ArticleCell cycle (Georgetown, Tex.)2013
PDIP38 is translocated to the spliceosomes/nuclear speckles in response to UV-induced DNA damage and is required for UV-induced alternative splicing of MDM2.
Article in Cell cycle (Georgetown, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Genome-wide CRISPR screen for human factors involved in alternative polyadenylation based on differential localization of CD47.Scientific reports · 2025Article
- ZNF32 histidine 179 and 183 single-site and double-site mutations promote nuclear speckle formation but differentially regulate the proliferation of breast cancer cells.Frontiers in cell and developmental biology · 2025Article
- Mammalian nuclear speckles exhibit stable association with chromatin: a biochemical study.Nucleus (Austin, Tex.) · 2022Article
- ZEB1 regulates bone metabolism in osteoporotic rats through inducing POLDIP2 transcription.Journal of orthopaedic surgery and research · 2022Article
- PrimPol: A Breakthrough among DNA Replication Enzymes and a Potential New Target for Cancer Therapy.Biomolecules · 2022Review
- Poldip2/Nox4 Mediates Lipopolysaccharide-Induced Oxidative Stress and Inflammation in Human Lung Epithelial Cells.Mediators of inflammation · 2022Article
- The polymerase δ-interacting protein family and their emerging roles in diseases.Frontiers in medicine · 2022Review
- Article
- Polymerase delta-interacting protein 38 (PDIP38) modulates the stability and activity of the mitochondrial AAA+ protease CLPXP.Communications biology · 2020Article
- Alternative Splicing and DNA Damage Response in Plants.Frontiers in plant science · 2020Review
- Light-induced injury in mouse embryos revealed by single-cell RNA sequencing.Biological research · 2019Article
- Maintenance of genome stability: the unifying role of interconnections between the DNA damage response and RNA-processing pathways.Current genetics · 2018Review
- Phosphorylation Alters the Properties of Pol η: Implications for Translesion Synthesis.iScience · 2018Article
- Review
- Polymerase δ-interacting Protein 2: A Multifunctional Protein.Journal of cardiovascular pharmacology · 2017Review
- PolDIP2 interacts with human PrimPol and enhances its DNA polymerase activities.Nucleic acids research · 2016Article
- The Involvement of Splicing Factor hnRNP A1 in UVB-induced Alternative Splicing of hdm2.Photochemistry and photobiology · 2016Article
- Luminal flow induces NADPH oxidase 4 translocation to the nuclei of thick ascending limbs.Physiological reports · 2016Article
- The RNA Splicing Response to DNA Damage.Biomolecules · 2015Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
PDIP38 (polymerase delta interacting protein 38) was originally discovered as a protein that interacts with DNA polymerase δ and PCNA. PDIP38 is present in multiple intracellular locations and is a multifunctional protein that has been implicated in several diverse cellular functions. We investigated the nuclear localization of PDIP38 in order to gain insights to its response to UV damage. PDIP38 was found to form distinct nuclear foci in response to UV irradiation in several cell lines, including HeLa S3 and A549 cells. However, these foci were not those associated with UV repair foci. Using various markers for different nuclear subcompartments, the UV-induced PDIP38 foci were identified as spliceosomes/nuclear speckles, the storage and assembly sites for mRNA splicing factors. To assess the role of PDIP38 in the regulation of splicing events, the effects of PDIP38 depletion on the UV-induced alternate splicing of MDM2 transcripts were examined by nested RT-PCR. Alternatively spliced MDM2 products were induced by UV treatment but were greatly reduced in cells expressing shRNA targeting PDIP38. These findings indicate that upon UV-induced DNA damage, PDIP38 is translocated to spliceosomes and contributes to the UV-induced alternative splicing of MDM2 transcripts. Similar results were obtained when cells were subjected to transcriptional stresses with actinomycin D or α-amanitin. Taken together, these studies show that PDIP38 is a protein regulated in a dynamic manner in response to genotoxic stress, as evidenced by its translocation to the spliceosomes. Moreover, PDIP38 is required for the induction of the alternative splicing of MDM2 in response to UV irradiation.
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