S. S. ‐. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn161 · Cited by 57
Fibroblast growth factor signaling in Caenorhabditis elegans
Borland, C. Z., Schutzman, J. L., & Stern, M. (2001) · BioEssays · doi:10.1002/bies.10007 · Cited by 54
Interleukin-2 signaling pathway analysis by quantitative phosphoproteomics
Osinalde, N., Hollegaard, H. M., Arrizabalaga, O., Ibarra, M. J. O., Blagoev, B., Zubiaga, A. M., Fullaondo, A., Arizmendi, J. M., & Kratchmarova, I. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.007 · Cited by 53
Role of SHP-2 in Fibroblast Growth Factor Receptor-Mediated Suppression of Myogenesis in C2C12 Myoblasts
Kontaridis, M. I., Liu, X., Zhang, L., & Bennett, A. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3875-3891.2002 · Cited by 53
Self-citation
Targeting KRAS mutations: orchestrating cancer evolution and therapeutic challenges
Choucair, K., Imtiaz, H., Uddin, M. H., Nagasaka, M., Al-Hallak, M. N., Philip, P. A., El-Rayes, B., Pasche, B., & Azmi, A. S. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02473-8 · Cited by 67
The TEL/PDGFβR fusion in chronic myelomonocytic leukemia signals through STAT5-dependent and STAT5-independent pathways
Sternberg, D., Tomasson, M. H., Carroll, M. P., Curley, D. P., Barker, G., Caprio, M., Wilbanks, A. M., Kazlauskas, A., & Gilliland, D. G. (2001) · Blood · doi:10.1182/blood.v98.12.3390 · Cited by 52
SHP2 Associates Directly with Tyrosine Phosphorylated p90 (SNT) Protein in FGF-Stimulated Cells
Ong, S. H., Lim, Y. P., Low, B. C., & Guy, G. R. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7272 · Cited by 52
Dominant-negative Mutants of Grb2 Induced Reversal of the Transformed Phenotypes Caused by the Point Mutation-activated Rat HER-2/Neu
Xie, Y., Pendergast, A. M., & Hung, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30717 · Cited by 51
The GTPase-Activating Protein of Ras Suppresses Platelet-Derived Growth Factor β Receptor Signaling by Silencing Phospholipase C-γ1
Valius, M., Secrist, J. P., & Kazlauskas, A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.6.3058 · Cited by 51
The Q61H mutation decouples KRAS from upstream regulation and renders cancer cells resistant to SHP2 inhibitors
Gebregiworgis, T., Kano, Y., St-Germain, J., Radulovich, N., Udaskin, M. L., Mentes, A., Huang, R., Poon, B. P. K., He, W., Valencia-Sama, I., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26526-y · Cited by 49
Granulocyte colony-stimulating factor and its receptor in normal hematophoietic cell development and myeloid disease
van de Geijn, G. J. M., Aarts, L. H. J., Erkeland, S. J., Prasher, J. M., & Touw, L. P. (2003) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/s10254-003-0014-0 · Cited by 50
Overlapping and distinct signals through leptin receptor (OB‐R) and a closely related cytokine signal transducer, gp130
Nakashima, K., Narazaki, M., & Taga, T. (1997) · FEBS Letters · doi:10.1016/s0014-5793(96)01430-5 · Cited by 50
Expression of Dominant Negative Mutant SHPTP2 Attenuates Phosphatidylinositol 3′-Kinase Activity via Modulation of Phosphorylation of Insulin Receptor Substrate-1
Ugi, S., Maegawa, H., Kashiwagi, A., Adachi, M., Olefsky, J. M., & Kikkawa, R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.21.12595 · Cited by 50
Regulation of immune function by protein tyrosine phosphatases
Okumura, M. (1995) · Current Opinion in Immunology · doi:10.1016/0952-7915(95)80104-9 · Cited by 50
Identification of a viability domain in the granulocyte/macrophage colony-stimulating factor receptor beta-chain involving tyrosine-750.
Inhorn, R. C., Carlesso, N., Durstin, M., Frank, D. A., & Griffin, J. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.19.8665 · Cited by 50
SHP-2 is a novel target of Abl kinases during cell proliferation
Mitra, S., Beach, C. M., Feng, G., & Plattner, R. (2008) · Journal of Cell Science · doi:10.1242/jcs.035691 · Cited by 51

Authors: Bennett, A. M., Tang, T. L., Sugimoto, S., Walsh, C. T., & Neel, B. G.
Affiliations: Beth Israel Deaconess Medical Center (US)
ORCID: Bennett, A M
Walsh, C T
Neel, B G
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1994-07-19
Volume: 91
Issue: 15
Pages: 7335-7339
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.91.15.7335
PMC: PMC44394
OpenAlex: W2006147172
Cited by: 397
References: 43
Citations by year: 2026: 8 · 2025: 4 · 2024: 4 · 2023: 9 · 2022: 11 · 2021: 13 · 2020: 7 · 2019: 6 · 2018: 10 · 2017: 5 · 2016: 10 · 2015: 4 · 2014: 5 · 2013: 10 · 2012: 7
FWCI: 12.78
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: American Cancer Society
National Institutes of Health (GM20011, CA49152)
National Cancer Institute (CA-49152)
National Institute of General Medical Sciences (GM 20011)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Keywords: PDGFRβ, Ras activation, Grb2, SOS1, receptor tyrosine kinase signaling, tyrosine phosphorylation, SH2 domain binding
MeSH terms: Animals, Base Sequence, Binding Sites, Cell Line, DNA, Humans, Mice, Inbred BALB C, Molecular Sequence Data, Phosphorylation, Genes, ras, Signal Transduction, 3T3 Cells, Protein Tyrosine Phosphatases, Receptors, Platelet-Derived Growth Factor, Intracellular Signaling Peptides and Proteins, Mice, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatase, Non-Receptor Type 11, SH2 Domain-Containing Protein Tyrosine Phosphatases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks