ArticleMolecular and cellular biology2011
CARHSP1 is required for effective tumor necrosis factor alpha mRNA stabilization and localizes to processing bodies and exosomes.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 51 citations in OpenAlex.
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- A chemical epigenetic tool to probe site-specific DNA-binding protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Defective Olfactomedin-2 connects adipocyte dysfunction to obesity.Nature communications · 2025Article
- The RNA binding protein CARHSP1 facilitates tumor growth, metastasis and immune escape by enhancing IL-17RA mRNA stabilization in prostate cancer.Cell & bioscience · 2025Article
- Quantitative proteomics reveals the dynamic proteome landscape of zebrafish embryos during the maternal-to-zygotic transition.iScience · 2024Article
- Protein Profiling of Placental Extracellular Vesicles in Gestational Diabetes Mellitus.International journal of molecular sciences · 2024Article
- Targeting an essentialiScience · 2023Article
- A PMM2-CDG caused by an A108V mutation associated with a heterozygous 70 kilobases deletion case report.Italian journal of pediatrics · 2022Article
- Identification of Novel Regulators of Radiosensitivity Using High-Throughput Genetic Screening.International journal of molecular sciences · 2022Review
- Equine vitiligo-like depigmentation in grey horses is related to genes involved in immune response and tumor metastasis.BMC veterinary research · 2021Article
- Genome-wide CRISPR/Cas9 screening identifies CARHSP1 responsible for radiation resistance in glioblastoma.Cell death & disease · 2021Article
- Impact of phosphorylation on thermal stability of proteins.Nature methods · 2021Article
- Review
- Pleiotropic roles of cold shock proteins with special emphasis on unexplored cold shock protein member of Plasmodium falciparum.Malaria journal · 2020Review
- Article
- MicroRNA sequences modulating inflammation and lipid accumulation in macrophage "foam" cells: Implications for atherosclerosis.World journal of cardiology · 2020Review
- HInflammation research : official journal of the European Histamine Research Society ... [et al.] · 2020Article
- Titanium Dioxide Nanoparticles Alter the Cellular Phosphoproteome in A549 Cells.Nanomaterials (Basel, Switzerland) · 2020Article
- Proximal Tubule Translational Profiling during Kidney Fibrosis Reveals Proinflammatory and Long Noncoding RNA Expression Patterns with Sexual Dimorphism.Journal of the American Society of Nephrology : JASN · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tumor necrosis factor alpha (TNF-α) is a critical mediator of inflammation, and its production is tightly regulated, with control points operating at nearly every step of its biosynthesis. We sought to identify uncharacterized TNF-α 3' untranslated region (3'UTR)-interacting proteins utilizing a novel screen, termed the RNA capture assay. We identified CARHSP1, a cold-shock domain-containing protein. Knockdown of CARHSP1 inhibits TNF-α protein production in lipopolysaccharide (LPS)-stimulated cells and reduces the level of TNF-α mRNA in both resting and LPS-stimulated cells. mRNA stability assays demonstrate that CARHSP1 knockdown decreases TNF-α mRNA stability from a half-life (t(1/2)) of 49 min to a t(1/2) of 22 min in LPS-stimulated cells and from a t(1/2) of 29 min to a t(1/2) of 24 min in resting cells. Transfecting CARHSP1 into RAW264.7 cells results in an increase in TNF-α 3'UTR luciferase expression in resting cells and CARHSP1 knockdown LPS-stimulated cells. We examined the functional effect of inhibiting Akt, calcineurin, and protein phosphatase 2A and established that inhibition of Akt or calcineurin but not PP2A inhibits CARHSP1 function. Subcellular analysis establishes CARHSP1 as a cytoplasmic protein localizing to processing bodies and exosomes but not on translating mRNAs. We conclude CARHSP1 is a TNF-α mRNA stability enhancer required for effective TNF-α production, demonstrating the importance of both stabilization and destabilization pathways in regulating the TNF-α mRNA half-life.
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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.