HuR binds to a single site on the C/EBPβ mRNA of 3T3-L1 adipocytes

Jones, Heath; Carver, M; Pekala, Phillip H.

doi:10.1016/j.bbrc.2007.01.136

Cited by 11 publications

(15 citation statements)

References 11 publications

(19 reference statements)

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“…In concordance with previous studies (13,23), we found that C/EBPb mRNA is a target of HuR in human ALCLs. Moreover, we showed that the kinase activity of NPM-ALK enhances the binding of HuR to C/EBPb mRNA, and more generally, as exemplified by actin and VEGF, to ARE-bearing mRNAs.…”

Section: Discussionsupporting

confidence: 81%

“…Previous studies performed in murine adipocytes revealed that C/EBPb 3 0 -UTR contains an AUUUA motif that constitutes a binding site for HuR (13). To determine whether HuR also binds to C/EBPb mRNA in ALK þ ALCLs, we performed RNP-IP assays using anti-HuR antibodies under conditions that preserved the RNP complexes integrity.…”

Section: C/ebpb 3 0 -Utr Is a Target Of The Rna-binding Protein Hur Imentioning

confidence: 99%

“…However, C/EBPb mRNA also possesses a 3 0 -untranslated region (3 0 -UTR) that contains U-and AU-rich elements (ARE), that has been shown to bind the AU-binding protein (AUBP) HuR in adipocytes (13). HuR is a ubiquitously expressed protein of 36 kDa that belongs to the Hu/ embryonic lethal abnormal vision (ELAV) family of proteins.…”

Section: Introductionmentioning

confidence: 99%

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HuR-Mediated Control of C/EBPβ mRNA Stability and Translation in ALK-Positive Anaplastic Large Cell Lymphomas

Bergalet

Fawal

Lopez

et al. 2011

Molecular Cancer Research

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The CCAAT/enhancer-binding protein b (C/EBPb) plays a major role in the pathogenesis of anaplastic large cell lymphomas (ALCL) that express the nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) tyrosine kinase (ALK þ ). Although ALK-mediated C/EBPb transcriptional activation has been reported, C/EBPb mRNA possesses U-and AU-rich domains in its 3 0 -untranslated region (3 0 -UTR) that might be privileged targets for posttranscriptional control in ALK þ ALCLs. The purpose of this study was to explore this possibility. By using human ALCL-derived cells and a murine model of ALK-transformed cells, we show that the AU-binding protein HuR binds to the 3 0

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Section: Discussionsupporting

confidence: 81%

Section: C/ebpb 3 0 -Utr Is a Target Of The Rna-binding Protein Hur Imentioning

confidence: 99%

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HuR-Mediated Control of C/EBPβ mRNA Stability and Translation in ALK-Positive Anaplastic Large Cell Lymphomas

Bergalet

Fawal

Lopez

et al. 2011

Molecular Cancer Research

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“…1B, lanes 1, 4, 7, and 10 display the various probes in the absence of added protein; lanes 2,5,8, and 11 show the probes ϩ protein; and lanes 3,6,9, and 12 display the interaction of the probes with protein and HuR antibody. As demonstrated in lanes 1-3, the ␤wt ARE forms a complex with HuR and is recognized by the HuR antibody, as we have demonstrated previously (28,32). Lanes 4 -6 display the ␤pm riboprobe in which single base changes at each terminus of the ARE were made, and, as shown in the figure, binding was not altered.…”

Section: Ectopic Expression Of Both Wild Type and Mutant C/ebp␤ Mrnasmentioning

confidence: 54%

“…Our recent detailed analysis demonstrated the presence of a single binding site for HuR in the C/EBP␤ mRNA. That site is in the AU-rich element (ARE) in the 3Ј-UTR of the message (32). Therefore, to address the function of HuR in the translocation and expression of C/EBP␤, we created constructs that expressed wild type C/EBP␤ as well as mutants that could not bind HuR (Fig.…”

Section: Ectopic Expression Of Both Wild Type and Mutant C/ebp␤ Mrnasmentioning

confidence: 99%

Post-transcriptional Control of CCAAT/Enhancer-binding Protein β (C/EBPβ) Expression

Cherry¹,

Jones²,

Karschner³

et al. 2008

Journal of Biological Chemistry

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In 3T3-L1 cells, HuR is constitutively expressed and prior to induction of differentiation localized predominantly to the nucleus. Within minutes of induction of differentiation, nuclear HuR binds to its target ligand mRNAs, and the complexes appear to move to the cytosol. One ligand mRNA is the CCAAT/ enhancer-binding protein ␤ (C/EBP␤) message. To examine the function and importance of the HuR-C/EBP␤ interaction, retroviral expression constructs were created in which the HuR binding site was altered by deletion (␤del) or deletion and substitution (␤d/s). Expression of these constructs in murine embryonic fibroblasts resulted in significant adipose conversion relative to those cells expressing wild type C/EBP␤. C/EBP␤ protein content was increased markedly in both ␤del and ␤d/s, which correlated with the acquisition of the adipocyte phenotype. Analysis of the ␤d/s cell line demonstrated a robust expression of C/EBP␣ coincident with peroxisome proliferatoractivated receptor ␥ expression. Total C/EBP␤ mRNA accumulation indicated no difference between cells harboring either the wild type C/EBP␤ cDNA or ␤d/s construct. However, cytosolic C/EBP␤ mRNA in the cells expressing the ␤d/s construct was maintained at levels between 2-and 7-fold greater than in the cells expressing the wild type construct. Alteration in mRNA half-life was not responsible for the increased accumulation. Mechanistically, these data suggest that HuR binding results in nuclear retention of the C/EBP␤ mRNA and is consistent with HuR control, at least in part, of mRNA processing.

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Novel Insights into Adipogenesis from the Perspective of Transcriptional and RNA N6‐Methyladenosine‐Mediated Post‐Transcriptional Regulation

et al. 2020

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Obesity is a critical risk factor causing the development of metabolic diseases and cancers. Its increasing prevalence worldwide has aroused great concerns of the researchers on adipose development and metabolic function. During adipose expansion, adipogenesis is a way to store lipids as well as to avoid lipotoxicity in other tissues, and may be an approach to offset the negative metabolic effects of obesity. In this Review, the transcriptional regulation of adipogenesis is outlined to characterize numerous biological processes in research on the determination of adipocyte fate and regulation of adipogenic differentiation. Notably, one of the post‐transcriptional modifications of mRNA, namely, N 6 ‐methyladenosine (m 6 A), has been recently found to play a role in adipogenesis. Here, the roles of m 6 A‐related enzymes and proteins in adipogenesis, with a particular focus on how these m 6 A‐related proteins function at different stages of adipogenesis, are mainly discussed. The Review also highlights the coordination role of the transcriptional and post‐transcriptional (RNA m 6 A methylation) regulation in adipogenesis and related biological processes. In this context, a better understanding of adipogenesis at both the transcriptional and post‐transcriptional levels may facilitate the development of novel strategies to improve metabolic health in obesity.

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HuR binds to a single site on the C/EBPβ mRNA of 3T3-L1 adipocytes

Cited by 11 publications

References 11 publications

HuR-Mediated Control of C/EBPβ mRNA Stability and Translation in ALK-Positive Anaplastic Large Cell Lymphomas

HuR-Mediated Control of C/EBPβ mRNA Stability and Translation in ALK-Positive Anaplastic Large Cell Lymphomas

Post-transcriptional Control of CCAAT/Enhancer-binding Protein β (C/EBPβ) Expression

Novel Insights into Adipogenesis from the Perspective of Transcriptional and RNA N6‐Methyladenosine‐Mediated Post‐Transcriptional Regulation

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