ArticleOncogene2003
The transformation suppressor protein Pdcd4 shuttles between nucleus and cytoplasm and binds RNA.
Article in Oncogene, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.
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Who cites it
60 citing papers in PubMed, 1 synthesis or guideline pooled it, 103 citations in OpenAlex.
- The clinical association of programmed cell death protein 4 (PDCD4) with solid tumors and its prognostic significance: a meta-analysis.Chinese journal of cancer · 2016Pooled it
- Functional characterisation of tumour suppressor PDCD4 reveals previously undisclosed role in the control of cell adhesion.Nucleic acids research · 2026Article
- The Impact of Pdcd4, a Translation Inhibitor, on Drug Resistance.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Human tumor suppressor protein Pdcd4 binds at the mRNA entry channel in the 40S small ribosomal subunit.Nature communications · 2024Article
- Human tumor suppressor PDCD4 directly interacts with ribosomes to repress translation.Cell research · 2024Article
- PDCD4 restricts PRRSV replication in an eIF4A-dependent manner and is antagonized by the viral nonstructural protein 9.Journal of virology · 2024Article
- The Role and Interactions of Programmed Cell Death 4 and its Regulation by microRNA in Transformed Cells of the Gastrointestinal Tract.Frontiers in oncology · 2022Review
- Neuronal activity regulates the nuclear proteome to promote activity-dependent transcription.The Journal of cell biology · 2021Article
- Localization and Functional Roles of Components of the Translation Apparatus in the Eukaryotic Cell Nucleus.Cells · 2021Review
- Clinical Significance of PDCD4 in Melanoma by Subcellular Expression and in Tumor-Associated Immune Cells.Cancers · 2021Article
- PDCD4 limits prooncogenic neuregulin-ErbB signaling.Cellular and molecular life sciences : CMLS · 2021Article
- PDCD4 controls the G1/S-phase transition in a telomerase-immortalized epithelial cell line and affects the expression level and translation of multiple mRNAs.Scientific reports · 2020Article
- Conjunctival melanoma copy number alterations and correlation with mutation status, tumor features, and clinical outcome.Pigment cell & melanoma research · 2019Article
- Control Mechanisms of the Tumor Suppressor PDCD4: Expression and Functions.International journal of molecular sciences · 2019Review
- The Regulatory Role of Non-coding RNAs on Programmed Cell Death Four in Inflammation and Cancer.Frontiers in oncology · 2019Review
- Interrelation of the Circulating and Tissue MicroRNA-21 with Tissue PDCD4 Expression and the Invasiveness of Iraqi Female Breast Tumors.Indian journal of clinical biochemistry : IJCB · 2019Article
- Cytoplasmic localization of programmed cell death 4 contributes to its anti-apoptotic function.Molecular and cellular biochemistry · 2018Article
- Expression of tumor suppressor programmed cell death 4 in endometrioid endometrial carcinomas and clinicopathological significance.Oncology letters · 2018Article
- The role of Pdcd4 in tumour suppression and protein translation.Biology of the cell · 2018Review
- Programmed cell death 4 mechanism of action: The model to be updated?Cell cycle (Georgetown, Tex.) · 2017Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Pdcd4 gene has originally been isolated in a search for genes that are activated in cells undergoing apoptosis. Independent of these studies, the Pdcd4 gene has been implicated in the suppression of tumor-promoter-mediated transformation of keratinocytes and as a downstream target of Myb in hematopoietic cells. The Pdcd4 protein has weak homology to the eucaryotic translation initiation factor eIF4G and has been shown to interact with certain translation initiation factors. To explore the molecular function of the Pdcd4 protein, we have studied its subcellular localization. We show that the Pdcd4 protein is a predominantly nuclear protein under normal growth conditions and that it is exported from the nucleus by a leptomycin B-sensitive mechanism upon serum withdrawal. The protein contains two nuclear export signals, one of which is very potent. In addition, we demonstrate that the Pdcd4 protein has RNA-binding activity and that the sequences involved in RNA-binding are located in the amino-terminal part of the protein. Taken together, our data raise the possibility that Pdcd4 is involved in some aspect of nuclear RNA metabolism in addition to its suspected role in protein translation.
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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.