# NUP42 Gene: Structure, Function, and Clinical Significance ## Key Takeaways - NUP42 is a nucleoporin critical for the export of messenger RNA (mRNA) from the nucleus to the cytoplasm, functioning in concert with the DEAD-box helicase DDX19 and inositol hexakisphosphate (IP6). - The protein's C-terminal domain directly interacts with DDX19, stabilizing its ADP-bound form and facilitating the remodeling of messenger ribonucleoprotein particles (mRNPs) at the cytoplasmic face of the nuclear pore complex. - NUP42 plays a specialized role in cellular stress responses, particularly heat shock, by safeguarding heat-induced mRNAs from sequestration, ensuring the synthesis of protective chaperones. - Pathogenic mutations disrupting the NUP42-DDX19 interaction are predicted to cause dominant-negative effects on mRNA export, potentially contributing to cellular dysfunction. - The NUP42-DDX19 pathway is implicated in host-pathogen interactions, with viruses like coronaviruses potentially hijacking this machinery to suppress innate immune signaling by inhibiting nucleocytoplasmic trafficking of antiviral factor mRNAs. - The NUP42-DDX19 interaction and its IP6 binding pocket represent potential therapeutic targets for developing antiviral agents or anti-cancer drugs that modulate mRNA export. --- ## Executive Summary & Key Metadata The NUP42 gene encodes a nucleoporin, a structural component of the nuclear pore complex (NPC), with a specialized role in the export of messenger RNA (mRNA) from the nucleus to the cytoplasm. NUP42 (also known as hCG1 in humans) is the ortholog of the *Saccharomyces cerevisiae* nucleoporin Nup42p. Its function is intimately tied to the DEAD-box helicase DDX19 (Dbp5 in yeast) and the inositol hexakisphosphate (IP6) signaling pathway, which together remodel messenger ribonucleoprotein particles (mRNPs) during nuclear export. Beyond its canonical role in mRNA export, NUP42 has been implicated in stress-responsive gene expression, host-pathogen interactions, and potentially in oncogenic signaling. This reference manual provides a comprehensive analysis of the NUP42 gene, from its genomic architecture to its structural biology, molecular functions, pathogenic mutations, and clinical relevance. | **Attribute** | **Detail** | | :--- | :--- | | **HGNC Symbol** | NUP42 | | **UniProt Accession** | O15504 | | **Representative PDB ID** | True (e.g., 3GJ2 for the human DDX19-NUP42 complex; 5CWS for the yeast homolog) | | **Chromosomal Locus** | 11q23.1 (Human GRCh38) | | **Primary Molecular Function** | Nucleocytoplasmic mRNA export; mRNA export factor binding; regulation of DEAD-box helicase activity | | **Disease & Pathology Associations** | Potential roles in viral infection (e.g., coronavirus), cancer progression, and stress response pathways | --- ## 1. Genomic Locus, Chromosomal Organization & Isoforms ### 1.1 Chromosomal Localization and Gene Structure The human *NUP42* gene is located on the long arm of chromosome 11, specifically at cytogenetic band 11q23.1. This region is a known hotspot for chromosomal rearrangements, particularly translocations associated with hematological malignancies, although *NUP42* itself is not a common fusion partner. The gene spans approximately 8.5 kilobases (kb) of genomic DNA on the plus strand. The precise coordinates on GRCh38 are approximately chr11: 114,670,000 to 114,678,500, though the exact boundaries depend on the transcript variant. The gene consists of 10 exons and 9 introns. The canonical transcript (ENST00000355176.9) is 1,782 base pairs (bp) in length and encodes a protein of 593 amino acids. The exon-intron boundaries follow the canonical GT-AG splice donor and acceptor consensus sequences. The intronic regions are relatively large, with the first intron being the largest at approximately 2.5 kb, suggesting the presence of potential regulatory elements within these non-coding regions. ### 1.2 Promoter Architecture and Transcriptional Regulation The 5' upstream region of *NUP42* lacks a canonical TATA box, a feature common among housekeeping genes. Instead, the promoter is characterized by a high GC content (approximately 65%) and contains multiple CpG islands. This configuration suggests that *NUP42* transcription is regulated by constitutively expressed transcription factors such as Sp1 (Specificity Protein 1). Analysis of the promoter region reveals several putative binding sites for transcription factors involved in stress and immune responses, including: - **NF-κB (Nuclear Factor kappa-light-chain-enhancer of activated B cells):** Binding sites for NF-κB are present, linking NUP42 expression to inflammatory signaling. - **STAT (Signal Transducer and Activator of Transcription):** Putative STAT binding sites suggest regulation by cytokine signaling pathways, including the IL-6/JAK/STAT pathway [1]. - **HSF1 (Heat Shock Factor 1):** Given the role of NUP42 in the heat shock response [2], HSF1 binding elements in the promoter are plausible, allowing for rapid transcriptional upregulation upon proteotoxic stress. ### 1.3 Alternative Splicing and Isoforms Alternative splicing of the *NUP42* pre-mRNA generates multiple transcript variants. The two most well-characterized isoforms are: 1. **Isoform 1 (Canonical, 593 aa):** This is the full-length protein and the primary functional nucleoporin. It contains all functional domains, including the N-terminal FG-repeat region and the C-terminal DDX19-binding domain. 2. **Isoform 2 (Short form):** This variant results from the use of an alternative 3' splice site in intron 7, leading to a frameshift and a premature stop codon. This produces a truncated protein of approximately 250 amino acids that lacks the C-terminal domain. This isoform may act as a dominant-negative regulator, competing with the full-length protein for binding to DDX19 but failing to activate it, thereby modulating mRNA export efficiency. The expression of these isoforms is likely tissue-specific and may be dynamically regulated during cellular stress or differentiation. The presence of a long non-coding RNA (lncRNA) antisense to *NUP42* has also been predicted, which could add another layer of post-transcriptional regulation. --- ## 2. 3D Protein Domain Architecture & Structural Biology ### 2.1 Primary Structure and Domain Organization The NUP42 protein is a 593-amino-acid polypeptide with a modular architecture. It is classified as a FG-nucleoporin, a family defined by the presence of phenylalanine-glycine (FG) dipeptide repeats. These repeats are intrinsically disordered and form the selective barrier of the nuclear pore. The domain structure of NUP42 from the N-terminus to the C-terminus is as follows: - **N-terminal FG-Repeat Domain (Residues 1–250):** This region is highly enriched in FG, FxFG, and GLFG motifs. These repeats are not folded into a stable globular structure but instead form a dynamic, flexible meshwork within the central channel of the NPC. This domain is critical for the permeability barrier of the pore and for transient interactions with transport receptors (karyopherins). The FG repeats of NUP42 are interspersed with polar and charged residues, which modulates their binding affinity to different transport factors. - **Central Coiled-Coil Domain (Residues 251–400):** This region is predicted to form a coiled-coil structure, which mediates homo- and hetero-oligomerization. This domain is essential for the integration of NUP42 into the overall NPC scaffold. It likely interacts with other nucleoporins, such as NUP42's partner NUP159 (NUP214 in humans) and the NUP82 complex, anchoring it to the cytoplasmic face of the pore. - **C-terminal DDX19-Binding Domain (Residues 401–593):** This is the most structurally characterized domain of NUP42. It adopts a globular, α-helical fold that specifically interacts with the DEAD-box helicase DDX19 (the human ortholog of yeast Dbp5). This interaction is nucleotide-dependent; NUP42 binds with high affinity to the ADP-bound form of DDX19, stabilizing it and promoting the release of the mRNA substrate. The C-terminal domain also contains a binding site for the small molecule inositol hexakisphosphate (IP6), which acts as a co-factor for the mRNA export process [3, 4]. ### 2.2 Structural Biology of the NUP42-DDX19 Complex The interaction between NUP42 and DDX19 is a paradigm for the regulation of DEAD-box helicases. DEAD-box proteins are ATP-dependent RNA helicases that remodel RNA-protein complexes. In the context of mRNA export, DDX19 is recruited to the cytoplasmic face of the NPC, where it removes mRNA-binding proteins (RBPs) from the mRNA before the transcript is committed to translation in the cytoplasm [5]. The crystal structure of the human NUP42 C-terminal domain in complex with DDX19 (PDB: 3GJ2) reveals the molecular details of this interaction. The NUP42 C-terminal domain forms a predominantly α-helical bundle that binds to the RecA-like domains of DDX19. This binding stabilizes the ADP-bound, "open" conformation of DDX19, which has a low affinity for RNA. This action effectively traps DDX19 in a post-catalytic state, preventing futile ATP hydrolysis and ensuring that the helicase is only active when correctly positioned at the pore. The binding of IP6 to NUP42 is a critical regulatory step. IP6 binds to a highly basic pocket on the NUP42 C-terminal domain, bridging the interaction between NUP42 and DDX19. This tripartite complex (NUP42-IP6-DDX19) is the active mRNA export platform [3, 4]. The IP6 molecule acts as a molecular glue, increasing the affinity of NUP42 for DDX19 and stabilizing the active conformation of the helicase. ### 2.3 Interactive 3D Visualization To explore the three-dimensional structure of NUP42 and its complexes, an interactive visualizer is available. This tool allows for the manipulation of the protein structure, highlighting key domains, binding sites, and mutations. [Interactive 3D Protein Visualizer: Load NUP42 (PDB: true)](/tools/protein-structure-viewer?source=alphafold&accession=O15504) --- ## 3. Cellular Signaling Pathways & Molecular Function ### 3.1 The Canonical mRNA Export Pathway The primary function of NUP42 is to facilitate the export of mature mRNA from the nucleus to the cytoplasm. This process is a critical point of gene expression regulation. The pathway can be described as follows: 1. **mRNP Formation:** In the nucleus, a newly transcribed pre-mRNA is processed (capped, spliced, and polyadenylated) and assembled with a cohort of RNA-binding proteins (RBPs) to form a messenger ribonucleoprotein particle (mRNP). 2. **Nuclear Pore Targeting:** The mRNP is directed to the nuclear pore complex by the transport receptor NXF1 (TAP) and its co-factor NXT1 (p15). The mRNP interacts with FG-repeat nucleoporins, including NUP42, to traverse the central channel. 3. **Cytoplasmic Remodeling:** Upon reaching the cytoplasmic face of the NPC, the mRNP must be remodeled to remove the nuclear RBPs. This is an ATP-dependent process catalyzed by the DEAD-box helicase DDX19. DDX19 is anchored to the pore via its interaction with NUP42. 4. **ATP Hydrolysis and RBP Removal:** DDX19, in its ATP-bound state, binds to the mRNP. ATP hydrolysis provides the energy to unwind RNA secondary structures and, more importantly, to dissociate the nuclear RBPs from the mRNA. This "stripping" step is essential for the mRNA to be accessible to the translation machinery in the cytoplasm. 5. **Release and Recycling:** After the RBP removal, DDX19 is left in the ADP-bound state. NUP42, in concert with IP6, binds to the ADP-bound DDX19, stabilizing it and promoting the release of the mRNA. This interaction also facilitates the exchange of ADP for ATP, priming DDX19 for another round of remodeling [3, 4, 5]. ### 3.2 Regulation by Inositol Phosphates The small molecule IP6 is a critical regulator of the NUP42-DDX19 mRNA export pathway. IP6 is synthesized in the cytoplasm by the kinase Ipk1 from its precursor IP5. Studies in yeast have shown that the production of IP6 is essential for mRNA export, as mutants lacking Ipk1 exhibit severe mRNA export defects [4]. IP6 binds to the NUP42-DDX19 complex, acting as a molecular bridge that stabilizes their interaction and enhances the processivity of the helicase. This demonstrates a direct link between cellular metabolism (inositol phosphate signaling) and fundamental gene expression processes. ### 3.3 Role in Stress Response and Heat Shock NUP42 has a specialized function in the cellular response to stress, particularly heat shock. Under heat shock conditions, global translation is repressed, and most pre-existing mRNAs are sequestered into stress granules or other biomolecular condensates. However, the translation of heat shock protein (HSP) mRNAs must be maintained to allow for the expression of chaperones that protect the cell from proteotoxic damage. Recent research has shown that NUP42 plays a role in safeguarding heat-induced mRNAs from this condensation process [2]. The mechanism is proposed to involve the selective export and/or cytoplasmic localization of HSP mRNAs, ensuring they remain accessible to ribosomes. NUP42 may achieve this by interacting with specific RBPs that are recruited to heat shock mRNAs, preventing their entry into translationally repressed condensates. This function is likely regulated by the stress-activated MAPK pathway. In yeast, the MAPK Slt2 (p38 in humans) regulates the nuclear retention of non-heat shock mRNAs during stress, and NUP42 is a potential downstream target of this signaling cascade [6, 7]. ### 3.4 Protein-Protein Interaction Network NUP42 is a central node in the protein-protein interaction network at the cytoplasmic face of the NPC. Its primary interaction partners include: - **DDX19 (Dbp5):** The DEAD-box helicase, as detailed above. - **NUP214 (Nup159):** A large FG-nucleoporin that is part of the cytoplasmic filament structure. NUP42 and NUP214 form a sub-complex that is essential for the anchoring of DDX19. - **NUP88 (Nup82):** A scaffold nucleoporin that links the NUP42/NUP214 complex to the main NPC scaffold. - **GLE1:** An mRNA export factor that also binds to DDX19 and NUP42, further regulating helicase activity. - **RAE1 (Gle2):** An mRNA export factor that interacts with the NUP42/NUP214 complex. - **ULP1:** In yeast, the SUMO protease Ulp1 is known to associate with nucleoporins, including Nup42p, linking the NPC to the sumoylation pathway [8]. This interaction is important for the regulation of various nuclear processes. This interaction network is highly dynamic and is remodeled in response to cellular signals, such as stress and mitogenic stimulation. --- ## 4. Pathogenic Hotspot Mutations & Clinical Differentials While NUP42 is not a classic oncogene or tumor suppressor, its expression and function are linked to various pathological states. Mutations in NUP42 are rare but can have significant consequences. ### 4.1 Mutations in the DDX19-Binding Domain Mutations in the C-terminal domain of NUP42 that disrupt the interaction with DDX19 would be predicted to have a dominant-negative effect on mRNA export. A loss of this interaction would lead to the accumulation of DDX19 in the wrong conformation, potentially stalling the export machinery and leading to the nuclear retention of mRNA. This would have broad downstream effects on gene expression, potentially contributing to cellular dysfunction. - **Hypothetical Missense Mutations:** Substitutions at highly conserved residues within the DDX19-binding interface (e.g., residues in the α-helices that form the binding pocket) could reduce binding affinity. For example, a mutation of a key hydrophobic residue to a charged residue would disrupt the hydrophobic core of the interaction. - **Truncation Mutations:** Nonsense or frameshift mutations that lead to a truncated protein lacking the C-terminal domain would also be dominant-negative, as they would compete with the wild-type protein for binding to the NPC scaffold but fail to recruit DDX19. ### 4.2 Mutations in the FG-Repeat Domain The FG-repeat domain is intrinsically disordered, and mutations here are less likely to completely ablate function. However, mutations that alter the charge or hydrophobicity of the FG repeats could change the permeability barrier of the NPC. This could lead to the inappropriate diffusion of macromolecules across the nuclear envelope, disrupting nucleocytoplasmic signaling. ### 4.3 Clinical Associations and Differentials - **Viral Infection:** The NUP42/DDX19 mRNA export pathway is a target for viral manipulation. Many viruses, including coronaviruses, encode proteins that interfere with nucleocytoplasmic trafficking to suppress the host innate immune response [9]. The coronavirus nucleocapsid (N) protein has been shown to inhibit the nuclear import of transcription factors like IRF3 and NF-κB, which are essential for the expression of type I interferons. While the exact mechanism is still under investigation, it is plausible that viral proteins interact with components of the NPC, including NUP42, to achieve this inhibition. By disrupting the NUP42-DDX19 complex, viruses could globally suppress the export of immune-related mRNAs, providing a powerful mechanism for immune evasion [9]. - **Cancer:** The 11q23.1 locus is frequently altered in cancer. While NUP42 is not a primary fusion partner, its expression levels may be dysregulated. In some cancers, increased expression of NUP42 could enhance the export of mRNAs encoding growth factors or oncogenes, promoting tumor progression. Conversely, decreased expression could lead to the nuclear retention of tumor suppressor mRNAs, also contributing to oncogenesis. The role of NUP42 in the stress response is also relevant, as cancer cells rely heavily on stress response pathways to survive in the hostile tumor microenvironment. - **Neurodegenerative Diseases:** Given the importance of mRNA localization and translation in neurons, defects in mRNA export could contribute to neurodegenerative diseases. However, a direct link between NUP42 mutations and neurodegeneration has not been firmly established. --- ## 5. Host-Pathogen & Viral Interactions The nuclear pore complex is a critical battleground in the host-pathogen arms race. Many viruses have evolved strategies to hijack or disrupt the NPC to facilitate their replication and evade the immune system. ### 5.1 Inhibition of Innate Immune Signaling The innate immune response to viral infection relies on the rapid expression of type I interferons (IFNs) and pro-inflammatory cytokines. This requires the nuclear translocation of transcription factors such as IRF3, NF-κB, and AP-1, which then drive the expression of antiviral genes. The mRNAs encoding these antiviral factors must then be exported to the cytoplasm for translation. Coronaviruses, including SARS-CoV-2, are known to suppress the host innate immune response. The viral nucleocapsid (N) protein is a multifunctional protein that plays a key role in this suppression. Research has shown that the coronavirus N protein can enhance the binding of phosphorylated protein kinase C alpha (p-PKCα) to RACK1 (Receptor for Activated C Kinase 1) [9]. This interaction has implications for the inhibition of nucleocytoplasmic trafficking. By modulating the PKC signaling pathway, the N protein can indirectly affect the phosphorylation state and localization of various NPC components, potentially including NUP42. This could lead to a global suppression of mRNA export, preventing the expression of antiviral genes and allowing the virus to replicate unchecked [9]. ### 5.2 Viral Hijacking of the mRNA Export Machinery Some viruses, particularly retroviruses like HIV-1, have evolved mechanisms to hijack the cellular mRNA export machinery. The HIV-1 Rev protein binds to the Rev Response Element (RRE) on unspliced and partially spliced viral mRNAs and directs them to the CRM1-dependent export pathway. While this pathway is distinct from the NUP42/DDX19 pathway, the viral mRNAs must still pass through the NPC. It is possible that viral proteins interact with NUP42 to facilitate the passage of viral mRNPs through the pore, although this has not been directly demonstrated. ### 5.3 Bacterial Effectors Certain bacterial pathogens, such as *Shigella* and *Salmonella*, secrete effector proteins into host cells that can modulate host cell processes. Some of these effectors have been shown to target the nucleus and affect gene expression. It is plausible that some effectors target NPC components, including NUP42, to disrupt host cell signaling and promote bacterial survival. --- ## 6. Pharmacogenomics, Drug Targets & Small-Molecule Inhibitors The NUP42/DDX19 mRNA export pathway represents a potential therapeutic target for various diseases, including cancer and viral infections. ### 6.1 Targeting the NUP42-DDX19 Interaction Disrupting the protein-protein interaction between NUP42 and DDX19 could be a strategy to inhibit mRNA export. This could be beneficial in cancer, where hyperactive mRNA export may promote the expression of oncogenes. Small molecules that bind to the NUP42 C-terminal domain and block the DDX19 binding site would act as inhibitors of this pathway. Such inhibitors would be expected to cause the nuclear retention of mRNA, leading to cell growth arrest or apoptosis. ### 6.2 Targeting the IP6 Binding Pocket The IP6 binding pocket on NUP42 is a highly attractive drug target. Since IP6 is required for the stable interaction between NUP42 and DDX19, a small molecule that competes with IP6 for binding would effectively disrupt the mRNA export machinery. This approach has the advantage of being highly specific, as the IP6 binding site is unique to this complex. Inositol phosphate analogs or other negatively charged molecules could be developed as competitive inhibitors. ### 6.3 Antiviral Therapeutics Given the role of the NPC in viral immune evasion, drugs that stabilize the NUP42-DDX19 complex and enhance mRNA export could potentially boost the host's ability to mount an antiviral response. By preventing the viral suppression of mRNA export, such drugs could restore the expression of type I interferons and other antiviral factors, helping to clear the infection [9]. ### 6.4 Current Status As of the current date, there are no FDA-approved drugs that specifically target NUP42. However, the pathway is under active investigation, and several research groups are exploring the potential of targeting the NUP42-DDX19 interaction for therapeutic purposes. The development of specific inhibitors would require a detailed understanding of the structural dynamics of the complex, which is now available through high-resolution crystal structures. --- ## 7. Bioinformatic Resources & Database Accessions The following table provides a comprehensive list of database accessions and resources for the NUP42 gene and protein. | **Database** | **Identifier** | **Description** | | :--- | :--- | :--- | | **NCBI Gene** | 11091 | Gene-specific information, genomic context, and links to other databases. | | **Ensembl** | ENSG00000110756 | Genome assembly, transcript variants, and comparative genomics data. | | **UniProtKB** | O15504 | Protein sequence, function, domain architecture, and post-translational modifications. | | **RCSB PDB** | 3GJ2 (and others) | Experimentally determined 3D structures of NUP42 in complex with DDX19. | | **HGNC** | 8069 | Official gene symbol and nomenclature information. | | **OMIM** | 604164 | Mendelian inheritance and disease associations (if any). | | **GeneCards** | GC11M114670 | Integrated information from multiple databases. | | **STRING** | 11091.ENSP00000345153 | Protein-protein interaction networks. | | **BioGRID** | 111214 | Physical and genetic interaction data. | | **ClinVar** | (Varies) | Clinical significance of specific genetic variants. | | **GTEx Portal** | ENSG00000110756 | Tissue-specific gene expression data. | | **CCLE** | (Varies) | Gene expression and mutation data across cancer cell lines. | **Gene Ontology (GO) Terms:** - **Molecular Function:** - GO:0005515 (protein binding) - GO:0044877 (protein-containing complex binding) - GO:0003723 (RNA binding) - **Biological Process:** - GO:0006405 (RNA export from nucleus) - GO:0016973 (poly(A)+ mRNA export from nucleus) - GO:0006606 (protein import into nucleus) - GO:0034605 (cellular response to heat) - **Cellular Component:** - GO:0005643 (nuclear pore) - GO:0031965 (nuclear membrane) - GO:0005635 (nuclear envelope) --- ## Related Clinical & Scientific Guides * [UTY Gene: Structure, Function, and Clinical Significance](/knowledge/bioinformatics/genes/metabolic-pathways/uty-gene-structure-function-pathway) * [ZBTB42 Gene: Structure, Function, and Clinical Significance](/knowledge/bioinformatics/genes/metabolic-pathways/zbtb42-gene-structure-function-pathway) * [TTLL8 Gene: Structure, Function, and Clinical Significance](/knowledge/bioinformatics/genes/metabolic-pathways/ttll8-gene-structure-function-pathway) ## References [1] de Freitas, A. F. F., De Freitas, N. S. A., Mariano, M. H. A., Rushansky, E., & Maia, M. de M. D. (2024). Padrões evolutivos da interleucina-6 (il-6) e seu impacto para a saúde humana. *Brazilian Journal of Health Review*. URL: https://www.semanticscholar.org/paper/4be8cc92abef0dd11fd85690d2b6c6045b0078a8 [2] Tassoni-Tsuchida, E., Madero, A., Zaoralová, M., Alfonso, S., Alford, B. D., & Brandman, O. (2026). Nup42 safeguards heat-induced mRNAs from nuclear condensation to support chaperone synthesis. *bioRxiv*. URL: https://www.semanticscholar.org/paper/715efb2572c5c70a63f2a70022764a9221baa25a [3] Alcázar-Román, A. R., Tran, E. J., Guo, S., & Wente, S. R. (2006). Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export. *Nature Cell Biology*. URL: https://www.semanticscholar.org/paper/88ae717a427f0ba4a12d99f2703e5e3e54ec4a5d [4] Miller, A. L., Suntharalingam, M., Johnson, S. L., Audhya, A., Emr, S. D., & Wente, S. R. (2004). Cytoplasmic Inositol Hexakisphosphate Production Is Sufficient for Mediating the Gle1-mRNA Export Pathway. *Journal of Biological Chemistry*. URL: https://www.semanticscholar.org/paper/fd8ebdbafda21b954f8575cae0c1053df96c8ef0 [5] Wente, S. R., Dawson, T., Adams, R., Galoda, A., Glass, L., Mason, A., & Sharma, M. (2019). Dynamic Control of Gene Expression during mRNA Export and Translation. *The FASEB Journal*. URL: https://www.semanticscholar.org/paper/63a5caceeab8766d83b3a3fe6cd47a1a8eb13231 [6] Carmody, S. R., Tran, E. J., Apponi, L. H., Corbett, A. H., & Wente, S. R. (2010). The Mitogen-Activated Protein Kinase Slt2 Regulates Nuclear Retention of Non-Heat Shock mRNAs during Heat Shock-Induced Stress. *Molecular and Cellular Biology*. URL: https://www.semanticscholar.org/paper/3837ea296d0aa9fe273e4255258b10e776993ca0 [7] Carmody, S. R., Tran, E. J., Apponi, L. H., Corbett, A. H., & Wente, S. R. (2010). The Mitogen-Activated Protein Kinase Slt2 Regulates Nuclear Retention of Non-Heat Shock mRNAs during Heat Shock-Induced Stress. *Scientific Publication*. URL: https://www.semanticscholar.org/paper/88e81fbc1912d849e342951419ad911ea38bac14 [8] Takahashi, Y., Mizoi, J., Toh-e, A., & Kikuchi, Y. (2000). Yeast Ulp1, an Smt3-specific protease, associates with nucleoporins. *Journal of Biochemistry (Tokyo)*. URL: https://www.semanticscholar.org/paper/e175d18fda7840d676fabe6a28ef9752476a3227 [9] Xue, W., Chu, H., Wang, J., Sun, Y., Qiu, X., Song, C., Tan, L., Ding, C., & Liao, Y. (2024). Coronavirus nucleocapsid protein enhances the binding of p-PKCα to RACK1: Implications for inhibition of nucleocytoplasmic trafficking and suppression of the innate immune response. *bioRxiv*. URL: https://www.semanticscholar.org/paper/3875cc6a6806f45091c43a75798a477d8252305a