GO:1903912 negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation: Integrated Stress Response Brake, Genes, Functions and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:1903912 describes any process that stops, prevents, or reduces the phosphorylation of eIF2 alpha (eIF2alpha) specifically triggered by endoplasmic reticulum (ER) stress.
• Phosphorylation of eIF2alpha at Ser51 is a central switch that attenuates global cap-dependent translation while selectively increasing translation of stress-responsive mRNAs such as ATF4.
• Negative regulation of this phosphorylation is primarily mediated by the phosphatase complex containing GADD34 (PPP1R15A) and protein phosphatase 1 (PP1), which dephosphorylates eIF2alpha and restores protein synthesis.
• Feedback inhibition of the unfolded protein response (UPR) by GADD34-mediated dephosphorylation prevents excessive translational silencing and promotes recovery from ER stress.
• Dysregulation of eIF2alpha phosphorylation is implicated in cancer, neurodegeneration, metabolic disorders, and inflammatory signaling, making this process a therapeutic target.
• CRISPR-based models (knockout, point mutation, knock-in, overexpression) enable precise interrogation of genes controlling eIF2alpha phosphorylation in ER stress contexts.
Description
The endoplasmic reticulum (ER) is the primary site for folding and modification of secretory and membrane proteins. When the folding capacity of the ER is overwhelmed, a condition known as ER stress, cells activate the unfolded protein response (UPR) to restore homeostasis. A key effector of the UPR is the phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF2alpha) at serine 51, which reduces global protein synthesis while favoring translation of select stress-response mRNAs such as ATF4. This phosphorylation is catalyzed by ER-resident kinases including PERK. However, sustained eIF2alpha phosphorylation is detrimental, and cells have evolved mechanisms to negatively regulate this modification. GO:1903912, negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation, captures the biological processes that stop, prevent, or reduce ER stress-induced eIF2alpha phosphorylation. Research into GO:1903912 is critical because the balance between eIF2alpha phosphorylation and its dephosphorylation determines cell fate under ER stress. Excessive phosphorylation can lead to apoptosis, while insufficient phosphorylation impairs adaptive UPR signaling. The best-characterized negative regulator is the growth arrest and DNA damage-inducible protein GADD34 (PPP1R15A), which recruits protein phosphatase 1 (PP1) to dephosphorylate eIF2alpha, providing feedback inhibition of the UPR. Other phosphatases and regulatory proteins may also contribute. Understanding this process at molecular, cellular, and organismal levels has broad implications for cancer, neurodegeneration, and inflammatory diseases. This article integrates authoritative QuickGO annotation for GO:1903912 with verified PubMed literature to provide a research-grade overview of the genes, mechanisms, and experimental models used to study negative regulation of ER stress-induced eIF2alpha phosphorylation. It is intended for researchers designing CRISPR-based experiments to dissect this pathway.
negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation At A Glance
| GO ID | GO:1903912 |
|---|---|
| GO term | negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation |
| Ontology | biological_process |
| Synonym | inhibition of eiF2alpha phosphorylation in response to ER stress; down-regulation of eiF2alpha phosphorylation in response to endoplasmic reticulum stress; negative regulation of regulation of translation initiation by eiF2alpha phosphorylation in response to endoplasmic reticulum stress |
| Major function | Dephosphorylation or prevention of eIF2alpha phosphorylation to restore protein synthesis and promote recovery from ER stress |
| Key regulator | GADD34 (PPP1R15A) in complex with protein phosphatase 1 (PP1) |
| Substrate | eIF2alpha (EIF2S1) at serine 51 |
| Associated process | Unfolded protein response (UPR), integrated stress response (ISR), translational control |
| Disease relevance | Cancer, neurodegeneration, inflammatory signaling, metabolic disorders |
What Is GO:1903912?
GO:1903912 is a biological process term defined as any process that stops, prevents, or reduces the frequency, rate, or extent of endoplasmic reticulum stress-induced eIF2alpha phosphorylation. In other words, it encompasses molecular events that counteract the phosphorylation of eIF2alpha at serine 51 specifically when triggered by ER stress, thereby modulating the translational attenuation arm of the unfolded protein response.
Why Is negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation Important in Cell Biology?
GO:1903912 is important because it represents a critical brake on the ER stress-induced translational shutdown. Without negative regulation, sustained eIF2alpha phosphorylation can lead to persistent inhibition of protein synthesis, cell cycle arrest, and apoptosis. The GADD34-PP1 phosphatase complex provides feedback inhibition that is essential for restoring translation and allowing cells to recover from ER stress. Dysregulation of this process contributes to diseases such as cancer, where tumor cells may exploit eIF2alpha dephosphorylation to survive stress, and neurodegeneration, where impaired recovery from ER stress leads to neuronal death. Thus, understanding the mechanisms and genes involved in GO:1903912 is fundamental for developing therapeutic strategies targeting the UPR.
• Maintains translational homeostasis by preventing excessive eIF2alpha phosphorylation during ER stress.
• Enables feedback inhibition of the UPR, allowing cells to resume protein synthesis after stress resolution.
• Modulates cell fate decisions between adaptation and apoptosis under ER stress.
• Influences inflammatory cytokine responses in astrocytes via PERK/eIF2alpha/JAK1 signaling.
• Plays a role in cancer cell survival by promoting recovery from ER stress.
• Implicated in neurodegenerative diseases where chronic ER stress contributes to neuronal loss.
• Affects viral infection outcomes by modulating host translation machinery.
• Provides a target for pharmacological modulation of the integrated stress response.
• Essential for proper folding and secretion of proteins in professional secretory cells.
• Serves as a paradigm for studying reversible phosphorylation in translational control.
What Happens During negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation?
ER Stress Sensing and eIF2alpha Phosphorylation
In simple terms: When the ER gets stressed, a kinase called PERK adds a phosphate to eIF2alpha, which slows down protein production.
Under ER stress, the kinase PERK (EIF2AK3) autophosphorylates and phosphorylates eIF2alpha at serine 51. This phosphorylation inhibits the guanine nucleotide exchange factor eIF2B, reducing the delivery of initiator methionine-tRNA to the ribosome and thereby attenuating global cap-dependent translation. Paradoxically, this translational block selectively enhances translation of certain mRNAs, such as ATF4, which contain upstream open reading frames, allowing the cell to mount an adaptive response.
Recruitment of GADD34-PP1 Phosphatase Complex
In simple terms: A protein called GADD34 brings a phosphatase (PP1) to remove the phosphate from eIF2alpha.
The negative regulation of eIF2alpha phosphorylation is primarily executed by the growth arrest and DNA damage-inducible protein GADD34 (PPP1R15A). GADD34 is a regulatory subunit that binds to the catalytic subunit of protein phosphatase 1 (PP1) and targets it to dephosphorylate eIF2alpha at serine 51. GADD34 is itself a transcriptional target of ATF4, creating a negative feedback loop: ER stress induces eIF2alpha phosphorylation and ATF4 translation, which in turn induces GADD34, leading to eIF2alpha dephosphorylation and restoration of translation.
Dephosphorylation of eIF2alpha and Translation Recovery
In simple terms: Once the phosphate is removed, protein production can restart, helping the cell recover from stress.
The GADD34-PP1 complex dephosphorylates eIF2alpha, reversing the inhibition of eIF2B and allowing global protein synthesis to resume. This dephosphorylation is critical for terminating the UPR and preventing prolonged translational arrest that could trigger apoptosis. Studies using GADD34 knockout cells show that loss of GADD34 leads to sustained eIF2alpha phosphorylation and impaired recovery from ER stress.
Feedback Inhibition of the Unfolded Protein Response
In simple terms: The same process that removes the phosphate also acts as a brake on the stress response, preventing it from going on too long.
GADD34-mediated dephosphorylation serves as a feedback inhibitor of the UPR. By reducing eIF2alpha phosphorylation, it decreases ATF4 translation and downstream UPR gene expression, thereby limiting the duration and intensity of the stress response. This feedback is essential for maintaining cellular homeostasis and preventing the deleterious effects of chronic UPR activation. Other phosphatases, such as PP1 regulatory subunit PPP1R15B (CReP), may also contribute to eIF2alpha dephosphorylation in unstressed or specific contexts.
Integration with Other Stress Pathways
In simple terms: This process is not isolated; it talks to other stress signals like inflammation and UV damage.
Negative regulation of eIF2alpha phosphorylation intersects with other signaling pathways. For example, in astrocytes, ER stress amplifies cytokine responses via a PERK/eIF2alpha/JAK1 axis, and modulation of eIF2alpha phosphorylation can influence inflammatory output. Additionally, ultraviolet light activates NF-kappaB through translational inhibition of IkappaBalpha synthesis, a process that may involve eIF2alpha phosphorylation and its regulation. These crosstalks highlight the broader physiological significance of GO:1903912.
Key Genes Involved in GO:1903912 negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation
The following genes and proteins are central to the negative regulation of ER stress-induced eIF2alpha phosphorylation, based on verified literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| PPP1R15A (GADD34) | Regulatory subunit of PP1 that targets eIF2alpha for dephosphorylation | Primary negative regulator; knockout leads to sustained eIF2alpha phosphorylation and impaired stress recovery |
| PPP1CA (PP1 catalytic subunit) | Catalytic subunit of protein phosphatase 1; dephosphorylates eIF2alpha when recruited by GADD34 | Essential for phosphatase activity; target for mutagenesis studies |
| EIF2S1 (eIF2alpha) | Substrate; phosphorylation at Ser51 inhibits translation initiation | Key effector; point mutation at Ser51 (S51A) prevents phosphorylation and alters UPR |
| EIF2AK3 (PERK) | ER stress sensor kinase that phosphorylates eIF2alpha | Upstream kinase; knockout abolishes ER stress-induced eIF2alpha phosphorylation |
| ATF4 | Transcription factor selectively translated upon eIF2alpha phosphorylation; induces GADD34 | Links phosphorylation to feedback regulation; knockout affects GADD34 induction |
| PPP1R15B (CReP) | Constitutive PP1 regulatory subunit; may contribute to eIF2alpha dephosphorylation | Potential redundant phosphatase; less studied in ER stress |
| JAK1 | Kinase involved in cytokine signaling; interacts with PERK/eIF2alpha axis in astrocytes | Modulates inflammatory responses; relevant to neuroinflammation |
| NFKB1 (NF-kappaB) | Transcription factor activated by translational inhibition of IkappaBalpha | Connects eIF2alpha phosphorylation to UV response |
| IKBKB (IKKbeta) | Kinase that activates NF-kappaB; affected by IkappaBalpha synthesis | Downstream of translational control |
| DDIT3 (CHOP) | Pro-apoptotic transcription factor induced by ER stress; downstream of eIF2alpha phosphorylation | Marker of UPR; modulated by GADD34 activity |
| HSPA5 (BiP) | ER chaperone; master regulator of UPR; its dissociation activates PERK | Upstream sensor; overexpression or knockout alters ER stress |
| XBP1 | Transcription factor downstream of IRE1 arm of UPR; not directly eIF2alpha but crosstalk | Context for integrated UPR studies |
| ATF6 | Transcription factor arm of UPR; crosstalk with eIF2alpha pathway | Potential modifier of ER stress outcomes |
| EIF2B1-5 | Guanine nucleotide exchange factor; inhibited by phosphorylated eIF2alpha | Target for studying translation recovery |
| PPP1R10 (PNUTS) | PP1 regulatory subunit; may modulate phosphatase specificity | Potential alternative regulator; less characterized |
| UBXN1 | Adaptor protein involved in ER-associated degradation; may influence ER stress | Indirect role; context-dependent |
| SEL1L | ERAD component; affects ER stress and UPR activation | Indirect modulator of eIF2alpha phosphorylation |
| ERN1 (IRE1alpha) | ER stress sensor; its arm can crosstalk with eIF2alpha pathway | For integrated UPR studies |
How Is negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation Regulated?
The negative regulation of ER stress-induced eIF2alpha phosphorylation is itself tightly regulated. The primary mechanism is transcriptional induction of GADD34 (PPP1R15A) by ATF4, which is preferentially translated when eIF2alpha is phosphorylated. This creates a negative feedback loop: ER stress increases eIF2alpha phosphorylation, which enhances ATF4 translation, leading to GADD34 expression and subsequent dephosphorylation of eIF2alpha. Additionally, the constitutive PP1 regulatory subunit PPP1R15B (CReP) may provide baseline dephosphorylation in unstressed cells. Other signaling pathways, such as mTOR, can influence translation and indirectly affect the UPR, but their direct role in regulating eIF2alpha phosphorylation is context-dependent. Inflammatory signals via JAK1 may also modulate this axis in specific cell types.
negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| PPP1R15A (GADD34) | Cancer, neurodegeneration, metabolic stress | Knockout and overexpression in cancer cell lines; xenograft models |
| EIF2S1 (eIF2alpha) | Neurodegeneration, cancer, viral infection | Point mutation S51A knock-in mice; CRISPR-edited cell lines |
| EIF2AK3 (PERK) | Wolcott-Rallison syndrome, diabetes, neurodegeneration | Knockout mice and patient-derived iPSCs |
| ATF4 | Cancer, metabolic disorders, neurodegeneration | Knockout and reporter knock-in for translational studies |
| JAK1 | Neuroinflammation, cytokine signaling | Astrocyte-specific knockout; cytokine profiling |
Cancer
Tumor cells often face ER stress due to rapid growth and poor vascularization. Negative regulation of eIF2alpha phosphorylation, primarily via GADD34, allows cancer cells to recover from stress and continue protein synthesis, promoting survival and chemoresistance. Targeting this pathway could sensitize tumors to ER stress-induced apoptosis. Studies in astrocytes show that ER stress amplifies cytokine responses via PERK/eIF2alpha/JAK1, suggesting a link between this pathway and tumor microenvironment inflammation.
Neurodegeneration
Chronic ER stress and dysregulated eIF2alpha phosphorylation are hallmarks of neurodegenerative diseases such as Alzheimer's and Parkinson's. Impaired negative regulation can lead to sustained translational repression and neuronal death. Modulating GADD34 activity or eIF2alpha dephosphorylation is being explored as a therapeutic strategy to restore proteostasis in neurons.
Inflammatory and Immune Disorders
The PERK/eIF2alpha/JAK1 axis in astrocytes links ER stress to cytokine production, and negative regulation of eIF2alpha phosphorylation may dampen inflammatory responses. Dysregulation of this process could contribute to neuroinflammation and autoimmune conditions. Additionally, UV light activates NF-kappaB through translational inhibition of IkappaBalpha, a process that intersects with eIF2alpha phosphorylation.
Metabolic Disorders
ER stress in pancreatic beta cells and hepatocytes contributes to insulin resistance and diabetes. Proper negative regulation of eIF2alpha phosphorylation is necessary for beta cell survival and function. GADD34 knockout mice show impaired recovery from ER stress, which may exacerbate metabolic dysfunction.
From negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of GADD34 sustain eIF2alpha phosphorylation under ER stress? | PPP1R15A knockout cell lines (e.g., HeLa, MEFs) |
| Does preventing eIF2alpha phosphorylation alter UPR gene expression? | EIF2S1 S51A point-mutation knock-in cells |
| Can GADD34 overexpression restore translation after ER stress? | GADD34 overexpression constructs in ER-stressed cells |
| How does PERK kinase activity affect downstream signaling? | EIF2AK3 knockout or kinase-dead knock-in models |
| What is the role of JAK1 in ER stress-induced cytokine production? | JAK1 knockout astrocytes; cytokine arrays |
| Can tagged GADD34 be used to study its interactome? | Endogenous GADD34 knock-in with FLAG/HA tag |
How to Study the negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Phospho-eIF2alpha Western blot | Level of eIF2alpha phosphorylation at Ser51 | Assessing GADD34 or PERK activity |
| Polysome profiling | Global translation status | Measuring translational recovery after ER stress |
| Ribo-seq | Ribosome occupancy and translation efficiency | Identifying mRNAs selectively translated upon eIF2alpha dephosphorylation |
| UPRE-luciferase reporter | UPR transcriptional activity | High-throughput screening for regulators |
| Immunoprecipitation | Protein-protein interactions (e.g., GADD34-PP1) | Studying complex formation |
| CRISPR knockout screen | Genes required for eIF2alpha dephosphorylation | Discovery of novel regulators |
| qRT-PCR | mRNA levels of UPR targets (e.g., ATF4, CHOP) | Validating transcriptional changes |
| Immunofluorescence | Subcellular localization of eIF2alpha or GADD34 | Visualizing ER stress responses |
Phospho-eIF2alpha Immunoblotting
Western blotting with phospho-specific antibodies against eIF2alpha (Ser51) is the standard method to measure the phosphorylation status. Total eIF2alpha is used as a loading control. This method is widely used to assess the effects of GADD34 knockout or overexpression.
Polysome Profiling and Ribo-seq
Polysome profiling separates actively translated mRNAs from untranslated pools, providing a global view of translation. Ribo-seq (ribosome footprinting) offers codon-level resolution and can reveal changes in translation efficiency of specific mRNAs, such as ATF4, upon modulation of eIF2alpha phosphorylation.
Reporter Assays for UPR Activation
Luciferase reporters driven by UPR element (UPRE) or ATF4-responsive promoters can quantify UPR activity. These assays are useful for high-throughput screening of genes that negatively regulate eIF2alpha phosphorylation.
CRISPR Screens and Functional Genomics
Genome-wide CRISPR knockout or activation screens can identify novel regulators of eIF2alpha phosphorylation. Cells are challenged with ER stress inducers (e.g., tunicamycin, thapsigargin) and survival or reporter activity is measured to pinpoint genes that modulate this process.
How CRISPR Can Be Used to Study GO:1903912 negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation
Knockout
CRISPR knockout of PPP1R15A (GADD34) is used to study the consequences of losing negative regulation. GADD34 knockout cells exhibit sustained eIF2alpha phosphorylation and impaired recovery from ER stress, making them a valuable model for testing therapeutic interventions. Similarly, knockout of EIF2AK3 (PERK) abolishes ER stress-induced eIF2alpha phosphorylation, providing a baseline for studying negative regulators.
Point Mutation
Point mutation of eIF2alpha at Ser51 to alanine (S51A) prevents phosphorylation, effectively bypassing the need for negative regulation. This knock-in model is used to dissect the specific contribution of eIF2alpha phosphorylation to UPR signaling and cell fate. CRISPR-mediated point mutations can also be introduced into PPP1R15A to disrupt its PP1-binding motif, separating its phosphatase-recruiting function from other activities.
Knock-in
Knock-in of epitope tags (e.g., FLAG, HA) into endogenous PPP1R15A allows for affinity purification and interactome analysis of the GADD34-PP1 complex. Additionally, knock-in of luciferase or fluorescent reporters into UPR target genes (e.g., ATF4) enables real-time monitoring of pathway activity in live cells.
Overexpression
Overexpression of GADD34 or constitutively active PP1 can enhance eIF2alpha dephosphorylation, protecting cells from ER stress-induced apoptosis. Conversely, overexpression of a dominant-negative GADD34 mutant that cannot bind PP1 can block negative regulation, leading to sustained phosphorylation. These models are useful for gain-of-function studies.
How EDITGENE Supports negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation Research
Researchers studying negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation-related genes often need to determine whether a candidate gene is causally involved in modulating eIF2alpha phosphorylation, translation recovery, or UPR feedback. Precise genetic models are essential to establish causality and to dissect the molecular mechanisms. EDITGENE provides a comprehensive suite of CRISPR-based services to accelerate this research.
Contact EDITGENE today to design your custom CRISPR model for negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation research.
Frequently Asked Questions About negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation
What is GO:1903912?
GO:1903912 is a Gene Ontology biological process term defined as any process that stops, prevents, or reduces the frequency, rate, or extent of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation.
What genes are involved in negative regulation of ER stress-induced eIF2 alpha phosphorylation?
Key genes include PPP1R15A (GADD34), which recruits protein phosphatase 1 (PP1) to dephosphorylate eIF2alpha, and PPP1CA (PP1 catalytic subunit). Other modulators include PPP1R15B (CReP) and components of the PERK/eIF2alpha/JAK1 axis.
How does GADD34 regulate eIF2alpha phosphorylation?
GADD34 (PPP1R15A) binds to PP1 and targets it to eIF2alpha, removing the inhibitory phosphate at Ser51. This feedback mechanism restores translation and limits the unfolded protein response.
What happens if eIF2alpha phosphorylation is not negatively regulated?
Sustained eIF2alpha phosphorylation leads to prolonged translational arrest, impaired recovery from ER stress, and increased apoptosis. This is observed in GADD34 knockout cells.
Which diseases are associated with dysregulation of eIF2alpha phosphorylation?
Dysregulation is linked to cancer, neurodegeneration, inflammatory disorders, and metabolic diseases such as diabetes.
What experimental models are used to study GO:1903912?
Common models include GADD34 knockout cell lines, eIF2alpha S51A knock-in cells, PERK knockout models, and CRISPR screens with ER stress inducers.
How can CRISPR be used to study negative regulation of eIF2alpha phosphorylation?
CRISPR can generate knockouts of PPP1R15A or EIF2AK3, point mutations in EIF2S1 (S51A), tagged knock-ins for interaction studies, and overexpression models to modulate pathway activity.
What is the role of PERK in eIF2alpha phosphorylation?
PERK (EIF2AK3) is an ER stress sensor kinase that phosphorylates eIF2alpha at Ser51, initiating translational attenuation. Negative regulation counteracts this phosphorylation.
Is eIF2alpha phosphorylation reversible?
Yes, it is reversible. GADD34-PP1 complex dephosphorylates eIF2alpha, allowing translation to resume after stress resolution.
How does ER stress-induced eIF2alpha phosphorylation affect inflammation?
In astrocytes, ER stress amplifies cytokine responses via a PERK/eIF2alpha/JAK1 signaling axis, and negative regulation may dampen this inflammatory output.
Conclusion
GO:1903912, negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation, is a critical biological process that ensures translational recovery and feedback inhibition of the unfolded protein response. The GADD34-PP1 phosphatase complex is the primary mediator, dephosphorylating eIF2alpha to restore protein synthesis and promote cell survival. Dysregulation of this process contributes to cancer, neurodegeneration, and inflammatory diseases, making it an attractive therapeutic target. CRISPR-based models, including knockouts, point mutations, knock-ins, and overexpression, are indispensable for dissecting the molecular players and for identifying novel regulators through library screening. EDITGENE offers comprehensive services to support such research, from custom cell line generation to bioinformatics analysis.
References
- 1. Harding HP et al.. 2000. Regulated translation initiation controls stress-induced gene expression in mammalian cells.. Mol Cell 6(5):1099-108 PMID: 11106749
- 2. Lahiri A et al.. 2025. Endoplasmic Reticulum Stress Amplifies Cytokine Responses in Astrocytes via a PERK/eIF2α/JAK1 Signaling Axis.. Glia 73(11):2273-2288 PMID: 40685560
- 3. Novoa I et al.. 2001. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha.. J Cell Biol 153(5):1011-22 PMID: 11381086
- 4. Wu S et al.. 2004. Ultraviolet light activates NFkappaB through translational inhibition of IkappaBalpha synthesis.. J Biol Chem 279(33):34898-902 PMID: 15184376
