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Interaction with Pyruvate Kinase M2 Destabilizes Tristetraprolin by Proteasome Degradation and Regulates Cell Proliferation in Breast Cancer

https://doi.org/10.1038/srep22449
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1 of the 41 references listed on this page is in the Retraction Watch database as retracted (export 2026-11-04): 10.1016/j.bbrc.2014.10.109 (notice 2014-10-29).

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1007/s00018-012-1150-yopenalex-snapshot
Multiple functions of tristetraprolin/TIS11 RNA-binding proteins in the regulation of mRNA biogenesis and degradation
inferredcites →https://doi.org/10.1016/j.abb.2007.04.011openalex-snapshot
Comparative expression of tristetraprolin (TTP) family member transcripts in normal human tissues and cancer cell lines
inferredcites →https://doi.org/10.1016/j.bbagrm.2013.02.003openalex-snapshot
Tristetraprolin (TTP): Interactions with mRNA and proteins, and current thoughts on mechanisms of action
inferredcites →https://doi.org/10.1016/j.bbrc.2014.10.109openalex-snapshot
RETRACTED: Inhibition of PKM2 sensitizes triple-negative breast cancer cells to doxorubicin
inferredcites →https://doi.org/10.1016/j.bbrc.2015.02.112openalex-snapshot
Secreted pyruvate kinase M2 facilitates cell migration via PI3K/Akt and Wnt/β-catenin pathway in colon cancer cells
inferredcites →https://doi.org/10.1016/j.cell.2012.06.033openalex-snapshot
Tristetraprolin Impairs Myc-Induced Lymphoma and Abolishes the Malignant State
inferredcites →https://doi.org/10.1016/j.cell.2012.07.018openalex-snapshot
PKM2 Phosphorylates Histone H3 and Promotes Gene Transcription and Tumorigenesis
inferredcites →https://doi.org/10.1016/j.cellsig.2011.09.015openalex-snapshot
Protor-2 interacts with tristetraprolin to regulate mRNA stability during stress
inferredcites →https://doi.org/10.1016/j.cellsig.2014.03.016openalex-snapshot
Using a yeast two-hybrid system to identify FTCD as a new regulator for HIF-1α in HepG2 cells
inferredcites →https://doi.org/10.1016/j.molcel.2012.01.001openalex-snapshot
Pyruvate Kinase M2 Regulates Gene Transcription by Acting as a Protein Kinase
inferredcites →https://doi.org/10.1016/j.molimm.2007.05.017openalex-snapshot
Tristetraprolin regulates TNF TNF-α mRNA stability via a proteasome dependent mechanism involving the combined action of the ERK and p38 pathways
inferredcites →https://doi.org/10.1016/j.semcancer.2005.04.009openalex-snapshot
Pyruvate kinase type M2 and its role in tumor growth and spreading
inferredcites →https://doi.org/10.1038/emboj.2009.321openalex-snapshot
Coordinated regulation of autophagy by p38α MAPK through mAtg9 and p38IP
inferredcites →https://doi.org/10.1038/nature06667openalex-snapshot
Pyruvate kinase M2 is a phosphotyrosine-binding protein
inferredcites →https://doi.org/10.1038/ncomms6566openalex-snapshot
PKM2 phosphorylates MLC2 and regulates cytokinesis of tumour cells
inferredcites →https://doi.org/10.1038/onc.2010.168openalex-snapshot
The RNA-binding zinc-finger protein tristetraprolin regulates AU-rich mRNAs involved in breast cancer-related processes
inferredcites →https://doi.org/10.1038/onc.2015.6openalex-snapshot
Regulatory circuit of PKM2/NF-κB/miR-148a/152-modulated tumor angiogenesis and cancer progression
inferredcites →https://doi.org/10.1038/sj.emboj.7600163openalex-snapshot
MK2‐induced tristetraprolin:14‐3‐3 complexes prevent stress granule association and ARE‐mRNA decay
inferredcites →https://doi.org/10.1074/jbc.m110.201137openalex-snapshot
Casein Kinase 2 Regulates the mRNA-destabilizing Activity of Tristetraprolin
inferredcites →https://doi.org/10.1074/jbc.m110465200openalex-snapshot
Cytoplasmic Localization of Tristetraprolin Involves 14-3-3-dependent and -independent Mechanisms
inferredcites →https://doi.org/10.1074/jbc.m111.254888openalex-snapshot
Novel Phosphorylation-dependent Ubiquitination of Tristetraprolin by Mitogen-activated Protein Kinase/Extracellular Signal-regulated Kinase Kinase Kinase 1 (MEKK1) and Tumor Necrosis Factor Receptor-associated Factor 2 (TRAF2)
inferredcites →https://doi.org/10.1074/jbc.m113.508226openalex-snapshot
Proviral Insertion in Murine Lymphomas 2 (PIM2) Oncogene Phosphorylates Pyruvate Kinase M2 (PKM2) and Promotes Glycolysis in Cancer Cells
inferredcites →https://doi.org/10.1074/jbc.m114.563312openalex-snapshot
Polyubiquitinated Tristetraprolin Protects from TNF-induced, Caspase-mediated Apoptosis
inferredcites →https://doi.org/10.1074/jbc.m402059200openalex-snapshot
The Stability of Tristetraprolin mRNA Is Regulated by Mitogen-activated Protein Kinase p38 and by Tristetraprolin Itself
inferredcites →https://doi.org/10.1093/abbs/gms106openalex-snapshot
Dual roles of PKM2 in cancer metabolism
inferredcites →https://doi.org/10.1124/jpet.107.133702openalex-snapshot
Compounds That Increase or Mimic Cyclic Adenosine Monophosphate Enhance Tristetraprolin Degradation in Lipopolysaccharide-Treated Murine J774 Macrophages
inferredcites →https://doi.org/10.1126/science.123.3191.309openalex-snapshot
On the Origin of Cancer Cells
inferredcites →https://doi.org/10.1128/mcb.21.9.6461-6469.2001openalex-snapshot
Mitogen-Activated Protein Kinase p38 Controls the Expression and Posttranslational Modification of Tristetraprolin, a Regulator of Tumor Necrosis Factor Alpha mRNA Stability
inferredcites →https://doi.org/10.1128/mcb.26.6.2408-2418.2006openalex-snapshot
Posttranslational Regulation of Tristetraprolin Subcellular Localization and Protein Stability by p38 Mitogen-Activated Protein Kinase and Extracellular Signal-Regulated Kinase Pathways
inferredcites →https://doi.org/10.1136/bmj.321.7261.624openalex-snapshot
ABC of breast diseases: Breast cancer---epidemiology, risk factors, and genetics
inferredcites →https://doi.org/10.1152/ajpcell.00506.2010openalex-snapshot
Constitutive ERK activity induces downregulation of tristetraprolin, a major protein controlling interleukin8/CXCL8 mRNA stability in melanoma cells
inferredcites →https://doi.org/10.1155/2009/634520openalex-snapshot
TIS11 Family Proteins and Their Roles in Posttranscriptional Gene Regulation
inferredcites →https://doi.org/10.1158/0008-5472.can-08-4238openalex-snapshot
The mRNA-Destabilizing Protein Tristetraprolin Is Suppressed in Many Cancers, Altering Tumorigenic Phenotypes and Patient Prognosis
inferredcites →https://doi.org/10.1371/journal.pone.0088301openalex-snapshot
A Regulatory Feedback Loop between HIF-1α and PIM2 in HepG2 Cells
inferredcites →https://doi.org/10.1371/journal.pone.0092949openalex-snapshot
HSP40 Interacts with Pyruvate Kinase M2 and Regulates Glycolysis and Cell Proliferation in Tumor Cells
inferredcites →https://doi.org/10.1586/14789450.4.6.711openalex-snapshot
Phosphorylation site analysis of the anti-inflammatory and mRNA-destabilizing protein tristetraprolin
inferredcites →https://doi.org/10.3109/1061186x.2012.736998openalex-snapshot
Glycolytic enzymes PGK1 and PKM2 as novel transcriptional targets of PPARγ in breast cancer pathophysiology
inferredcites →https://doi.org/10.4049/jimmunol.174.12.7883openalex-snapshot
Structure/Function Analysis of Tristetraprolin (TTP): p38 Stress-Activated Protein Kinase and Lipopolysaccharide Stimulation Do Not Alter TTP Function
inferredcites →https://doi.org/10.4161/cc.20309openalex-snapshot
ZFP36 expression impairs glioblastoma cell lines viability and invasiveness by targeting multiple signal transduction pathways
inferredcites →https://doi.org/10.4161/cc.9.24.14217openalex-snapshot
TIS11/TTP gene family: It's never too late for tumor suppressors
inferredcites →https://doi.org/10.4161/jkst.20662openalex-snapshot
PKM2, STAT3 and HIF-1α

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4771969openalex-extracted
Modulation of Stress Granule Dynamics by Phosphorylation and Ubiquitination in Plants
inferred← citeshttps://doi.org/10.1002/wrna.1368openalex-snapshot
Hallmarks of cancer and AU ‐rich elements
inferred← citeshttps://doi.org/10.1007/s00432-024-05723-4openalex-snapshot
Identification and validation of a lactate metabolism-related six-gene prognostic signature in intrahepatic cholangiocarcinoma
inferred← citeshttps://doi.org/10.1007/s12094-019-02187-8openalex-snapshot
Emerging roles of aerobic glycolysis in breast cancer
inferred← citeshttps://doi.org/10.1016/b978-0-443-13212-4.00029-5openalex-snapshot
An altered metabolic landscape drives quiescence to the reawakening of cancer stem cells
inferred← citeshttps://doi.org/10.1016/j.bbcan.2024.189157openalex-snapshot
Molecular insights into the role of mixed lineage kinase 3 in cancer hallmarks
inferred← citeshttps://doi.org/10.1016/j.bcp.2018.11.003openalex-snapshot
Non-mitotic effect of albendazole triggers apoptosis of human leukemia cells via SIRT3/ROS/p38 MAPK/TTP axis-mediated TNF-α upregulation
inferred← citeshttps://doi.org/10.1016/j.bioorg.2021.104891openalex-snapshot
Discovery and development of tumor glycolysis rate-limiting enzyme inhibitors
inferred← citeshttps://doi.org/10.1016/j.cellsig.2016.09.002openalex-snapshot
Treatment with MAPKAP2 (MK2) inhibitor and DNA methylation inhibitor, 5-aza dC, synergistically triggers apoptosis in hepatocellular carcinoma (HCC) via tristetraprolin (TTP)
inferred← citeshttps://doi.org/10.1016/j.cmet.2020.04.022openalex-snapshot
A Metabolic Roadmap for Somatic Stem Cell Fate
inferred← citeshttps://doi.org/10.1016/j.cytogfr.2016.11.004openalex-snapshot
Post-transcriptional regulation of cytokine and growth factor signaling in cancer
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2021.07.133openalex-snapshot
Carboxyl group-modified α-lactalbumin induces TNF-α-mediated apoptosis in leukemia and breast cancer cells through the NOX4/p38 MAPK/PP2A axis
inferred← citeshttps://doi.org/10.1016/j.isci.2024.111162openalex-snapshot
Modulation of stress granule dynamics by phosphorylation and ubiquitination in plants
inferred← citeshttps://doi.org/10.1016/j.jcmgh.2020.09.012openalex-snapshot
Tristetraprolin Promotes Hepatic Inflammation and Tumor Initiation but Restrains Cancer Progression to Malignancy
inferred← citeshttps://doi.org/10.1016/j.molimm.2019.09.004openalex-snapshot
CXCL4 is a driver of cytokine mRNA stability in monocyte-derived dendritic cells
inferred← citeshttps://doi.org/10.1038/s41577-020-0406-2openalex-snapshot
Lactate modulation of immune responses in inflammatory versus tumour microenvironments
inferred← citeshttps://doi.org/10.1111/imr.12932openalex-snapshot
Cell‐intrinsic mechanisms to restrain inflammatory responses in T lymphocytes
inferred← citeshttps://doi.org/10.1111/jcmm.14949openalex-snapshot
SIRT3, PP2A and TTP protein stability in the presence of TNF‐α on vincristine‐induced apoptosis of leukaemia cells
inferred← citeshttps://doi.org/10.11606/d.17.2023.tde-10082023-095622openalex-snapshot
Papel da enzima piruvato quinase M2 (PKM2) na modulação da ativação astrocitária
inferred← citeshttps://doi.org/10.1186/s12943-018-0791-3openalex-snapshot
Pyruvate kinase M2 fuels multiple aspects of cancer cells: from cellular metabolism, transcriptional regulation to extracellular signaling
inferred← citeshttps://doi.org/10.1186/s13075-018-1638-4openalex-snapshot
Control of cytokine mRNA degradation by the histone deacetylase inhibitor ITF2357 in rheumatoid arthritis fibroblast-like synoviocytes: beyond transcriptional regulation
inferred← citeshttps://doi.org/10.1186/s13578-019-0317-8openalex-snapshot
PKM2, function and expression and regulation
inferred← citeshttps://doi.org/10.18632/oncotarget.15999openalex-snapshot
MiR-let-7a inhibits cell proliferation, migration, and invasion by down-regulating PKM2 in cervical cancer
inferred← citeshttps://doi.org/10.18632/oncotarget.22529openalex-snapshot
PKM2 in carcinogenesis and oncotherapy
inferred← citeshttps://doi.org/10.18632/oncotarget.25850openalex-snapshot
Nuclear PKM2 promotes the progression of oral squamous cell carcinoma by inducing EMT and post-translationally repressing TGIF2
inferred← citeshttps://doi.org/10.2147/ott.s152999openalex-snapshot
Expression of pyruvate kinase M2 in human bladder cancer and its correlation with clinical parameters and prognosis
inferred← citeshttps://doi.org/10.2174/0118715206394408250806065235openalex-snapshot
Promising Role of PKM2 in the Diagnosis and Prognosis of Ovarian Cancer
inferred← citeshttps://doi.org/10.3389/fcell.2024.1414759openalex-snapshot
Stress granule-related genes during embryogenesis of an invertebrate chordate
inferred← citeshttps://doi.org/10.3389/fgene.2022.970619openalex-snapshot
Non-coding regions of nuclear-DNA-encoded mitochondrial genes and intergenic sequences are targeted by autoantibodies in breast cancer
inferred← citeshttps://doi.org/10.3389/fimmu.2025.1512859openalex-snapshot
A novel glycolysis-related gene signature for predicting prognosis and immunotherapy efficacy in breast cancer
inferred← citeshttps://doi.org/10.3389/fmicb.2022.934786openalex-snapshot
Intestinal Flora-Derived Kynurenic Acid Protects Against Intestinal Damage Caused by Candida albicans Infection via Activation of Aryl Hydrocarbon Receptor
inferred← citeshttps://doi.org/10.3390/ijms21186648openalex-snapshot
mRNA Post-Transcriptional Regulation by AU-Rich Element-Binding Proteins in Liver Inflammation and Cancer
inferred← citeshttps://doi.org/10.3390/v13040584openalex-snapshot
Negative Regulation of the Innate Immune Response through Proteasomal Degradation and Deubiquitination
inferred← citeshttps://doi.org/10.3892/ijo.2020.5152openalex-snapshot
Critical role of mTOR in regulating aerobic glycolysis in carcinogenesis (Review)
inferred← citeshttps://doi.org/10.5582/bst.2022.01473openalex-snapshot
RNA-binding proteins in metabolic-associated fatty liver disease (MAFLD): From mechanism to therapy
inferred← citeshttps://doi.org/10.57709/17536307openalex-snapshot
Dimer Pyruvate Kinase M2 Regulates de novo Collagen Synthesis and Crosslinking in Pathological Fibrosis
inferred← citeshttps://doi.org/10.70675/c8ff778czca4bz4c16z8ceez5a2cd64a9aabopenalex-snapshot
Découverte d'un nouveau type de régulateur de réplication ADN : l'enzyme glycolytique pyruvate kinase en Bacillus subtilis
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