ArticleProceedings of the National Academy of Sciences of the United States of America2006
The protein ENH is a cytoplasmic sequestration factor for Id2 in normal and tumor cells from the nervous system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 78 citations in OpenAlex.
- DPSCs-Exos promote OPCs differentiation and white matter repair via Myl9-mediated PRMT5 nucleation after ischemic stroke.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2026Article
- Scaffolding Protein ENH Promotes Tumor Angiogenesis and Growth Through Macrophage Recruitment and Polarization.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A Novel Effect of Id2 in Microglia TNFα Regulation.Molecular neurobiology · 2025Article
- Activation of feedforward wiring in adult hippocampal neurons by the basic-helix-loop-helix transcription factor Ascl4.PNAS nexus · 2024Article
- Article
- Role of a Pdlim5:PalmD complex in directing dendrite morphology.Frontiers in cellular neuroscience · 2024Article
- Review
- The unexpected versatility of ALP/Enigma family proteins.Frontiers in cell and developmental biology · 2022Review
- Recurrent rewiring of the adult hippocampal mossy fiber system by a single transcriptional regulator, Id2.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mechanical Sensing Element PDLIM5 Promotes Osteogenesis of Human Fibroblasts by Affecting the Activity of Microfilaments.Biomolecules · 2021Article
- Novel phospho-switch function of delta-catenin in dendrite development.The Journal of cell biology · 2020Article
- PDLIM5 inhibits STUB1-mediated degradation of SMAD3 and promotes the migration and invasion of lung cancer cells.The Journal of biological chemistry · 2020Article
- Somatic Mutations Confer Severe Peripheral Neuropathy in POEMS Syndrome-Associated Multicentric Castleman Disease.Neuroscience bulletin · 2020Article
- An Overview of the Cytoskeleton-Associated Role of PDLIM5.Frontiers in physiology · 2020Review
- Ablation of the microRNA-17-92 cluster in neural stem cells diminishes adult hippocampal neurogenesis and cognitive function.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- High expression of PDLIM5 facilitates cell tumorigenesis and migration by maintaining AMPK activation in prostate cancer.Oncotarget · 2017Article
- The Id-protein family in developmental and cancer-associated pathways.Cell communication and signaling : CCS · 2017Review
- Article
- MicroRNA-17-92 regulates myoblast proliferation and differentiation by targeting the ENH1/Id1 signaling axis.Cell death and differentiation · 2016Article
- The Role of Id2 Protein in Neuroblatoma in Children.Pathology oncology research : POR · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Id2 is a natural inhibitor of the basic helix-loop-helix transcription factors and the retinoblastoma tumor suppressor protein. Active Id2 prevents differentiation and promotes cell-cycle progression and tumorigenesis in the nervous system. A key event that regulates Id2 activity during differentiation is translocation from the nucleus to the cytoplasm. Here we show that the actin-associated protein enigma homolog (ENH) is a cytoplasmic retention factor for Id2. ENH contains three LIM domains, which bind to the helix-loop-helix domain of Id proteins in vitro and in vivo. ENH is up-regulated during neural differentiation, and its ectopic expression in neuroblastoma cells leads to translocation of Id2 from the nucleus to the cytoplasm, with consequent inactivation of transcriptional and cell-cycle-promoting functions of Id2. Conversely, silencing of ENH by RNA interference prevents cytoplasmic relocation of Id2 in neuroblastoma cells differentiated with retinoic acid. Finally, the differentiated neural crest-derived tumor ganglioneuroblastoma coexpresses Id2 and ENH in the cytoplasm of ganglionic cells. These data indicate that ENH contributes to differentiation of the nervous system through cytoplasmic sequestration of Id2. They also suggest that ENH is a restraining factor of the oncogenic activity of Id proteins in neural tumors.
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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.