Cited by 193Erythropoietin and Anemia TreatmentCytokine Signaling Pathways and InteractionsProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.

Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein

Damen, JE, Liu, L, Cutler, RL, Krystal, G·1993·Blood

DOI 10.1182/blood.v82.8.2296.2296

Open this paper in CoChat — free account

Abstract

Although the erythropoietin receptor (EpR) lacks a tyrosine kinase consensus sequence within its proline-rich intracellular domain, addition of its ligand to Ep-responsive cells stimulates the rapid and transient tyrosine phosphorylation of a number of cellular proteins. The characterization of these phosphorylatable substrates, which include 5 major phosphoproteins with molecular masses of approximately 145, 130, 97, 72, and 56 Kd is an essential step in understanding the signal transduction pathways used by Ep. Recently, we and others have shown that the major 72-Kd tyrosine phosphorylated protein is the EpR itself. We now report, using both murine DA-3 and human MO7E cell lines engineered to express high levels of biologically responsive EpRs (and designated DA-ER and MO7-ER, respectively), that the major 56-Kd tyrosine phosphorylated protein is the recently identified SH2-containing protein, p52shc. Interestingly, in Ep-stimulated cells, anti-Shc antibodies coprecipitate the major 145-Kd tyrosine phosphorylated protein in both DA-ER and MO7-ER cells. Tyrosine phosphorylation of both proteins is detectable within 30 seconds of incubation with Ep at 37 degrees C, reaches a maximum between 2 and 5 minutes, and declines by 30 minutes. In addition, tyrosine phosphorylated Shc appears capable of associating with the activated EpR, but this could only be shown in MO7-ER cells. Lastly, as has been shown previously with the tyrosine kinase containing receptors for epidermal growth…

Integrity signals

Registry

Crossref · 10.1182/blood.v82.8.2296.2296

Cites

36 of 36 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

This paper’s full text isn’t openly available, 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?

The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
Lowenstein, E. J., Daly, R. J., Batzer, A., Li, W., Margolis, B. L., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar‐Sagi, D., & Schlessinger, J. (1992) · Cell · doi:10.1016/0092-8674(92)90167-b · Cited by 1,632
A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction
Pelicci, G., Lanfrancone, L., Grignani, F., McGlade, J. C., Cavallo, F., Forni, G., Nicoletti, I., Grignani, F., Pawson, T. J., & Pelicci, P. G. (1992) · Cell · doi:10.1016/0092-8674(92)90536-l · Cited by 1,326
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
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
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
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
Ras1 and a putative guanine nucleotide exchange factor perform crucial steps in signaling by the sevenless protein tyrosine kinase
Simon, M. A., Bowtell, D. D. L., Dodson, G. S., Laverty, T., & Rubin, G. M. (1991) · Cell · doi:10.1016/0092-8674(91)90065-7 · Cited by 860
Human Sos1: a Guanine Nucleotide Exchange Factor for Ras that Binds to GRB2
Chardin, P., Camonis, J., Gale, N. W., Aelst, L. V., Schlessinger, J., Wigler, M. H., & Bar‐Sagi, D. (1993) · Science · doi:10.1126/science.8493579 · Cited by 799
Expression cloning of the murine erythropoietin receptor
D’Andrea, A. D., Lodish, H. F., & Wong, G. G. (1989) · Cell · doi:10.1016/0092-8674(89)90965-3 · Cited by 737

Show all 36 references

Sorted by citations

Multiple Myeloma: Increasing Evidence for a Multistep Transformation Process
Hallek, M. J., Bergsagel, P. L., & Anderson, K. C. (1998) · Blood · doi:10.1182/blood.v91.1.3 · Cited by 750
Small Peptides as Potent Mimetics of the Protein Hormone Erythropoietin
Wrighton, N. C., Farrell, F. X., Chang, R., Kashyap, A. K., Barbone, F. P., Mulcahy, L. S., Johnson, D. L., Barrett, R. W., Jolliffe, L. K., & Dower, W. J. (1996) · Science · doi:10.1126/science.273.5274.458 · Cited by 672
Signaling by the cytokine receptor superfamily: JAKs and STATs
Ihle, J. N., Witthuhn, B. A., Quelle, F. W., Yamamoto, K., Thierfelder, W. E., Kreider, B. L., & Silvennoinen, O. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90026-4 · Cited by 648
The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase.
Damen, J. E., Liu, L., Rosten, P., Humphries, R. K., Jefferson, A. B., Majerus, P. W., & Krystal, G. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.4.1689 · Cited by 633
Self-citation
Signaling Through the Hematopoietic Cytokine Receptors
Ihle, J. N., Witthuhn, B. A., Quelle, F. W., Yamamoto, K., & Silvennoinen, O. (1995) · Annual Review of Immunology · doi:10.1146/annurev.iy.13.040195.002101 · Cited by 612
Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span
Helgason, C. D., Damen, J. E., Rosten, P., Grewal, R., Sorensen, P., Chappel, S. M., Borowski, A., Jirik, F., Krystal, G., & Humphries, R. K. (1998) · Genes & Development · doi:10.1101/gad.12.11.1610 · Cited by 556
Self-citation
Signaling via Shc family adapter proteins
Ravichandran, K. S. (2001) · Oncogene · doi:10.1038/sj.onc.1204776 · Cited by 424
p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity.
Lioubin, M. N., Algate, P. A., Tsai, S., Carlberg, K., Aebersold, A., & Rohrschneider, L. R. (1996) · Genes & Development · doi:10.1101/gad.10.9.1084 · Cited by 418
Opposite effects of the p52shc/p46shc and p66shc splicing isoforms on the EGF receptor–MAP kinase–fos signalling pathway
Migliaccio, E., Mele, S., Salcini, A. E., Pelicci, G., Lai, K. V., Superti‐Furga, G., Pawson, T. J., Fiore, P. P. D., Lanfrancone, L., & Pelicci, P. G. (1997) · The EMBO Journal · doi:10.1093/emboj/16.4.706 · Cited by 395
SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival
Liu, Q., Sasaki, T., Kozieradzki, I., Wakeham, A., Itie, A., Dumont, D. J., & Penninger, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.7.786 · Cited by 341
Structure, function, and biology of SHIP proteins
Rohrschneider, L. R., Fuller, J. F., Wolf, I., Liu, Y., & Lucas, D. M. (2000) · Genes & Development · doi:10.1101/gad.14.5.505 · Cited by 294
Molecular analysis of the granulocyte colony-stimulating factor receptor
Avalos, B. (1996) · Blood · doi:10.1182/blood.v88.3.761.bloodjournal883761 · Cited by 293
Direct Association with and Dephosphorylation of Jak2 Kinase by the SH2-Domain-Containing Protein Tyrosine Phosphatase SHP-1
Jiao, H., Berrada, K., Yang, W., Tabrizi, M. H., Platanias, L. C., & Yi, T. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.6985 · Cited by 290
Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin‐induced cell proliferation and Stat5 activation.
Damen, J. E., Wakao, H., Miyajima, A., Krošl, J., Humphries, R. K., Cutler, R. L., & Krystal, G. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00243.x · Cited by 275
Self-citation
Hematopoietic Growth Factors Signal Through the Formation of Reactive Oxygen Species
Sattler, M., Winkler, T., Verma, S., Byrne, C. H., Shrikhande, G., Salgia, R., & Griffin, J. D. (1999) · Blood · doi:10.1182/blood.v93.9.2928 · Cited by 254
Multiple cytokines induce the tyrosine phosphorylation of Shc and its association with Grb2 in hemopoietic cells.
Cutler, R. L., Liu, L., Damen, J. E., & Krystal, G. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80558-4 · Cited by 228
Self-citation
Signal Transduction in the Erythropoietin Receptor System
Wojchowski, D. M., Gregory, R. C., Miller, C. P., Pandit, A. K., & Pircher, T. J. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4673 · Cited by 227
The c-Mpl Ligand (Thrombopoietin) Stimulates Tyrosine Phosphorylation of Jak2, Shc, and c-Mpl
Drachman, J. G., Griffin, J. D., & Kaushansky, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.4979 · Cited by 223
The Janus Protein Tyrosine Kinase Family and Its Role in Cytokine Signaling
Ihle, J. N. (1995) · Advances in immunology · doi:10.1016/s0065-2776(08)60582-9 · Cited by 210
Interleukin 2 and erythropoietin activate STAT5/MGF via distinct pathways.
Wakao, H., Harada, N., Kitamura, T., Mui, A., & Miyajima, A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07250.x · Cited by 211
The Inositol Polyphosphate 5-Phosphatase Ship Is a Crucial Negative Regulator of B Cell Antigen Receptor Signaling
Liu, Q., Oliveira-dos-Santos, A., Mariathasan, S., Bouchard, D., Jones, J. V., Sarao, R., Kozieradzki, I., Ohashi, P. S., Penninger, J. M., & Dumont, D. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.7.1333 · Cited by 205
Multiple Cytokines Stimulate the Binding of a Common 145-Kilodalton Protein to Shc at the Grb2 Recognition Site of Shc
Liu, L., Damen, J. E., Cutler, R. L., & Krystal, G. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6926 · Cited by 181
Self-citation
The Proto-oncogene Product c-Cbl Becomes Tyrosine Phosphorylated by Stimulation with GM-CSF or Epo and Constitutively Binds to the SH3 Domain of Grb2/Ash in Human Hematopoietic Cells
Odai, H., Sasaki, K., Iwamatsu, A., Hanazono, Y., Tanaka, T., Mitani, K., Yazaki, Y., & Hirai, H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.18.10800 · Cited by 177
Identification of a novel pathway important for proliferation and differentiation of primary erythroid progenitors
Klingmüller, U., Wu, H., Hsiao, J. G., Toker, A., Duckworth, B. C., Cantley, L. C., & Lodish, H. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.3016 · Cited by 172
Interaction of Shc with Grb2 Regulates Association of Grb2 with mSOS
Ravichandran, K. S., Lorenz, U. M., Shoelson, S. E., & Burakoff, S. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.593 · Cited by 170
Growth Hormone-promoted Tyrosyl Phosphorylation of SHC Proteins and SHC Association with Grb2
VanderKuur, J. A., Allevato, G., Billestrup, N., Norstedt, G., & Carter‐Su, C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7587 · Cited by 160
Synergistic Activation of MAP Kinase (ERK1/2) by Erythropoietin and Stem Cell Factor Is Essential for Expanded Erythropoiesis
Sui, X., Krantz, S. B., You, M., & Zhao, Z. J. (1998) · Blood · doi:10.1182/blood.v92.4.1142 · Cited by 158
Differentiation stage-specific activation of p38 mitogen-activated protein kinase isoforms in primary human erythroid cells
Uddin, S., Ah-Kang, J., Ulaszek, J., Mahmud, D., & Wickrema, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307075101 · Cited by 151
Recombinant human erythropoietin antagonizes trastuzumab treatment of breast cancer cells via Jak2-mediated Src activation and PTEN inactivation
Liang, K., Esteva, F. J., Albarracin, C., Stemke-Hale, K., Lu, Y., Bianchini, G., Yang, C.-Y., Li, Y., Li, X., Chen, C.-T., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.025 · Cited by 139
Involvement of SH2-containing Phosphotyrosine Phosphatase Syp in Erythropoietin Receptor Signal Transduction Pathways
Tauchi, T., Feng, G., Shen, R., Hoatlin, M. E., Bagby, G. C., Kabat, D., Lu, L., & Broxmeyer, H. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5631 · Cited by 139
Phosphorylation of Tyrosine 503 in the Erythropoietin Receptor (EpR) Is Essential for Binding the P85 Subunit of Phosphatidylinositol (PI) 3-Kinase and for EpR-associated PI 3-Kinase Activity
Damen, J. E., Cutler, R. L., Jiao, H., Yi, T., & Krystal, G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23402 · Cited by 139
Self-citation
Erythropoietin protects against diabetes through direct effects on pancreatic β cells
Choi, D., Schroer, S. A., Lu, S. Y., Wang, L., Wu, X., Liu, Y., Zhang, Y., Gaisano, H. Y., Wagner, K., Wu, H., et al. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20100665 · Cited by 130
The Src Homology 2 (SH2) Domain of SH2-containing Inositol Phosphatase (SHIP) Is Essential for Tyrosine Phosphorylation of SHIP, Its Association with Shc, and Its Induction of Apoptosis
Liu, L., Damen, J. E., Hughes, M. R., Babić, I., Jirik, F. R., & Krystal, G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.8983 · Cited by 119
Self-citation
Recruitment and Phosphorylation of SH2-Containing Inositol Phosphatase and Shc to the B-Cell Fcϒ Immunoreceptor Tyrosine-Based Inhibition Motif Peptide Motif
Tridandapani, S., Kelley, T. W., Pradhan, M., Cooney, D. S., Justement, L. B., & Coggeshall, K. M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4305 · Cited by 117
Molecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast Cancer
Fiszman, G. L., & Jasnis, M. A. (2011) · International Journal of Breast Cancer · doi:10.4061/2011/352182 · Cited by 119
Shc Interaction with Src Homology 2 Domain Containing Inositol Phosphatase (SHIP) in VivoRequires the Shc-Phosphotyrosine Binding Domain and Two Specific Phosphotyrosines on SHIP
Lamkin, T. D., Walk, S. F., Liu, L., Damen, J. E., Krystal, G., & Ravichandran, K. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10396 · Cited by 118
Self-citation
The Role of Tyrosine Phosphorylation in Proliferation and Maturation of Erythroid Progenitor Cells
Klingmüller, U. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00637.x · Cited by 116
Shc, Grb2, Sosl, and a 150-Kilodalton Tyrosine-Phosphorylated Protein Form Complexes with Fms in Hematopoietic Cells
Lioubin, M. N., Myles, G. M., Carlberg, K., Bowtell, D. D. L., & Rohrschneider, L. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.5682-5691.1994 · Cited by 117
Shc adaptor proteins are key transducers of mitogenic signaling mediated by the G protein‐coupled thrombin receptor.
Chen, Y., Grall, D., Salcini, A. E., Pelicci, P. G., Pouysségur, J., & Obberghen‐Schilling, E. V. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00441.x · Cited by 110
The T-cell antigen receptor utilizes Lck, Raf-1, and MEK-1 for activating mitogen-activated protein kinase. Evidence for the existence of a second protein kinase C-dependent pathway in an Lck-negative Jurkat cell mutant.
Gupta, S., Weiss, A., Kumar, G., Wang, S., & Nel, A. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32560-7 · Cited by 109
Phosphatidylinositol 3′-Kinase and SH2-Containing Inositol Phosphatase (SHIP) Are Recruited by Distinct Positive and Negative Growth-Regulatory Domains in the Granulocyte Colony-Stimulating Factor Receptor
Hunter, M. G., & Avalos, B. R. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.10.4979 · Cited by 106
Establishment of normal, terminally differentiating mouse erythroid progenitors: molecular characterization by cDNA arrays
Dolznig, H., Boulmé, F., Stangl, K., Deiner, E. M., Mikulits, W., Beug, H., & Müllner, E. W. (2001) · The FASEB Journal · doi:10.1096/fj.00-0705fje · Cited by 105
A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain.
O’Bryan, J. P., Songyang, Z., Cantley, L. C., Der, C. J., & Pawson, T. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2729 · Cited by 105
AP1 Regulation of Proliferation and Initiation of Apoptosis in Erythropoietin-Dependent Erythroid Cells
Jacobs-Helber, S. M., Wickrema, A., Birrer, M. J., & Sawyer, S. T. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.3699 · Cited by 101
Multiple hemopoietins, with the exception of interleukin-4, induce modification of Shc and mSos1, but not their translocation.
Welham, M. J., Duronio, V., Leslie, K. B., Bowtell, D. D. L., & Schrader, J. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31944-0 · Cited by 100
Engagement of Gab1 and Gab2 in Erythropoietin Signaling
Wickrema, A., Shahab Uddin, M. S., Sharma, A. K., Chen, F., Alsayed, Y. M., Ahmad, S., Sawyer, S. T., Krystal, G., Yi, T., Nishada, K., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.35.24469 · Cited by 97
Self-citation
Erythropoietin Induces the Tyrosine Phosphorylation of Insulin Receptor Substrate-2
Verdier, F., Chrétien, S., Billat, C., Gisselbrecht, S., Lacombe, C., & Mayeux, P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26173 · Cited by 104
Cloning and characterization of human SHIP, the 145-kD inositol 5- phosphatase that associates with SHC after cytokine stimulation
Ware, M., Rosten, P., Damen, J., Liu, L., Humphries, R., & Krystal, G. (1996) · Blood · doi:10.1182/blood.v88.8.2833.bloodjournal8882833 · Cited by 96
Self-citation
Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease
Terzioglu, G., & Young-Pearse, T. L. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00674-9 · Cited by 91
Erythropoietin-Induced Activation of STAT5 Is Impaired in the Myelodysplastic Syndrome
Hoefsloot, L. H., Amelsvoort, M. P.-V., Broeders, L., van der Plas, D. C., van Lom, K., Hoogerbrugge, H., Touw, I. P., & Löwenberg, B. (1997) · Blood · doi:10.1182/blood.v89.5.1690 · Cited by 93
The SH2-Containing Inositol Polyphosphate 5-Phosphatase, Ship, Is Expressed During Hematopoiesis and Spermatogenesis
Liu, Q., Shalaby, F., Jones, J., Bouchard, D., & Dumont, D. J. (1998) · Blood · doi:10.1182/blood.v91.8.2753.2753_2753_2759 · Cited by 95
Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis
Tauchi, T., Damen, J. E., Toyama, K., Feng, G., Broxmeyer, H., & Krystal, G. (1996) · Blood · doi:10.1182/blood.v87.11.4495.bloodjournal87114495 · Cited by 95
Self-citation
Erythropoietin and Interleukin-3 Activate Tyrosine Phosphorylation of CBL and Association With CRK Adaptor Proteins
Barber, D. L., Mason, J. M., Fukazawa, T., Reedquist, K. A., Druker, B. J., Band, H., & D’Andrea, A. D. (1997) · Blood · doi:10.1182/blood.v89.9.3166 · Cited by 92
Activation of phosphatidylinositol 3-kinase is important for erythropoietin-induced erythropoiesis from CD34+ hematopoietic progenitor cells
Myklebust, J. H., Blomhoff, H. K., Rusten, L. S., Stokke, T., & Smeland, E. B. (2002) · Experimental Hematology · doi:10.1016/s0301-472x(02)00868-8 · Cited by 93
Distinct Signaling from Stem Cell Factor and Erythropoietin in HCD57 Cells
Jacobs-Helber, S. M., Penta, K., Sun, Z., Lawson, A. E., & Sawyer, S. T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.6850 · Cited by 89
Erythropoietin receptor-operated Ca2+ channels: Activation by phospholipase C-γ1
Marrero, M. B., Venema, R. C., Ma, H., Ling, B. N., & Eaton, D. C. (1998) · Kidney International · doi:10.1046/j.1523-1755.1998.00887.x · Cited by 85
Activation-induced Association of a 145-kDa Tyrosine-phosphorylated Protein with Shc and Syk in B Lymphocytes and Macrophages
Crowley, M. T., Harmer, S. L., & DeFranco, A. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.2.1145 · Cited by 81
Erythropoietin induces cancer cell resistance to ionizing radiation and to cisplatin
Belenkov, S., Shenouda, G., Rizhevskaya, E., Cournoyer, D., Belzile, J.-P., Souhami, L., Dević, S., & Chow, T. Y.-K. (2004) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.1525.3.12 · Cited by 84
Multimeric cytokine receptors: common versus specific functions
Sato, N., & Miyajima, A. (1994) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(94)90133-3 · Cited by 83
Missense mutation of the erythropoietin receptor is a rare event in human erythroid malignancies
Couedic, J. L., Mitjavila, M. T., Villeval, J., Féger, F., Gobert, S., Mayeux, P., Casadevall, N., & Vainchenker, W. (1996) · Blood · doi:10.1182/blood.v87.4.1502.bloodjournal8741502 · Cited by 79
Negative signaling in B cells: SHIP Grbs Shc
Tridandapani, S., Kelley, T. W., Cooney, D. S., Pradhan, M., & Coggeshall, K. M. (1997) · Immunology Today · doi:10.1016/s0167-5699(97)01112-2 · Cited by 76
Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells
Schmandt, R. E., Liu, S. K., & McGlade, C. J. (1999) · Oncogene · doi:10.1038/sj.onc.1202507 · Cited by 75
Expression and activation of SH2/PTB-containing ShcA adaptor protein reflects the pattern of neurogenesis in the mammalian brain
Conti, L., De‐Fraja, C., Gulisano, M., Migliaccio, E., Govoni, S. M., & Cattaneo, E. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.15.8185 · Cited by 76
Janus kinases in cytokine signalling
Ihle, J. N., & Marshall, C. J. (1996) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1996.0012 · Cited by 74
Protein Kinase C α Controls Erythropoietin Receptor Signaling
Lindern, M. V., Amelsvoort, M. P.-V., van Dijk, T., Deiner, E., van den Akker, E., Vries, S. E. V. E., Willems, P. H. G. M., Beug, H., & Löwenberg, B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007042200 · Cited by 75
Shc, Grb2, Sos1, and a 150-kilodalton tyrosine-phosphorylated protein form complexes with Fms in hematopoietic cells.
Lioubin, M. N., Myles, G. M., Carlberg, K., Bowtell, D. D. L., & Rohrschneider, L. R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.9.5682 · Cited by 74
Shc Proteins Are Localized on Endoplasmic Reticulum Membranes and Are Redistributed after Tyrosine Kinase Receptor Activation
Lotti, L. V., Lanfrancone, L., Migliaccio, E., Zompetta, C., Pelicci, G., Salcini, A. E., Falini, B., Pelicci, P. G., & Torrisi, M. R. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.5.1946 · Cited by 73
Analysis of Interleukin-2-dependent Signal Transduction through the Shc/Grb2 Adapter Pathway
Evans, G. A., Goldsmith, M. A., Johnston, J. A., Xu, W., Weiler, S. R., Erwin, R. A., Howard, O. M. Z., Abraham, R. T., O’Shea, J. J., Greene, W. C., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.48.28858 · 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
Induction of sequence-specific DNA-binding factors by erythropoietin and the spleen focus-forming virus
Ohashi, T., Masuda, M., & Ruscetti, S. K. (1995) · Blood · doi:10.1182/blood.v85.6.1454.bloodjournal8561454 · Cited by 71
Activation of the transcription factor NF-κB by the erythropoietin receptor
Bittorf, T., Büchse, T., Sasse, T., Jaster, R., & Brock, J. (2001) · Cellular Signalling · doi:10.1016/s0898-6568(01)00189-9 · Cited by 70
Association between GRB2/Sos and Insulin Receptor Substrate 1 Is Not Sufficient for Activation of Extracellular Signal-Regulated Kinases by Interleukin-4: Implications for Ras Activation by Insulin
Pruett, W., Yuan, Y. P., Rose, E., Batzer, A., Harada, N., & Skolnik, E. Y. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1778 · Cited by 69
Multiple Forms of the SH2-Containing Inositol Phosphatase, SHIP, Are Generated by C-Terminal Truncation
Damen, J. E., Liu, L., Ware, M. D., Ermolaeva, M. V., Majerus, P. W., & Krystal, G. (1998) · Blood · doi:10.1182/blood.v92.4.1199 · Cited by 68
Self-citation
Deregulation of erythropoiesis by the Friend spleen focus-forming virus
Ruscetti, S. K. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00074-6 · Cited by 70
Molecular Mechanisms of Erythropoietin Signaling
Cheung, J. Y., & Miller, B. A. (2001) · The Nephron journals/Nephron journals · doi:10.1159/000045918 · Cited by 66
The Signal Transduction Pathway of Erythropoietin Involves Three Forms of Mitogen‐Activated Protein (MAP) Kinase in UT7 Erythroleukemia Cells
Gobert, S., Duprez, V., Lacombe, C., Gisselbrecht, S., & Mayeux, P. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.075_c.x · Cited by 65
Core erythropoietin receptor signals for late erythroblast development
Menon, M. P., Fang, J., & Wojchowski, D. M. (2005) · Blood · doi:10.1182/blood-2005-02-0684 · Cited by 65
Co-stimulation-dependent activation of a JNK-kinase in T lymphocytes
Avraham, A., Jung, S., Samuels, Y., Seger, R., & Ben‐Neriah, Y. (1998) · European Journal of Immunology · doi:10.1002/(sici)1521-4141(199808)28:08 · Cited by 71
The role of SHIP in growth factor induced signalling
Huber, M., Helgason, C. D., Damen, J. E., Scheid, M. P., Duronio, V., Liu, L., Ware, M. D., Humphries, R. K., & Krystal, G. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(98)00049-2 · Cited by 63
Self-citation
Ras activation in normal white blood cells and childhood acute lymphoblastic leukemia.
von Lintig, F. C., Huvar, I., Law, P., Diccianni, M. B., Yu, A. L.-T., & Boss, G. R. (2000) · PubMed · Cited by 59
Essential Role for the C-Terminal Noncatalytic Region of SHIP in FcγRIIB1-Mediated Inhibitory Signaling
Aman, M. J., Walk, S. F., March, M., Su, H.-P., Carver, D. J., & Ravichandran, K. S. (2000) · Molecular and Cellular Biology · doi:10.1128/.20.10.3576-3589.2000 · Cited by 61
The extended box 2 subdomain of erythropoietin receptor is nonessential for Jak2 activation yet critical for efficient mitogenesis in FDC-ER cells
He, T., Jiang, N., Zhuang, H., Quelle, D. E., & Wojchowski, D. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32302-5 · Cited by 59
Modulation of Calcium Channels in Human Erythroblasts by Erythropoietin
Cheung, J. Y., Zhang, X.-Q., Bokvist, K. B., Tillotson, D. L., & Miller, B. A. (1997) · Blood · doi:10.1182/blood.v89.1.92 · Cited by 57
T Cell Activation through the CD43 Molecule Leads to Vav Tyrosine Phosphorylation and Mitogen-activated Protein Kinase Pathway Activation
Pedraza‐Alva, G., de Long, L. M., Burakoff, S. J., & Rosenstein, Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14218 · Cited by 56
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
Erythroid Cells Rendered Erythropoietin Independent by Infection with Friend Spleen Focus-Forming Virus Show Constitutive Activation of Phosphatidylinositol 3-Kinase and Akt Kinase: Involvement of Insulin Receptor Substrate-Related Adapter Proteins
Nishigaki, K., Hanson, C. A., Ohashi, T., Thompson, D. M., Muszynski, K. W., & Ruscetti, S. K. (2000) · Journal of Virology · doi:10.1128/jvi.74.7.3037-3045.2000 · Cited by 55
A Novel Spliced Form of SH2-Containing Inositol Phosphatase Is Expressed During Myeloid Development
Lucas, D. M., & Rohrschneider, L. R. (1999) · Blood · doi:10.1182/blood.v93.6.1922.406k21_1922_1933 · Cited by 54
B cell antigen receptor cross‐linking induces tyrosine phosphorylation and membrane translocation of a multimeric Shc complex that is augmented by CD19 co‐ligation
Lankester, A. C., van Schijndel, G. M. W., Rood, P. M. L., Verhoeven, A. J., & van Lier, R. A. W. (1994) · European Journal of Immunology · doi:10.1002/eji.1830241136 · Cited by 54
Tyrosine phosphorylation of the erythropoietin receptor: role for differentiation and mitogenic signal transduction
Gobert, S., Porteu, F., Pallu, S., Muller, O., Sabbah, M., Dusanter‐Fourt, I., Courtois, G., Lacombe, C., Gisselbrecht, S., & Mayeux, P. (1995) · Blood · doi:10.1182/blood.v86.2.598.bloodjournal862598 · Cited by 54
Role of the vav Proto-oncogene Product (Vav) in Erythropoietin-mediated Cell Proliferation and Phosphatidylinositol 3-Kinase Activity
Shigematsu, H., Iwasaki, H., Otsuka, T., Ohno, Y., Arima, F., & Niho, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14334 · Cited by 52
A Dominant Negative Erythropoietin (EPO) Receptor Inhibits EPO-Dependent Growth and Blocks F-gp55-Dependent Transformation
Barber, D. L., DeMartino, J. C., Showers, M. O., & D’Andrea, A. D. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.4.2257 · Cited by 52
Megakaryocyte growth and development factor and interleukin-3 induce patterns of protein-tyrosine phosphorylation that correlate with dominant differentiation over proliferation of mpl-transfected 32D cells
Mu, S., Xia, M., Elliott, G., Bogenberger, J., Swift, S. E., Bennett, L., Lappinga, D., Hecht, R. M., Lee, R., & Saris, C. P. (1995) · Blood · doi:10.1182/blood.v86.12.4532.bloodjournal86124532 · Cited by 52
Signal Transduction Pathways Regulating Hematopoietic Differentiation
Smithgall, T. E. (1998) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01346-2 · Cited by 50
The SH2 Inositol 5-Phosphatase Ship1 Is Recruited in an SH2-dependent Manner to the Erythropoietin Receptor
Mason, J. M., Beattie, B. K., Liu, Q., Dumont, D., & Barber, D. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4398 · Cited by 50
Erythropoietin Activates Raf1 by an Shc-Independent Pathway in CTLL-EPO-R Cells
Barber, D. L., Corless, C. N., Xia, K., Roberts, T. M., & D’Andrea, A. D. (1997) · Blood · doi:10.1182/blood.v89.1.55 · Cited by 48
Jun N-terminal kinase promotes proliferation of immature erythroid cells and erythropoietin-dependent cell lines
Jacobs-Helber, S. M., & Sawyer, S. T. (2004) · Blood · doi:10.1182/blood-2003-05-1754 · Cited by 48
A common epitope is shared by activated signal transducer and activator of transcription-5 (STAT5) and the phosphorylated erythropoietin receptor: implications for the docking model of STAT activation
Barber, D. L., Beattie, B. K., Mason, J. M., Nguyen, M. H.-H., Yoakim, M., Neel, B. G., D’Andrea, A. D., & Frank, D. A. (2001) · Blood · doi:10.1182/blood.v97.8.2230 · Cited by 45
Polycythemia Vera V. Enhanced Proliferation and Phosphorylation Due to Vanadate Are Diminished in Polycythemia Vera Erythroid Progenitor Cells: A Possible Defect of Phosphatase Activity in Polycythemia Vera
Dai, C., Krantz, S. B., & Sawyer, S. T. (1997) · Blood · doi:10.1182/blood.v89.10.3574 · Cited by 45
Role of Gab proteins in phosphatidylinositol 3-kinase activation by thrombopoietin (Tpo)
Bouscary, D., Lecoq‐Lafon, C., Chrétien, S., Zompì, S., Fichelson, S., Muller, O., Porteu, F., Dusanter‐Fourt, I., Gisselbrecht, S., Mayeux, P., et al. (2001) · Oncogene · doi:10.1038/sj.onc.1204317 · Cited by 44
Requirement for JAK2 inErythropoietin-Induced Signalling Pathways
Bittorf, T., Jaster, R., Lüdtke, B., Kamper, B., & Brock, J. (1997) · Cellular Signalling · doi:10.1016/s0898-6568(96)00121-0 · Cited by 44

Authors: Damen, J., Liu, L., Cutler, R., & Krystal, G.
Affiliations: Terry Fox Laboratory, B.C. Cancer Agency, Vancouver, Canada.
BC Cancer Agency (CA)
ORCID: Liu, L
Krystal, G
Venue: Blood
Publisher: American Society of Hematology
Published: 1993-10-15
Volume: 82
Issue: 8
Pages: 2296-2303
ISSN: 0006-4971 (ISSN-L)
1528-0020
DOI: 10.1182/blood.v82.8.2296.2296
OpenAlex: W50290146
Cited by: 193
References: 36
Citations by year: 2026: 1 · 2023: 3 · 2022: 1 · 2018: 1 · 2017: 2 · 2012: 4
FWCI: 13.78
Type: journal article
Language: en
Open access: closed
Locations: Blood (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: erythropoietin, erythropoietin receptor, Shc, Grb2, tyrosine phosphorylation, signal transduction, Ras activation, receptor tyrosine kinase, MO7e cells
MeSH terms: Src Homology 2 Domain-Containing, Transforming Protein 1, Animals, Cell Line, Erythropoietin, Cricetinae, Humans, Molecular Weight, Phosphoproteins, Phosphorylation, Proteins, Tyrosine, Oncogene Proteins, Receptors, Erythropoietin, Adaptor Proteins, Vesicular Transport, Adaptor Proteins, Signal Transducing, Mice, Shc Signaling Adaptor Proteins

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

Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein

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