ArticleThe Journal of cell biology2014
The p53-induced factor Ei24 inhibits nuclear import through an importin β-binding-like domain.
Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.
- Gene network profiling in muscle-invasive bladder cancer: A systematic review and meta-analysis.Urologic oncology · 2022Pooled it
- Biological significance, molecular mechanisms and clinical potential of EI24 in cancer.Chinese medical journal · 2026Review
- p53-Mediated Mitochondrial Translocation of EI24 Triggered by ER Stress Plays an Important Role in Arsenic-Induced Liver Damage via Activating Mitochondrial Apoptotic Pathway.Biological trace element research · 2024Article
- The Nuclear Transporter Importin 13 Can Regulate Stress-Induced Cell Death through the Clusterin/KU70 Axis.Cells · 2023Article
- Nuclear TransporterCells · 2022Article
- Nuclear transporter Importin-13 plays a key role in the oxidative stress transcriptional response.Nature communications · 2021Article
- Adenovirus Terminal Protein Contains a Bipartite Nuclear Localisation Signal Essential for Its Import into the Nucleus.International journal of molecular sciences · 2021Article
- The ataxin-1 interactome reveals direct connection with multiple disrupted nuclear transport pathways.Nature communications · 2020Article
- EI24 tethers endoplasmic reticulum and mitochondria to regulate autophagy flux.Cellular and molecular life sciences : CMLS · 2020Article
- EI24, as a Component of Autophagy, Is Involved in Pancreatic Cell Proliferation.Frontiers in oncology · 2019Article
- DNA damage triggers tubular endoplasmic reticulum extension to promote apoptosis by facilitating ER-mitochondria signaling.Cell research · 2018Article
- KPNB1 inhibition disrupts proteostasis and triggers unfolded protein response-mediated apoptosis in glioblastoma cells.Oncogene · 2018Article
- Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V.Scientific reports · 2018Article
- Functional Blockade of Small GTPase RAN Inhibits Glioblastoma Cell Viability.Frontiers in oncology · 2018Article
- Extensive cargo identification reveals distinct biological roles of the 12 importin pathways.eLife · 2017Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
The etoposide-induced protein Ei24 was initially identified as a p53-responsive, proapoptotic factor, but no clear function has been described. Here, we use a nonbiased proteomics approach to identify members of the importin (IMP) family of nuclear transporters as interactors of Ei24 and characterize an IMPβ-binding-like (IBBL) domain within Ei24. We show that Ei24 can bind specifically to IMPβ1 and IMPα2, but not other IMPs, and use a mutated IMPβ1 derivative to show that Ei24 binds to the same site on IMPβ1 as the IMPα IBB. Ectopic expression of Ei24 reduced the extent of IMPβ1- or IMPα/β1-dependent nuclear protein import specifically, whereas specific alanine substitutions within the IBBL abrogated this activity. Induction of endogenous Ei24 expression through etoposide treatment similarly inhibited nuclear import in a mouse embryonic fibroblast model. Thus, Ei24 can bind specifically to IMPβ1 and IMPα2 to impede their normal role in nuclear import, shedding new light on the cellular functions of Ei24 and its tumor suppressor role.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.