Cited by 203Cytokine Signaling Pathways and InteractionsProtein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase Signaling

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

A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1

Open access

Haspel, Richard L., Darnell, James E.·1999·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.96.18.10188PMC PMC17864

Open this paper in CoChat — free account

Abstract

The Stat1 activation-inactivation cycle involves phosphorylation of Stat1 in the cytoplasm, translocation to the nucleus, and then a return of the protein to the cytoplasm in a dephosphorylated state. However, the intracellular site of Stat1 dephosphorylation has not been determined. As receptor signaling declines, the flow of activated Stat1 molecules should be to the site of their dephosphorylation. We found that upon receptor-Janus kinase inactivation, either gradual or abruptly induced by staurosporine treatment, the flow of Stat1 was from cytoplasm to the nucleus and the nucleus was the final compartment in which phosphorylated Stat1 was detected. N-terminal mutants of Stat1, previously shown to remain phosphorylated for a longer time than wild-type Stat1, were able to enter the nucleus and were not inactivated in the presence of staurosporine, directly demonstrating that these mutations affect phosphatase access and/or activity during the normal dephosphorylation of Stat1. In the presence of sodium vanadate, a phosphatase inhibitor, phosphorylated Stat1 accumulated in the nucleus as the total amount of Stat1 in the cytoplasm declined to low levels. We conclude that the nucleus is the site of Stat1 inactivation and that dephosphorylation is required for the rapid nuclear export of Stat1.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1073/pnas.96.18.10188

Cites

36 of 36 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins
Darnell, J. E., Kerr, L. M., & Stark, G. R. (1994) · Science · doi:10.1126/science.8197455 · Cited by 6,080
STATs and Gene Regulation
Darnell, J. E. (1997) · Science · doi:10.1126/science.277.5332.1630 · Cited by 3,979
Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis
Fried, M. G., & Crothers, D. M. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.23.6505 · Cited by 2,658
A family of cytokine-inducible inhibitors of signalling
Starr, R., Willson, T. A., Viney, E. M., Murray, L. J. L., Rayner, J. R., Jenkins, B. J., Gonda, T. J., Alexander, W. S., Metcalf, D., Nicola, N. A., et al. (1997) · Nature · doi:10.1038/43206 · Cited by 2,066
JAKS AND STATS: Biological Implications
Leonard, W. J., & O’Shea, J. J. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.293 · Cited by 1,826
TRANSCRIPTIONAL RESPONSES TO POLYPEPTIDE LIGANDS: The JAK-STAT Pathway
Schindler, C., & Darnell, J. E. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.003201 · Cited by 1,808
Targeted Disruption of the Stat1 Gene in Mice Reveals Unexpected Physiologic Specificity in the JAK–STAT Signaling Pathway
Meraz, M. A., White, J. M., Sheehan, K. C. F., Bach, E. A., Rodig, S. J., Dighe, A. S., Kaplan, D. H., Riley, J. K., Greenlund, A. C., Campbell, D., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81288-x · Cited by 1,656
A new protein containing an SH2 domain that inhibits JAK kinases
Endo, T. A., Masuhara, M., Yokouchi, M., Suzuki, R., Sakamoto, H., Mitsui, K., Matsumoto, A., Tanimura, S., Ohtsubo, M., Misawa, H., et al. (1997) · Nature · doi:10.1038/43213 · Cited by 1,408
Endocytosis
Mukherjee, S., Ghosh, R. K., & Maxfield, F. R. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.3.759 · Cited by 1,299
Structure and function of a new STAT-induced STAT inhibitor
Naka, T., Narazaki, M., Hirata, M., Matsumoto, T., Minamoto, S., Aono, A., Nishimoto, N., Kajita, T., Taga, T., Yoshizaki, K., et al. (1997) · Nature · doi:10.1038/43219 · Cited by 1,040

Show all 36 references

Research works printed but not linked: 1

D Levy, J E Darnell New Biol 2, 923–928 (1990).

Sorted by citations

Interferon-γ: an overview of signals, mechanisms and functions
Schroder, K., Hertzog, P. J., Ravasi, T., & Hume, D. A. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0603252 · Cited by 4,120
Oncogenic kinase signalling.
Blume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738
Principles of interleukin (IL)-6-type cytokine signalling and its regulation
HEINRICH, P. C., BEHRMANN, I., HAAN, S., HERMANNS, H. M., MÜLLER-NEWEN, G., & SCHAPER, F. (2003) · Biochemical Journal · doi:10.1042/bj20030407 · Cited by 3,272
STATs: transcriptional control and biological impact
Levy, D. E., & Darnell, J. E. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm909 · Cited by 3,201
Regulation of JAK–STAT signalling in the immune system
Shuai, K., & Liu, B. (2003) · Nature reviews. Immunology · doi:10.1038/nri1226 · Cited by 1,410
Mass Spectrometry in Proteomics
Aebersold, R. H., & Goodlett, D. R. (2001) · Chemical Reviews · doi:10.1021/cr990076h · Cited by 1,235
Transcription factors as targets for cancer therapy
Darnell, J. E. (2002) · Nature Reviews Cancer · doi:10.1038/nrc906 · Cited by 1,194
Signaling through the JAK/STAT pathway, recent advances and future challenges
Kisseleva, T., Bhattacharya, S., Braunstein, J., & Schindler, C. (2002) · Gene · doi:10.1016/s0378-1119(02)00398-0 · Cited by 1,170
Activated STAT signaling in human tumors provides novel molecular targets for therapeutic intervention.
Buettner, R., Mora, L. B., & Jove, R. (2002) · PubMed · Cited by 1,036
The molecular details of cytokine signaling via the JAK/STAT pathway
Morris, R., Kershaw, N. J., & Babon, J. J. (2018) · Protein Science · doi:10.1002/pro.3519 · Cited by 943
Signal Transduction and the Control of Gene Expression
Brivanlou, A. H., & Darnell, J. E. (2002) · Science · doi:10.1126/science.1066355 · Cited by 699
Identification of a Nuclear Stat1 Protein Tyrosine Phosphatase
ten Hoeve, J., de Jesus Ibarra-Sanchez, M., Fu, Y., Zhu, W., Tremblay, M., David, M., & Shuai, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5662-5668.2002 · Cited by 507
TYK2 and JAK2 Are Substrates of Protein-tyrosine Phosphatase 1B
Myers, M. P., Andersen, J. N., Cheng, A., Tremblay, M. L., Horvath, C. M., Parisien, J.-P., Salmeen, A. E., Barford, D., & Tonks, N. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100583200 · Cited by 475
Ebola Virus VP24 Binds Karyopherin α1 and Blocks STAT1 Nuclear Accumulation
Reid, S. P., Leung, L. W., Hartman, A. L., Martinez, O., Shaw, M. L., Carbonnelle, C., Volchkov, V. E., Nichol, S. T., & Basler, C. F. (2006) · Journal of Virology · doi:10.1128/jvi.02349-05 · Cited by 463
The role of Stat5a and Stat5b in signaling by IL-2 family cytokines
Lin, J., & Leonard, W. J. (2000) · Oncogene · doi:10.1038/sj.onc.1203523 · Cited by 369
Complex roles of Stat1 in regulating gene expression
Ramana, C. V., Chatterjee‐Kishore, M., Nguyen, H., & Stark, G. R. (2000) · Oncogene · doi:10.1038/sj.onc.1203525 · Cited by 335
Identification of nucleocytoplasmic cycling as a remote sensor in cellular signaling by databased modeling
Swameye, I., Müller, T. G., Timmer, J., Sandra, O., & Klingmüller, U. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0237333100 · Cited by 316
Modulation of STAT signaling by STAT-interacting proteins
Shuai, K. (2000) · Oncogene · doi:10.1038/sj.onc.1203522 · Cited by 379
Interferon α/β-mediated inhibition and promotion of interferon γ: STAT1 resolves a paradox
Nguyen, K. B., Cousens, L. P., Doughty, L., Pien, G. C., Durbin, J. E., & Biron, C. A. (2000) · Nature Immunology · doi:10.1038/76940 · Cited by 303
Transcriptional regulation by STAT1 and STAT2 in the interferon JAK-STAT pathway
Au-Yeung, N., Mandhana, R., & Horvath, C. M. (2013) · JAK-STAT · doi:10.4161/jkst.23931 · Cited by 307
Regulated nuclear import of the STAT1 transcription factor by direct binding of importin‐α
McBride, K. M., Banninger, G., McDonald, C., & Reich, N. C. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1754 · Cited by 289
Inborn errors of human STAT1: allelic heterogeneity governs the diversity of immunological and infectious phenotypes
Boisson‐Dupuis, S., Kong, X., Okada, S., Cypowyj, S., Puel, A., Abel, L., & Casanova, J. (2012) · Current Opinion in Immunology · doi:10.1016/j.coi.2012.04.011 · Cited by 293
A phosphorylation-acetylation switch regulates STAT1 signalingPreprint
Krämer, O. H., Knauer, S. K., Greiner, G., Jandt, E., Reichardt, S., Gührs, K., Stauber, R. H., Böhmer, F., & Heinzel, T. (2009) · Genes & Development · doi:10.1101/gad.479209 · Cited by 282
High local protein concentrations at promoters: Strategies in prokaryotic and eukaryotic cells
Dröge, P., & Müller‐Hill, B. (2001) · BioEssays · doi:10.1002/1521-1878(200102)23:2 · Cited by 60
Survival pathways in hypertrophy and heart failure: The gp130-STAT3 axis
Fischer, P., & Hilfiker‐Kleiner, D. (2007) · Basic Research in Cardiology · doi:10.1007/s00395-007-0674-z · Cited by 271
Sensitization of IFN-γ Jak-STAT signaling during macrophage activation
Hu, X., Herrero, C., Li, W.-P., Antoniv, T. T., Falck-Pedersen, E., Koch, A. E., Woods, J. M., Haines, G. K., & Ivashkiv, L. B. (2002) · Nature Immunology · doi:10.1038/ni828 · Cited by 238
Paramyxoviruses SV5 and HPIV2 Assemble STAT Protein Ubiquitin Ligase Complexes from Cellular Components
Ulane, C. M., & Horvath, C. M. (2002) · Virology · doi:10.1006/viro.2002.1773 · Cited by 227
Cytokine receptor signaling pathways
Leonard, W. J., & Lin, J. (2000) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2000.106899 · Cited by 221
SLIM Is a Nuclear Ubiquitin E3 Ligase that Negatively Regulates STAT Signaling
Tanaka, T., Soriano, M. A., & Grusby, M. J. (2005) · Immunity · doi:10.1016/j.immuni.2005.04.008 · Cited by 205
Nuclear export signal located within the DNA‐binding domain of the STAT1transcription factor
McBride, K. M., McDonald, C., & Reich, N. C. (2000) · The EMBO Journal · doi:10.1093/emboj/19.22.6196 · Cited by 196
Multiple transcription factor families regulate axon growth and regeneration
Moore, D. L., & Goldberg, J. L. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20934 · Cited by 195
Nucleocytoplasmic translocation of Stat1 is regulated by a leucine-rich export signal in the coiled-coil domain
Begitt, A., Meyer, T., van Rossum, M., & Vinkemeier, U. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.190318397 · Cited by 185
Inhibition of IFN-γ Signaling by Glucocorticoids
Hu, X., Li, W.-P., Meng, C. F., & Ivashkiv, L. B. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.9.4833 · Cited by 177
Signal Transducers and Activators of Transcription (STATs): Novel Targets of Chemopreventive and Chemotherapeutic Drugs
Klampfer, L. (2006) · Current Cancer Drug Targets · doi:10.2174/156800906776056491 · Cited by 169
SHP-2 Is a Dual-specificity Phosphatase Involved in Stat1 Dephosphorylation at Both Tyrosine and Serine Residues in Nuclei
Wu, T., Hong, Y. K., Wang, X., Ling, M. Y., Dragoi, A. M., Chung, A. S., Campbell, A. G., Han, Z.-Y., Feng, G., & Chin, Y. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207536200 · Cited by 170
Implications of an antiparallel dimeric structure of nonphosphorylated STAT1 for the activation–inactivation cycle
Zhong, M., Henriksen, M. A., Takeuchi, K., Schaefer, O., Liu, B., ten Hoeve, J., Ren, Z., Mao, X., Chen, X., Shuai, K., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501063102 · Cited by 177
Inhibition of IL-2-induced Jak-STAT signaling by glucocorticoids
Bianchi, M., Meng, C. F., & Ivashkiv, L. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160099797 · Cited by 164
Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domainPreprint
Mertens, C., Zhong, M., Krishnaraj, R., Zou, W., Chen, X., & Darnell, J. E., Jr. (2006) · Genes & Development · doi:10.1101/gad.1485406 · Cited by 170
Survival pathways in hypertrophy and heart failure: The gp130-STAT3 axis
Fischer, P., & Hilfiker‐Kleiner, D. (2007) · Basic Research in Cardiology · doi:10.1007/s00395-007-0658-z · Cited by 161
DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1
Meyer, T., Marg, A., Lemke, P., Wiesner, B., & Vinkemeier, U. (2003) · Genes & Development · doi:10.1101/gad.268003 · Cited by 161
Weapons of STAT destruction
Horvath, C. M. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04425.x · Cited by 161
Expression of suppressors of cytokine signaling during liver regeneration
Campbell, J. S., Prichard, L., Schaper, F., Schmitz, J., Stephenson-Famy, A., Rosenfeld, M. E., Argast, G. M., Heinrich, P. C., & Fausto, N. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11867 · Cited by 156
Signaling by STATs.
Ivashkiv, L. B., & Hu, X. (2004) · Arthritis Research · doi:10.1186/ar1197 · Cited by 160
Functional Interaction of STAT3 Transcription Factor with the Cell Cycle Inhibitor p21 WAF1/CIP1/SDI1 *
Coqueret, O., & Gascan, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001601200 · Cited by 169
STAT proteins: a kaleidoscope of canonical and non-canonical functions in immunity and cancer
Awasthi, N. P., Liongue, C., & Ward, A. C. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01214-y · Cited by 155
Regulation of Stat3 nuclear export
Bhattacharya, S., & Schindler, C. (2003) · Journal of Clinical Investigation · doi:10.1172/jci15372 · Cited by 147
STAT1 and pathogens, not a friendly relationship
Najjar, I., & Fagard, R. (2010) · Biochimie · doi:10.1016/j.biochi.2010.02.009 · Cited by 147
Interferon-α directly represses megakaryopoiesis by inhibiting thrombopoietin-induced signaling through induction of SOCS-1
Wang, Q., Miyakawa, Y., Fox, N. E., & Kaushansky, K. (2000) · Blood · doi:10.1182/blood.v96.6.2093 · Cited by 139
Stat1-Vitamin D Receptor Interactions Antagonize 1,25-Dihydroxyvitamin D Transcriptional Activity and Enhance Stat1-Mediated Transcription
Vidal, M., Ramana, C. V., & Dusso, A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.8.2777-2787.2002 · Cited by 137
Selective STAT Protein Degradation Induced by Paramyxoviruses Requires both STAT1 and STAT2 but Is Independent of Alpha/Beta Interferon Signal Transduction
Parisien, J.-P., Lau, J. F., Rodriguez, J. J., Ulane, C. M., & Horvath, C. M. (2002) · Journal of Virology · doi:10.1128/jvi.76.9.4190-4198.2002 · Cited by 136
CD28 costimulation is required not only to induce IL-12 receptor but also to render Janus kinases / STAT4 responsive to IL-12 stimulation in TCR-triggered T cells
Park, W.-R., Park, C.-S., Tomura, M., Ahn, H.-J., Nakahira, Y., 岩崎, 正., Gao, P. H., Abe, R., Hamaoka, T., & Fujiwara, H. (2001) · European Journal of Immunology · doi:10.1002/1521-4141(200105)31:5 · Cited by 20
Paramyxovirus strategies for evading the interferon response
Gotoh, B., Komatsu, T., Takeuchi, K., & Yokoo, J. (2002) · Reviews in Medical Virology · doi:10.1002/rmv.357 · Cited by 131
A Drosophila PIAS homologue negatively regulates stat92E
Betz, A., Lampen, N., Martinek, S., Young, M. W., & Darnell, J. E., Jr. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171302098 · Cited by 132
Paradigm shifts in the cell biology of STAT signaling
Sehgal, P. B. (2008) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.07.003 · Cited by 135
Cyanidin-3-Glucoside Suppresses Cytokine-Induced Inflammatory Response in Human Intestinal Cells: Comparison with 5-Aminosalicylic Acid
Serra, D., Paixão, J., Nunes, C., Dinis, T. C. P., & Almeida, L. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073001 · Cited by 124
STAT1-induced Apoptosis Is Mediated by Caspases 2, 3, and 7
Sironi, J., & Ouchi, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307774200 · Cited by 123
Distinct roles of the NH 2 - and COOH-terminal domains of the protein inhibitor of activated signal transducer and activator of transcription (STAT) 1 (PIAS1) in cytokine-induced PIAS1–Stat1 interaction
Liao, J., Fu, Y., & Shuai, K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5267 · Cited by 116
Cyclin D1 Represses STAT3 Activation through a Cdk4-independent Mechanism
Bienvenu, F., Gascan, H., & Coqueret, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100795200 · Cited by 115
STAT3-dependent enhanceosome assembly and disassembly: synergy with GR for full transcriptional increase of the α2-macroglobulin genePreprint
Lerner, L. R., Henriksen, M. A., Zhang, X., & Darnell, J. E., Jr. (2003) · Genes & Development · doi:10.1101/gad.1135003 · Cited by 116
Signal transducers and activators of transcription as regulators of growth, apoptosis and breast development
Bromberg, J. (2000) · Breast Cancer Research · doi:10.1186/bcr38 · Cited by 113
Viral inhibition of MHC class II antigen presentation
Hegde, N. R. (2003) · Trends in Immunology · doi:10.1016/s1471-4906(03)00099-1 · Cited by 101
Pharmaceutical intervention in the JAK/STAT signaling pathway
Seidel, H. M., Lamb, P., & Rosen, J. (2000) · Oncogene · doi:10.1038/sj.onc.1203550 · Cited by 97
Oncostatin M: a pleiotropic cytokine in the central nervous system
Chen, S., & Benveniste, E. N. (2004) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2004.06.002 · Cited by 97
The role of signal transducers and activators of transcription in colon cancer
Klampfer, L. (2007) · Frontiers in bioscience · doi:10.2741/2893 · Cited by 97
Phospho-Ser727 of STAT3 regulates STAT3 activity by enhancing dephosphorylation of phospho-Tyr705 largely through TC45
Wakahara, R., Kunimoto, H., Tanino, K., Kojima, H., Inoue, A., Shintaku, H., & Nakajima, K. (2012) · Genes to Cells · doi:10.1111/j.1365-2443.2011.01575.x · Cited by 95
Silencing STATs: lessons from paramyxovirus interferon evasion
Horvath, C. M. (2004) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2004.02.003 · Cited by 96
Arginine Methylation of STAT1 Regulates Its Dephosphorylation by T Cell Protein Tyrosine Phosphatase
Zhu, W. Z., Mustelin, T., & David, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200346200 · Cited by 94
Cell Type-Specific and Tyrosine Phosphorylation-Independent Nuclear Presence of STAT1 and STAT3
Meyer, T., Gavénis, K., & Vinkemeier, U. (2002) · Experimental Cell Research · doi:10.1006/excr.2001.5405 · Cited by 94
GATA-3 transcriptional imprinting in Th2 lymphocytes: A mathematical model
Höfer, T., Nathansen, H., Löhning, M., Radbruch, A., & Heinrich, R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142284699 · Cited by 90
P-STAT1 mediates higher-order chromatin remodelling of the human MHC in response to IFNγ
Christova, R., Jones, T. A., Wu, P., Bolzer, A., Costa‐Pereira, A. P., Watling, D., Kerr, I. M., & Sheer, D. (2007) · Journal of Cell Science · doi:10.1242/jcs.012328 · Cited by 93
STAT1 from the cell membrane to the DNA
Lillemeier, B. F., Köster, M., & Kerr, I. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.10.2508 · Cited by 88
STAT signalling in cell proliferation and in development
Williams, J. G. (2000) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00119-2 · Cited by 85
STAT Signaling in Glioma Cells
Swiatek-Machado, K., & Kaminska, B. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-30651-9_10 · Cited by 86
Noncytolytic Clearance of Sindbis Virus Infection from Neurons by Gamma Interferon Is Dependent on Jak/Stat Signaling
Burdeinick-Kerr, R., Govindarajan, D., & Griffin, D. E. (2009) · Journal of Virology · doi:10.1128/jvi.02381-08 · Cited by 81
MUC1 gene overexpressed in breast cancer: structure and transcriptional activity of the MUC1 promoter and role of estrogen receptor alpha (ERalpha) in regulation of the MUC1 gene expression.
Zaretsky, J. Z., Barnea, I., Aylon, Y., Gorivodsky, M., Wreschner, D. H., & Keydar, I. (2006) · Molecular Cancer · doi:10.1186/1476-4598-5-57 · Cited by 80
SHP2 Is Overexpressed and Inhibits pSTAT1-Mediated APM Component Expression, T-cell Attracting Chemokine Secretion, and CTL Recognition in Head and Neck Cancer Cells
Leibowitz, M. S., Srivastava, R. M., Filho, P. A. A., Egloff, A. M., Wang, L., Seethala, R. R., Ferrone, S., & Ferris, R. L. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-1517 · Cited by 76
Regulation of STAT1 Nuclear Export by Jak1
Mowen, K. A., & David, M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7273-7281.2000 · Cited by 75
Prolactin-induced production of cytokines in macrophages in vitro involves JAK/STAT and JNK MAPK pathways
Tripathi, A., & Sodhi, A. (2008) · International Immunology · doi:10.1093/intimm/dxm145 · Cited by 74
Ubiquitin-Specific Protease 13 Regulates IFN Signaling by Stabilizing STAT1
Yeh, H.-M., Yu, C.-Y., Yang, H.-C., Ko, S.-H., Liao, C., & Lin, Y. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300225 · Cited by 73
STAT Signaling in Glioma Cells
Swiatek-Machado, K., & Kaminska, B. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-4719-7_10 · Cited by 74
Proteasome-mediated Degradation of STAT1α following Infection of Macrophages with Leishmania donovani
Forget, G., Gregory, D. J., & Olivier, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414126200 · Cited by 71
Modeling the nonlinear dynamics of cellular signal transduction
TIMMER, J., MÜLLER, T. G., SWAMEYE, I., SANDRA, O., & KLINGMÜLLER, U. (2004) · International Journal of Bifurcation and Chaos · doi:10.1142/s0218127404010461 · Cited by 68
A Functional Nuclear Localization Sequence in the C-terminal Domain of SHP-1
Craggs, G., & Kellie, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102846200 · Cited by 68
Sendai virus C protein impairs both phosphorylation and dephosphorylation processes of Stat1
Komatsu, T., Takeuchi, K., Yokoo, J., & Gotoh, B. (2002) · FEBS Letters · doi:10.1016/s0014-5793(01)03301-4 · Cited by 66
Stat3 isoforms, α and β, demonstrate distinct intracellular dynamics with prolonged nuclear retention of Stat3β mapping to its unique C-terminal end
Huang, Y., Qiu, J., Dong, S., Redell, M. S., Poli, V., Mancini, M. A., & Tweardy, D. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704548200 · Cited by 65
Regulation of hepatic stellate cell activation and growth by transcription factor myocyte enhancer factor 2
Xuemin, W., Tang, X., Gong, X., Albanis, E., Friedman, S. L., & Mao, Z. (2004) · Gastroenterology · doi:10.1053/j.gastro.2004.07.007 · Cited by 65
Turning off signal transducer and activator of transcription (STAT): The negative regulation of STAT signaling
Chen, W., Daines, M., & Hershey, G. K. K. (2004) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2004.06.042 · Cited by 66
Human Cytomegalovirus IE1 Protein Elicits a Type II Interferon-Like Host Cell Response That Depends on Activated STAT1 but Not Interferon-γ
Knoblach, T., Grandel, B., Seiler, J., Nevels, M. M., & Paulus, C. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002016 · Cited by 62
Conservation of a Unique Mechanism of Immune Evasion across the Lyssavirus Genus
Wiltzer, L., Larrous, F., Oksayan, S., Ito, N., Marsh, G. A., Wang, L. F., Blondel, D., Bourhy, H., Jans, D. A., & Moseley, G. W. (2012) · Journal of Virology · doi:10.1128/jvi.01249-12 · Cited by 63
Decoding inflammation, its causes, genomic responses, and emerging countermeasures
Hawiger, J., & Zienkiewicz, J. (2019) · Scandinavian Journal of Immunology · doi:10.1111/sji.12812 · Cited by 62
Anti-Inflammatory Effects of Ellagic Acid on Keratinocytes via MAPK and STAT Pathways
Gil, T., Hong, C.-H., & An, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031277 · Cited by 62
STAT-1 and c-Fos interaction in nitric oxide synthase-2 gene activation
Xu, W., COMHAIR, S. A. A., Zheng, S., Chu, S. C., Marks-Kończalik, J., Moss, J., Haque, S. J., & ERZURUM, S. C. (2003) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00441.2002 · Cited by 60
Intercellular Adhesion Molecule-1 (ICAM-1) Gene Expression in Human T Cells Is Regulated by Phosphotyrosyl Phosphatase Activity
Roy, J., Audette, M., & Tremblay, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005067200 · Cited by 57
The Amino-Terminal Extensions of the Longer Sendai Virus C Proteins Modulate pY701-Stat1 and Bulk Stat1 Levels Independently of Interferon Signaling
Garcin, D., Marq, J., Goodbourn, S., & Kolakofsky, D. (2003) · Journal of Virology · doi:10.1128/jvi.77.4.2321-2329.2003 · Cited by 57
STAT dynamics
Reich, N. C. (2007) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2007.06.021 · Cited by 55
Impairment of Interferon-Induced IRF-7 Gene Expression due to Inhibition of ISGF3 Formation by Trichostatin A
Génin, P., Morin, P., & Civas, A. (2003) · Journal of Virology · doi:10.1128/jvi.77.12.7113-7119.2003 · Cited by 53
Stat5 in the mammary gland: Controlling normal development and cancer
Barash, I. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20771 · Cited by 54
Nuclear β-Arrestin1 Functions as a Scaffold for the Dephosphorylation of STAT1 and Moderates the Antiviral Activity of IFN-γ
Mo, W., Zhang, L., Yang, G., Zhai, J., Hu, Z., Chen, Y., Chen, X., Hui, L., Huang, R., & Hu, G. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.06.017 · Cited by 51
Signal transduction by type I interferons.
David, M. (2002) · BioTechniques · doi:10.2144/oct0207 · Cited by 61
Nuclear tyrosine phosphorylation: the beginning of a map
Cans, C., Mangano, R., Barilà, D., Neubauer, G., & Superti‐Furga, G. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(00)00434-2 · Cited by 47

Authors: Haspel, R. L., & Darnell, J. E.
Affiliations: Rockefeller University (US)
ORCID: Haspel, Richard L.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1999-08-31
Volume: 96
Issue: 18
Pages: 10188-10193
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.96.18.10188
PMC: PMC17864
OpenAlex: W2120019133
Cited by: 203
References: 36
Citations by year: 2026: 1 · 2025: 1 · 2024: 2 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 5 · 2019: 6 · 2018: 3 · 2017: 1 · 2015: 4 · 2014: 6 · 2013: 10 · 2012: 7
FWCI: 8.69
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Cancer Institute (CA 09673, T32CA009673)
National Institute of Allergy and Infectious Diseases (AI 32849, R37AI034420, AI 34420, R01AI032489)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
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
Keywords: STAT1, protein tyrosine phosphatase, nuclear export, Janus kinase, staurosporine, nuclear translocation, sodium vanadate, transcription factor regulation
MeSH terms: Animals, Cell Line, Cell Nucleus, DNA-Binding Proteins, Humans, Kinetics, Phosphorylation, Protein-Tyrosine Kinases, Recombinant Proteins, Transfection, Vanadates, Signal Transduction, Trans-Activators, Mutagenesis, Site-Directed, Protein Tyrosine Phosphatases, Staurosporine, STAT1 Transcription Factor, Mice

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

A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks