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Gene regulation in the immediate-early response process
Open accessAbstract
Immediate-early genes (IEGs) can be activated and transcribed within minutes after stimulation, without the need for de novo protein synthesis, and they are stimulated in response to both cell-extrinsic and cell-intrinsic signals. Extracellular signals are transduced from the cell surface, through receptors activating a chain of proteins in the cell, in particular extracellular-signal-regulated kinases (ERKs), mitogen-activated protein kinases (MAPKs) and members of the RhoA-actin pathway. These communicate through a signaling cascade by adding phosphate groups to neighboring proteins, and this will eventually activate and translocate TFs to the nucleus and thereby induce gene expression. The gene activation also involves proximal and distal enhancers that interact with promoters to simulate gene expression. The immediate-early genes have essential biological roles, in particular in stress response, like the immune system, and in differentiation. Therefore they also have important roles in various diseases, including cancer development. In this paper we summarize some recent advances on key aspects of the activation and regulation of immediate-early genes.
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From Comparative Analysis of HPA-Axis Dysregulation and Dynamic Molecular Mechanisms in Acute Versus Chronic Social Defeat Stress (2025) · cites this paper as [45]
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“these are known to regulate neuronal activity and inflammatory responses under stress conditions”
From Comparative Analysis of HPA-Axis Dysregulation and Dynamic Molecular Mechanisms in Acute Versus Chronic Social Defeat Stress (2025) · cites this paper as [45]
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Liu, J., Grogan, L., Nau, M., Allegra, C. J., Chu, E., & Wright, J. J. (2001) · International Journal of Oncology · doi:10.3892/ijo.18.4.863 · Cited by 66
Angiotensin II–Stimulated Signaling Through G Proteins and β-Arrestin
Shenoy, S. K., & Lefkowitz, R. (2005) · Science's STKE · doi:10.1126/stke.3112005cm14 · Cited by 65
Bebien, M., Salinas, S., Bécamel, C., Richard, V., Linares, L. K., & Hipskind, R. (2003) · Oncogene · doi:10.1038/sj.onc.1206334 · Cited by 65
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“…signal, such as growth factors (e.g. platelet-derived growth factor (PDGF) and epidermal growth factor (EGF)), mitogens and phorbol esters, immunological and neurological signals, developmental, and stress (e.g. UV, toxins) (Herschman, 1991; Morgan and Curran, 1991; O'Donnell et al., 2012).”
BackgroundTranscriptional Dynamics Reveal Critical Roles for Non-coding RNAs in the Immediate-Early Response
Aitken, S., Magi, S., Alhendi, A. M. N., Itoh, M., Kawaji, H., Lassmann, T., Daub, C. O., Arner, E., Carninci, P., Forrest, A. R. R., et al. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004217 · Cited by 64 · cited 2×
“After stimulation of IEG expression the production of these microRNAs is blocked, but then comes quickly back to normal levels (Aitken et al., 2015; Avraham et al., 2010).”
BackgroundDynamic bookmarking of primary response genes by p300 and RNA polymerase II complexes
Byun, J. S., Wong, M., Cui, W., Idelman, G., Li, Q., Siervi, A. D., Bilke, S., Haggerty, C. M., Player, A. N., Wang, Y. H., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905469106 · Cited by 61 · cited 3×
“The importance of the control of MKL1 activation by TCFs or other factors is clear in megakaryoblastic leukemia, where MKL1 is fused to the RBM15 protein and activated due to constitutive nuclear localization (Cen et al., 2003; Guettler et al., 2008).”
BackgroundZhang, F., Lin, M., Abidi, P., Thiel, G., & Liu, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305564200 · Cited by 60
Spaapen, F., van den Akker, G., Caron, M. M. J., Prickaerts, P., Rofel, C., Dahlmans, V. E. H., Surtel, D. A., Paulis, Y. W. J., Schweizer, F., Welting, T. J. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058083 · Cited by 50
Convergence of the SUMO and MAPK pathways on the ETS-domain transcription factor Elk-1.
Yang, S.-H., & Sharrocks, A. (2006) · Biochemical Society Symposium · doi:10.1042/bss0730121 · Cited by 49 · cited 2×
“The TCF component is a receptor of this signal, being a direct MAPK phosphorylation target (Selvaraj et al., 2015; Shaw and Saxton, 2003; Yang and Sharrocks, 2006).”
BackgroundRegulation of lymphocyte fate by Ras/ERK signals
Yasuda, T., & Kurosaki, T. (2008) · Cell Cycle · doi:10.4161/cc.7.23.7103 · Cited by 48 · cited 1×
“…in mammalian cells, including ERK (extracellular signal regulated kinase), RSK (p90 ribosomal S6 kinase), JNK (c-Jun N-terminal kinase), p38, and ERK5 (extracellular signal regulated kinase-5, also called Big MAP kinase-1 (BMK1)) (Raman et al., 2007; Yang et al., 2003; Yasuda and Kurosaki, 2008).”
BackgroundRegulation of Egr-1 by association with the proteasome component C8.
Bae, M., Jeong, C.-H., Kim, S.-H., Bae, M., Jeong, J.-W., Ahn, M., Bae, S., Kim, N., Kim, C., Kim, K., et al. (2002) · Biochimica et Biophysica Acta · doi:10.1016/s0167-4889(02)00310-5 · Cited by 45 · cited 2×
“…and non-DNA-binding domains (Bahrami et al., 2015), it has interaction with CEBPB, PSMA3 and P53 and is involved in the regulation of cell growth and differentiation in response to signals such as mitogens, growth factors, and stress stimuli (Bae et al., 2002; Liu et al., 2001; Zhang et al., 2003).”
BackgroundFos family protein degradation by the proteasome.
Gomard, T., Jariel-Encontre, I., Basbous, J., Bossis, G., Mocquet-Torcy, G., & Piechaczyk, M. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360858 · Cited by 40 · cited 2×
“For example, expression of the FOS gene peaks 30e60min after stimulation, and returns to basal expression after 90min (Greenberg and Ziff, 1984).”
BackgroundCascades of transcriptional induction during human lymphocyte activation.
Ellisen, L., Palmer, R., Maki, R., Truong, V., Tamayo, P., Oliner, J., & Haber, D. A. (2001) · European Journal of Cell Biology · doi:10.1078/0171-9335-00162 · Cited by 35 · cited 1×
“They have been found within or close to almost 40% of all promoters of mammalian genes (Deaton and Bird, 2011; Fatemi et al., 2005).”
BackgroundGolebski, K., Luiten, S., van Egmond, D., Groot, E. J. J. D., Röschmann, K., Fokkens, W. J., & van Drunen, C. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087768 · Cited by 34
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“The TCF component is a receptor of this signal, being a direct MAPK phosphorylation target (Selvaraj et al., 2015; Shaw and Saxton, 2003; Yang and Sharrocks, 2006).”
BackgroundPreparing the First Responders: Building the Inflammatory Transcriptome from the Ground Up
Rogatsky, I., & Adelman, K. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.038 · Cited by 33
Invasion is a genetic program regulated by transcription factors.
Ozanne, B., Spence, H., Mcgarry, L., & Hennigan, R. (2006) · Current Opinion in Genetics and Development · doi:10.1016/j.gde.2005.12.012 · Cited by 33 · cited 1×
“This transcription factor plays an important role during both normal development and disease states such as cancer (Ozanne et al., 2006).”
BackgroundTranscriptional activity of megakaryoblastic leukemia 1 (MKL1) is repressed by SUMO modification
Nakagawa, K., & Kuzumaki, N. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00880.x · Cited by 31
Rye, M. B., Sandve, G. K., Daub, C. O., Kawaji, H., Carninci, P., Forrest, A. R. R., & Drabløs, F. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-120 · Cited by 31
Self-citationLessons on transcriptional control from the serum response network
Galbraith, M. D., & Espinosa, J. M. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.01.011 · Cited by 28
Mylona, A., Nicolas, R., Maurice, D., Sargent, M., Tuil, D., Daegelen, D., Treisman, R., & Costello, P. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01058-10 · Cited by 27 · cited 1×
“Phosphorylation of MKL1 inhibits its activity, while SUMO-modification of MKL1 and myocardin has the opposite effect (Nakagawa and Kuzumaki, 2005; Wang et al., 2007).”
BackgroundRole of human transcription elongation factor DSIF in the suppression of senescence and apoptosis
Komori, T., Inukai, N., Yamada, T., Yamaguchi, Y., & Handa, H. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01273.x · Cited by 27
Flouriot, G., Huet, G., Demay, F., Pakdel, F., Boujrad, N., & Michel, D. (2014) · Biochemical Journal · doi:10.1042/bj20131240 · Cited by 25 · cited 1×
“They will also initiate changes in post-translational modifications of histones, leading to changes in the chromatin structure (Ciccarelli and Giustetto, 2014; Flouriot et al., 2014; Sawicka et al., 2014).”
BackgroundFujita, T., Piuz, I., & Schlegel, W. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.10.032 · Cited by 25
Tatebe, K., Zeytun, A., Ribeiro, R. M., Hoffmann, R., Harrod, K. S., & Forst, C. V. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-170 · Cited by 21 · cited 1×
“Chromatin remodeling allows proteins of the regulatory transcription machinery access to condensed genomic DNA, and thereby control of gene expression (Teif and Rippe, 2009).”
BackgroundBertelsen, T., Iversen, L., Riis, J. L., Arthur, J. S., Bibby, B., Kragballe, K., & Johansen, C. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2010.01153.x · Cited by 21 · cited 1×
“Also RNA polymerase II is accumulated and “poised” at the proximal promoter region of IEGs (Byun et al., 2009; Tullai et al., 2007).”
BackgroundMostocotto, C., Carbone, M., Battistelli, C., Ciotti, A., Amati, P., & Maione, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102575 · Cited by 13 · cited 2×
“Depending on the kind of cell type and the duration of signaling, the biological outcome may be different (Murphy and Blenis, 2006).”
BackgroundKhan, D. H., & Davie, J. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.03.029 · Cited by 10
A property-based analysis of human transcription factors
Bahrami, S., Ehsani, R., & Drabløs, F. (2015) · BMC Research Notes · doi:10.1186/s13104-015-1039-6 · Cited by 10
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Metadata
- Authors
- Bahrami, S., & Drabløs, F.
- Affiliations
- Norwegian University of Science and Technology (NO)
- Corresponding author
- Drabløs, Finn
- Venue
- Advances in Biological Regulation
- Publisher
- Elsevier BV
- Published
- 2016-09
- Volume
- 62
- Pages
- 37-49
- ISSN
- 2212-4926 (ISSN-L)
- OpenAlex
- W2349918789
- Cited by
- 465
- References
- 109
- Citations by year
- 2026: 49 · 2025: 50 · 2024: 40 · 2023: 50 · 2022: 65 · 2021: 64 · 2020: 42 · 2019: 44 · 2018: 36 · 2017: 20 · 2016: 5
- FWCI
- 3.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Advances in Biological Regulation (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Helse Midt-Norge
- Norges Teknisk-Naturvitenskapelige Universitet
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gene Regulatory Network Analysis
- Keywords
- immediate early genes, gene expression regulation, transcription factor activation, MAPK signaling, ERK, signal transduction, enhancers, promoter regulation, stress response, immune response, cell differentiation, cancer
- MeSH terms
- Actins, Animals, Cell Differentiation, Cell Nucleus, Eukaryotic Cells, Gene Expression Regulation, Humans, Phosphorylation, Promoter Regions, Genetic, Transcription Factors, Signal Transduction, Genes, Immediate-Early, rhoA GTP-Binding Protein, Mitogen-Activated Protein Kinases, Extracellular Signal-Regulated MAP Kinases
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