The DOI matches its Crossref record; 138 of the 138 references it cites were found in a registry or an index.
Phosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival
Abstract
Mitogen-activated protein kinase (MAPK) pathways constitute a large modular network that regulates a variety of physiological processes, such as cell growth, differentiation, and apoptotic cell death. The function of the ERK pathway has been depicted as survival-promoting, in essence by opposing the proapoptotic activity of the stress-activated c-Jun NH(2)-terminal kinase (JNK)/p38 MAPK pathways. However, recently published work suggests that extracellular regulated kinase (ERK) pathway activity is suppressed by JNK/p38 kinases during apoptosis induction. In this review, we will summarize the current knowledge about JNK/p38-mediated mechanisms that negatively regulate the ERK pathway. In particular, we will focus on phosphatases (PP2A, MKPs) as inhibitors of ERK pathway activity in regulating apoptosis. A model proposed in this review places the negative regulation of the ERK pathway in a central position for the cellular decision-making process that determines whether cells will live or die in response to apoptosis-promoting signals. In addition, we will discuss the potential functional relevance of negative regulation of ERK pathway activity, for physiological and pathological conditions (e.g., cellular transformation).
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“The p38 pathway has been reported to interfere with ERK activity during apoptosis (see 88 for review); thus, ERK activity was assayed in these genotypes by measuring phospho-ERK levels.”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [88]
Citations
Cites
1 retracted
A Regulatory Role for p38δ MAPK in Keratinocyte Differentiation
Efimova, T., Broome, A., & Eckert, R. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302759200 · Cited by 135
RetractedMutations of the BRAF gene in human cancer
Davies, H., Bignell, G. R., Cox, C., Stephens, P., Edkins, S., Clegg, S., Teague, J., Woffendin, H., Garnett, M. J., Bottomley, W., et al. (2002) · Nature · doi:10.1038/nature00766 · Cited by 10,674
Opposing Effects of ERK and JNK-p38 MAP Kinases on Apoptosis
Xia, Z., Dickens, M., Raingeaud, J., Davis, R. J., & Greenberg, M. E. (1995) · Science · doi:10.1126/science.270.5240.1326 · Cited by 5,273
Signal transduction by the JNK group of MAP kinases
Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
AP-1 as a regulator of cell life and death
Shaulian, E., & Karin, M. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e131 · Cited by 2,961 · cited 1×
“The most classical JNK substrate is the transcription factor c-Jun, from which JNK derived its name (2, 5, 33).”
BackgroundProtein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling
Hunter, T. R. (1995) · Cell · doi:10.1016/0092-8674(95)90405-0 · Cited by 2,961
Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
Roberts, P. J., & Der, C. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210422 · Cited by 2,788
Roux, P. P., & Blenis, J. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.2.320-344.2004 · Cited by 2,540
Raingeaud, J., Gupta, S., Rogers, J. S., Dickens, M., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7420 · Cited by 2,244
Research works printed but not linked: 1
- 10.1042/bj3530417 · DOI
Cited by
Sorted by citations
Items 701–800 of 826
Radhakrishnan, H. R. G., Chithamparam, P., & Muthukumaran, A. (2026) · Springer eBooks · doi:10.1007/978-981-96-9670-3_11 · Cited by 1
He, W., Sun, Y., Liang, W., Lan, J., & Xiong, Y. (2026) · Transplantation Proceedings · doi:10.1016/j.transproceed.2025.12.011 · Cited by 1
Antiviral effect of chelerythrine chloride against tick-borne encephalitis virus
Li, J., Zhao, D., Yan, S., Qiu, L., Qin, H., Gao, X., Jiang, B., Yu, W., Zhu, Y., Tao, Y., et al. (2026) · Virology Journal · doi:10.1186/s12985-026-03125-1 · Cited by 1
Self-citationZhong, Y., Xiao, C., Liang, Y., Wang, P., Long, Y., Li, S., Song, N., Shang, W., Yang, W., & Zhang, X. (2026) · Natural Products and Bioprospecting · doi:10.1007/s13659-026-00593-4 · Cited by 1
Self-citationEffects of transfection of ICAP-1α and its mutants on adhesion and migration of 2H-11 cells
Zhang, J., Luo, W., Liu, Z., Lin, J., & Cheng, Z. (2010) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-010-0544-z · Cited by 1
Ding, K. (2014) · Medicinal Chemistry · doi:10.4172/2161-0444.1000187 · Cited by 1
Morotomi‐Yano, K., & Yano, K. (2015) · Cited by 1
Correlation between spina bifida manifesta in fetal rats and c-Jun N-terminal kinase signaling.
Ma, Y., Bao, Y., Li, C., Jiao, F., Xin, H., & Yuan, Z. (2012) · PubMed Central · doi:10.3969/j.issn.1673-5374.2012.32.001 · Cited by 1
Babar, S. M. E., Islam, M. F., Rahman, K. M. T., & Sumi, S. S. (2013) · International Journal of Bioscience Biochemistry and Bioinformatics · doi:10.7763/ijbbb.2013.v3.184 · Cited by 1
Albrecht, W., & Laufer, S. (2012) · Royal Society of Chemistry eBooks · doi:10.1039/9781849735346-00137 · Cited by 1
Jia, L., Li, X., Gu, Y., & Cui, W. (2016) · American Journal of Nephrology · doi:10.1159/000450838 · Cited by 1
Anti-cancer effects of lucidadiol against malignant melanoma cells
Shin, S.-A., Lee, J. S., Joo, B. J., Ryu, G., Han, M., Kim, H., An, J., Koo, M. H., Youn, U. J., Lee, J. H., et al. (2021) · Applied Biological Chemistry · doi:10.1186/s13765-021-00647-w · Cited by 1
Lu, X., Guifang, J., Hehan, Y., & Hong, Y. H. (2021) · Journal of Holistic Integrative Pharmacy · doi:10.1016/s2707-3688(23)00080-8 · Cited by 1
Zeng, P., Wu, X., Chen, C., Zhang, J., Rashid, H. U., & Zhang, P. (2024) · Peptide Science · doi:10.1002/pep2.24371 · Cited by 1
GPSD: a hybrid learning framework for the prediction of phosphatase-specific dephosphorylation sites
Han, C., Fu, S., Chen, M., Gou, Y., Liu, D., Zhang, C., Huang, X., Xiao, L., Zhao, M., Zhang, J., et al. (2024) · Briefings in Bioinformatics · doi:10.1093/bib/bbae694 · Cited by 1
(2015) · Inflammation and Cell Signaling · doi:10.14800/ics.926 · Cited by 1
Signaling Pathways in Giardia lamblia
Lauwaet, T., & Gillin, F. D. (2011) · Springer eBooks · doi:10.1007/978-3-7091-0198-8_12 · Cited by 1
Glucocorticoid-Induced Cardioprotection: A Novel Role for Autophagy
Engelbrecht, A., & Loos, B. (2012) · InTech eBooks · doi:10.5772/52406 · Cited by 1
dos Santos, A. R., Lopes-Costa, P. V., Gontijo, J. A. R., & da Silva, B. B. (2012) · European Journal of Obstetrics & Gynecology and Reproductive Biology · doi:10.1016/j.ejogrb.2012.05.036 · Cited by 1
Information Theoretical Study of Cross-Talk Mediated Signal Transduction in MAPK Pathways
Maity, A. K., Chaudhury, P., & Banik, S. K. (2017) · Entropy · doi:10.3390/e19090469 · Cited by 1
Sharma, M., Webber, S. A., Zeevi, A., & Mohanakumar, T. (2019) · Human Immunology · doi:10.1016/j.humimm.2019.01.008 · Cited by 1
Consequences of Oxidative Stress and ROS-Mediated Pathways Cellular Signaling Stress Response
Madkour, L. H. (2020) · Nanomedicine and nanotoxicology · doi:10.1007/978-3-030-37297-2_5 · Cited by 1
Dendritic cells in cancer immunotherapy
Gato, M., Liechtenstein, T., Blanco‐Luquin, I., Zudaire, I., Kochan, G. T., & Escors, D. (2015) · Anales del Sistema Sanitario de Navarra · doi:10.23938/assn.0077 · Cited by 1
Jauregui, D., Khogali, M. K., Xing, Y., Fan, X., Wen, K., Liu, L., Zhao, M., Geng, T., & Gong, D. (2022) · Agriculture · doi:10.3390/agriculture12030347 · Cited by 1
Fong, L. E., Bass, V. L., Spudich, S., & Miller‐Jensen, K. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/371922 · Cited by 1
Duc, D. L., & Schöneberg, T. (2019) · Oxford University Press eBooks · doi:10.1093/oxfordhb/9780198789666.013.2 · Cited by 1
Biswas, D., Dao, K. T., Mercer, A., Cowie, A. M., Duffley, L., Hiani, Y. E., Kienesberger, P. C., & Pulinilkunnil, T. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.21.960153 · Cited by 1
Fomina‐Yadlin, D., Kubicek, S., Vetere, A., He, K. H. H., Schreiber, S. L., & Wagner, B. K. (2012) · PLoS ONE · doi:10.1371/annotation/c41ac082-32ac-4837-b4ed-9fd8ad91c1e0 · Cited by 1
Wang, J., Xiao, B., Kimura, E., Mongan, M., Hsu, W.-W., Medvedovic, M., Puga, A., & Xia, Y. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.14.585101 · Cited by 1
Tumour suppressor proteins in proliferating and differentiating cells
Bodalina, U. M. (2014) · University of the Witwatersrand, Johannesburg Institutional Repository on DSpace (University of the Witwatersrand, Johannesburg)
Santamaría, P. (2011) · Gredos (University of Salamanca) · doi:10.14201/gredos.108987
Blume, L. C., Eldeeb, K., & Howlett, A. C. (2014) · doi:10.1002/9781118451281.ch2
Receptores vanilóides TRPV1 na retina.
Leonelli, M. (2011) · doi:10.11606/t.42.2011.tde-22072011-131242
Casein kinase 2 controls synapse organization and stability
Bulat, V. (2013) · edoc (University of Basel) · doi:10.5451/unibas-006136875
Neural stem cell characteristics affected by oncogenic pathways and in a human motoneuron disease
Kerosuo, L. (2009) · Työväentutkimus Vuosikirja
Rewiring ret : PTB-adaptor regulated signaling and cell biology
Lundgren, K. C. (2008) · Figshare
Casteel, M. (2011) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.12823
Estudio de las vías de supervivencia y muerte neuronal en modelos de la enfermedad de Huntington
Rubia, P. P. (2010) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya)
MicroRNA-155 mediates sepsis-associated cardiovascular dysfunction
Carreiras, F. B. (2015) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) · doi:10.34626/1vmm-d187
Gonda, R. L. (2011) · D-Scholarship@Pitt (University of Pittsburgh)
Discovering Novel Feedback and Crosstalk Mechanisms in Cellular Signaling Pathways
Er, E. E. (2013) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)
Two epithelial cell lines, MCF7 and HCC2998, dissociate after hyperactivation of p38 MAP kinase
Okoshi, R., Shu, C.-L., & Fukui, Y. (2012) · HOAJ Biology · doi:10.7243/2050-0874-1-12
Brederlau, A. (2008) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Identification and validation of therapeutic targets in sarcoma models
Maruwge, W. (2009) · Figshare
Regulation of nerve growth factor signaling by protein phosphatase 2A
Kanegan, M. J. V. (2008) · doi:10.17077/etd.23exfh2c
Kudrna, R. A. (2014) · KU ScholarWorks (The University of Kansas)
CROSSTALK FACILITATES SPATIAL SIGNAL PROPAGATION THROUGH MAPK CASCADES
ZHANG, Y., Chen, K., Wang, J., CHEN, A., Meichun, Z., & Zhou, T. (2009) · Journal of Biological Systems · doi:10.1142/s0218339009002855
Sweeney, T. E. (2010) · DukeSpace (Duke University)
Castro, N. (2010) · University of Minnesota Digital Conservancy (University of Minnesota)
Xenobiotic-metabolizing enzymes elevated in multiple mouse models of slow aging
Steinbaugh, M. J. (2012) · Deep Blue (University of Michigan)
Role of Myostatin in oxidative stress in skeletal muscle
Sandhya, S. (2013) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/53725
MICROCYSTIN-LR INDUCES PHOSPHORYLATION OF ERK AND JNK IN HUMAN HEPATOCYTE HL7702
Sun, Y., Huang, P., & Xu, L. (2011) · Acta Hydrobiologica Sinica · doi:10.3724/issn1000-3207-2011-1-180-2
Regulation of IL-12, IL-23, IL-27 in Response to IFN-γ/LPS in Human Monocytes and Macrophages
Blahoianu, M. A. (2013) · uO Research (University of Ottawa) · doi:10.20381/ruor-3302
München, F. D. L.-M.-U. (2013)
Vrana, J. A. (2015) · The Research Repository @ WVU (West Virginia University) · doi:10.33915/etd.6880
AVALIAÇÃO IN VITRO DO POTENCIAL BIOLÓGICO DE MYRCIARIA PLINIOIDES (D. LEGRAND) EM CÉLULAS TUMORAIS
Leipelt, J. (2016) · Americanae (AECID Library)
Shah, S. (2016) · Libraries and Cultural Resources (University of Calgary) · doi:10.11575/prism/26991
Cell Memory in the Mitogen-Activated Protein Kinase Signaling Pathway
Lyashenko, E. (2015) · doi:10.7916/d8rf5svz
Regulation of Metalloproteinase-dependent Ectodomain Shedding in Cytokine Biology and Inflammation
Murthy, A. (2012) · Library and Archives Canada (Government of Canada)
ヒト歯肉線維芽細胞の増殖,接着およびERK 1/2シグナルに対するエムドゲイン由来合成ペプチドの影響
大輔, 木., 弘仁, 嘉., 和也, 富., 正皓, 野., 伸浩, 山., 直季, 橋., 安井, 菜., 田口, 洋., 昭男, 田., & 誠, 梅. (2017) · 歯科医学 · doi:10.18905/shikaigaku.80.1_1
Protein engineering of p38 MAP kinase for substrate identification
Yasovich, N. (2012) · York University Digital Library (York University)
Kato, H., Taguchi, Y., Tominaga, K., Noguchi, M., Imai, K., Ruan, Y., Takahashi, S., Kimura, D., Shida, M., Taguchi, R., et al. (2018) · Preprints.org · doi:10.20944/preprints201801.0037.v1
Adaptive approach to melanoma cancer using mapk pathway
Sidharth, B., Priya, K., & Pallavi, M. S. (2017) · International Conference on Communications and Signal Processing (ICCSP) · doi:10.1109/iccsp.2017.8286628
Jung, T. W., Kim, S., Kim, D., Shin, E., Park, Y. B., & Lee, K. (2018) · Pharmacology · doi:10.1159/000487892
Cardioprotection by Drug-Induced Changes in Glucose and Glycogen Metabolism
Omar, M. A. (2012) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3x923
Lactoferrin Promotes Proliferation and Wound Healing of Human Gingival Fibroblasts -in vitro study
Suzuki, N. (2019) · 日本歯周病学会会誌 · doi:10.2329/perio.61.18
A Toxicological Application of Signal Transduction
Miller, J. V., Prince, N., Mouch, J. A., & Boyd, J. W. (2019) · doi:10.1002/9781119060208.ch8
Interplays and feedback loops of oncogenic signaling pathways in B cell non-Hodgkin lymphoma
Rausch, I. (2019) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7302
Microfluidic Approaches for Probing Protein Phosphorylation in Cells
Deng, J. (2018) · VTechWorks (Virginia Tech)
Articular Cartilage Development
Athanasiou, K. A., Darling, E. M., DuRaine, G. D., Hu, J. C. Y., & Reddi, A. H. (2017) · doi:10.1201/9781315194158-2
The Key Role of the Phosphatase PP2A in the Development of Acute Myeloid Leukemia
Marco, J., Peris, I., Vicente, C., & Arriazu, E. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.94380
Chen, Y., Kato, H., Taguchi, Y., Kimura, D., Nakata, T., Tominaga, K., & Umeda, M. (2021) · Journal of Osaka Dental University · doi:10.18905/jodu.55.2_219
Ito, O., Ido, K., Ishido, K., & Hitotsumatsu, T. (2012) · PubMed
Derry, W. B. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718188163.793487867
Articular Cartilage Development
(2013) · CRC Press eBooks · doi:10.1201/b14183-3
Silke, J. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733218432.793575596
Zavala, M. (2022) · El Servicio de Difusión de la Creación Intelectual (National University of La Plata) · doi:10.35537/10915/139765
Gupta, N., Ansari, S., Verma, R., Singh, O. N., Yadav, M. K., Binayke, A., Jakhar, K., Mani, S., Awasthi, A., Shalimar, S., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.05.502940
Rémy, É., Rebouissou, S., Chaouiya, C., Zinovyev, A. Y., Radvanyi, F., & Calzone, L. (2023) · doi:10.1158/0008-5472.22407093
Workman, H. C., Sweeney, C. A., & Carraway, K. L. (2023) · doi:10.1158/0008-5472.c.6499766.v1
Puustinen, P., Junttila, M. R., Vanhatupa, S., Sablina, A. A., Hector-Greene, M., Teittinen, K. J., Raheem, O., Ketola, K., Lin, S., Kast, J., et al. (2023) · doi:10.1158/0008-5472.c.6499386.v1
Self-citationRémy, É., Rebouissou, S., Chaouiya, C., Zinovyev, A. Y., Radvanyi, F., & Calzone, L. (2023) · doi:10.1158/0008-5472.22407093.v1
Puustinen, P., Junttila, M. R., Vanhatupa, S., Sablina, A. A., Hector-Greene, M., Teittinen, K. J., Raheem, O., Ketola, K., Lin, S., Kast, J., et al. (2023) · doi:10.1158/0008-5472.22379901
Self-citationWu, M., Wei, X., Chen, Q., Liu, Y., He, Y., Zhang, K., Liu, Y., & Wei, W. (2024) · Research Square · doi:10.21203/rs.3.rs-3898800/v1
Ruan, L., Zheng, M., Xia, X., Pang, C., Wang, Y., Fan, Z., Yang, J., Qing, Q., Lin, H., Tao, Y., et al. (2024) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/0113862073285988240229081558
Imtiyaz, K., Shafi, M., Mirza, B., & Rizvi, M. M. A. (2025) · Pharmacological Research - Natural Products · doi:10.1016/j.prenap.2025.100347
Metadata
- Authors
- Junttila, M. R., Li, S., & Westermarck, J.
- Affiliations
- Åbo Akademi University (FI)
- University of Helsinki (FI)
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2007-11-26
- Volume
- 22
- Issue
- 4
- Pages
- 954-965
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2003060606
- Cited by
- 826
- References
- 138
- Citations by year
- 2026: 12 · 2025: 21 · 2024: 24 · 2023: 19 · 2022: 32 · 2021: 48 · 2020: 28 · 2019: 36 · 2018: 42 · 2017: 41 · 2016: 58 · 2015: 49 · 2014: 76 · 2013: 72 · 2012: 74
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- ERK signaling, phosphatase, protein phosphatase 2A, apoptosis, cell survival
- MeSH terms
- Animals, Cell Survival, Humans, Models, Biological, Phosphoprotein Phosphatases, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System
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