ArticleMolecular and cellular biology2011
Chaperone Hsp27 modulates AUF1 proteolysis and AU-rich element-mediated mRNA degradation.
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 34 papers.
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Who cites it
34 citing papers in PubMed, 58 citations in OpenAlex.
- Reaching Outer Space and Enabling the mRNA Revolution: A Critical Role of Partnerships for Successful Drug and Vaccine Development.Handbook of experimental pharmacology · 2024Review
- Relationship betweenJournal of thoracic disease · 2021Article
- Post-translational Control of RNA-Binding Proteins and Disease-Related Dysregulation.Frontiers in molecular biosciences · 2021Review
- Post-transcriptional regulation of inflammation by RNA-binding proteins via cis-elements of mRNAs.Journal of biochemistry · 2019Review
- Inhibition of the Stromal p38MAPK/MK2 Pathway Limits Breast Cancer Metastases and Chemotherapy-Induced Bone Loss.Cancer research · 2018Article
- ZFP36L1 and AUF1 Induction Contribute to the Suppression of Inflammatory Mediators Expression by Globular Adiponectin via Autophagy Induction in Macrophages.Biomolecules & therapeutics · 2018Article
- Phosphorylated Hsp27 is mutually exclusive with ATRX loss and the IDH1Journal of clinical pathology · 2018Article
- HSPB1 mutations causing hereditary neuropathy in humans disrupt non-cell autonomous protection of motor neurons.Experimental neurology · 2017Article
- HSPB1 facilitates ERK-mediated phosphorylation and degradation of BIM to attenuate endoplasmic reticulum stress-induced apoptosis.Cell death & disease · 2017Article
- Inactivation of p38 MAPK contributes to stem cell-like properties of non-small cell lung cancer.Oncotarget · 2017Article
- Differential IL-1β secretion by monocyte subsets is regulated by Hsp27 through modulating mRNA stability.Scientific reports · 2016Article
- Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular Inflammation.Frontiers in immunology · 2016Review
- Viral activation of stress-regulated Rho-GTPase signaling pathway disrupts sites of mRNA degradation to influence cellular gene expression.Small GTPases · 2015Review
- Mutant glucocerebrosidase in Gaucher disease recruits Hsp27 to the Hsp90 chaperone complex for proteasomal degradation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Viral activation of MK2-hsp27-p115RhoGEF-RhoA signaling axis causes cytoskeletal rearrangements, p-body disruption and ARE-mRNA stabilization.PLoS pathogens · 2015Article
- Global discovery of high-NaCl-induced changes of protein phosphorylation.American journal of physiology. Cell physiology · 2014Article
- p38MAPK plays a crucial role in stromal-mediated tumorigenesis.Cancer discovery · 2014Article
- HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.Cancers · 2014Article
- mRNA decay factor AUF1 binds the internal ribosomal entry site of enterovirus 71 and inhibits virus replication.PloS one · 2014Article
- HspB1 silences translation of PDZ-RhoGEF by enhancing miR-20a and miR-128 expression to promote neurite extension.Molecular and cellular neurosciences · 2013Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
AUF1 is an AU-rich element (ARE)-binding protein that recruits translation initiation factors, molecular chaperones, and mRNA degradation enzymes to the ARE for mRNA destruction. We recently found chaperone Hsp27 to be an AUF1-associated ARE-binding protein required for tumor necrosis factor alpha (TNF-α) mRNA degradation in monocytes. Hsp27 is a multifunctional protein that participates in ubiquitination of proteins for their degradation by proteasomes. A variety of extracellular stimuli promote Hsp27 phosphorylation on three serine residues--Ser(15), Ser(78), and Ser(82)-by a number of kinases, including the mitogen-activated protein (MAP) pathway kinases p38 and MK2. Activating either kinase stabilizes ARE mRNAs. Likewise, ectopic expression of phosphomimetic mutant forms of Hsp27 stabilizes reporter ARE mRNAs. Here, we continued to examine the contributions of Hsp27 to mRNA degradation. As AUF1 is ubiquitinated and degraded by proteasomes, we addressed the hypothesis that Hsp27 phosphorylation controls AUF1 levels to modulate ARE mRNA degradation. Indeed, selected phosphomimetic mutants of Hsp27 promote proteolysis of AUF1 in a proteasome-dependent fashion and render ARE mRNAs more stable. Our results suggest that the p38 MAP kinase (MAPK)-MK2-Hsp27 signaling axis may target AUF1 destruction by proteasomes, thereby promoting ARE mRNA stabilization.
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