import of proteins. KEY WORDS: HuR, RNA stability, Nuclear import, Retinoic acid, Cellular retinoic acid-binding protein, NFκB INTRODUCTION One of the best-characterized RNA-binding proteins in animals is HuR (encoded for by Elavl1), a ubiquitously-expressed member of the embryonic lethal abnormal vision (ELAV)/Hu family of RNA-binding proteins.

Human antigen R (HuR) is an RNA-binding protein that regulates the stability, translation, and nucleus-to-cytoplasm shuttling of its target mRNAs. While HuR is normally localized within the nucleus, it has been shown that HuR binds mRNAs in the nucleus and then escorts the mRNAs to the cytoplasm where HuR protects them from degradation.

This protein functions through post-transcriptional modification of mRNA transcripts by changing the nucleotide content of the RNA. One of the best-characterized RNA-binding proteins in animals is HuR (encoded for by Elavl1), a ubiquitously-expressed member of the embryonic lethal abnormal vision (ELAV)/Hu family of RNA-binding proteins. In the nucleus, HuR is involved in various functions, including RNA splicing and nuclear export. HuR (Human antigen R, encoded by Embryonic Lethal Abnormal Vision‐Like Protein 1, ELAVL1) is an RNA‐binding protein, 26 it may effect the stabilization of mRNAs so as to regulate their expression and is involved in various biological progresses. 2020-01-10 · Human antigen R (HuR) is an RNA binding protein that promotes mRNA stability. Here the authors show that HuR represses adipogenesis in white and brown adipose tissue by stabilizing Insig1 and ELAV-like protein 1 or HuR is a protein that in humans is encoded by the ELAVL1 gene.

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Effective and specific knockdown of HuR was observed at the mRNA and protein levels (Supplementary Fig. S1). Human antigen R (HuR) is an RNA-binding protein that posttranscriptionally regulates many cancer-trait genes. CDC6, a central regulator of DNA replication, is regulated by HuR. In this study, we investigated the role of HuR in colorectal cancer tumorigenesis and oxaliplatin (L-OHP) resistance, as well as the underlying mechanisms involving CDC6. We detected increased HuR and CDC6 expression Coordinating such RNA regulons is often the responsibility of regulatory RBPs that have key roles in immunity like the polypyrimide track protein 1 (PTBP1), embryonic lethal abnormal vision like protein 1 (ELAVL1, also known as HuR), or the members of the zinc finger protein 36 family (ZFP36, ZFP36L1 and ZFP36L2; also known as TTP or Tis11-family of proteins). The RNA-binding protein HuR associates with the p53 mRNA, as reported previously, and with the NPM mRNA, computationally predicted to be a target of HuR. Here, we show that HuR binds the NPM and p53 3′-untranslated regions and stabilizes these mRNAs in polyamine-depleted intestinal epithelial cells. Albeit the suppression of mRNA translation may derive from eIF3a binding to the 5′-UTRs of target mRNAs, how eIF3a may accelerate mRNA translation remains unknown.

Human antigen R (HuR) is an RNA-binding protein that posttranscriptionally regulates many cancer-trait genes. CDC6, a central regulator of DNA replication, is regulated by HuR. In this study, we investigated the role of HuR in colorectal cancer tumorigenesis and oxaliplatin (L-OHP) resistance, as well as the underlying mechanisms involving CDC6. We detected increased HuR and CDC6 expression

compellingly demonstrate in mice that increased HuR activity in myeloid cells has a protective role in the onset of pathologic intestinal inflammation (i.e., colitis) and colitis-associated cancer (CAC). HuR is an RNA-binding protein that resides predominantly in the nucleus but shuttles to the cytosol carrying mRNAs containing a uridylate-rich region in the 3'untranslated region. RNA-binding protein HuR binds to and stabilizes OIP5-AS1. Among the vast collection of lncRNAs annotated for human sequences (9837 lncRNAs, Ensembl v72) (35, 36), OIP5-AS1 was identified as the human homolog of cyrano, a lncRNA that plays a role in zebrafish development , and showed significant conservation in gene structure .

HuR is a member of the embryonic lethal abnormal vision (ELAV) family of RNA-binding proteins . It can shuttle between the nucleus and the cytoplasm, and the stabilization of ARE-mRNA by HuR is believed to be linked to its localization in the cytoplasm (12,13).

The protein encoded by this gene is a member of the ELAVL protein family. This encoded protein contains 3 RNA-binding domains and binds cis-acting AU-rich elements. One of its best-known functions is to stabilize mRNAs in order to regulate gene expression. 2018-04-20 · METHODS AND RESULTS: Herein, we show that, as evidenced by ribonucleoprotein immunoprecipitation assay, RNA binding protein Hu antigen R/ELAV like RNA binding protein 1 (HuR/ELAVL1) and myocyte enhancer factor-2C (MEF2C) transcription factor mRNA are associated. HuR positively regulated transcription factor MEF2C mRNA expression by protecting its mRNA from degradation.

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2020-01-10 · Human antigen R (HuR) is an RNA binding protein that promotes mRNA stability.

The complete spectrum of genes whose expression is regulated by HuR and are the basis for the broad range of cellular functions of the protein is incompletely understood. Human antigen R (HuR) is an RNA-binding protein that regulates the stability, translation, and nucleus-to-cytoplasm shuttling of its target mRNAs. While HuR is normally localized within the nucleus, it has been shown that HuR binds mRNAs in the nucleus and then escorts the mRNAs to the cytoplasm where HuR protects them from degradation. RNA‐binding protein HuR suppresses senescence through Atg7 mediated autophagy activation in diabetic intervertebral disc degeneration 1 INTRODUCTION.
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HuR, a member of the ELAV family of RNA-binding proteins, is a multifunctional protein that has been implicated in the regulation of various aspects of RNA metabolism (Hinman and Lou, 2008). Although primarily known for binding to the 3′ UTRs of mRNAs and increasing their intrinsic stability, several recent reports identified HuR as a bona fide translational regulator as well.

The RNA-binding protein HuR associates with the p53 mRNA, as reported previously, and with the NPM mRNA, computationally predicted to be a target of HuR. Here, we show that HuR binds the NPM and p53 3′-untranslated regions and stabilizes these mRNAs in polyamine-depleted intestinal epithelial cells. Albeit the suppression of mRNA translation may derive from eIF3a binding to the 5′-UTRs of target mRNAs, how eIF3a may accelerate mRNA translation remains unknown. In this study, we show that eIF3a up-regulates translation of Chk1 but not Chk2 mRNA by interacting with HuR, which binds directly to the 3′-UTR of Chk1 mRNA.