ArticleCell cycle (Georgetown, Tex.)2011
The dual-specificity phosphatase hYVH1 (DUSP12) is a novel modulator of cellular DNA content.
Article in Cell cycle (Georgetown, Tex.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- DUSP family phosphatases in cell signaling, inflammation, and chronic diseases.Journal of biomedical science · 2026Review
- DUSP12 promotes cell cycle progression and protects cells from ZNF622 mediated apoptosis.Cell death & disease · 2026Article
- Mutational Analyses of the Cysteine-Rich Domain of Yvh1, a Protein Required for Translational Competency in Yeast.Biology · 2022Article
- Zinc-binding domain mediates pleiotropic functions of Yvh1 in Cryptococcus neoformans.Journal of microbiology (Seoul, Korea) · 2021Article
- Expression of DUSP12 Reduces Lung Vascular Endothelial Cell Damage in a Murine Model of Lipopolysaccharide-Induced Acute Lung Injury via the Apoptosis Signal-Regulating Kinase 1 (ASK1)-Jun N-Terminal Kinase Activation (JNK) Pathway.Medical science monitor : international medical journal of experimental and clinical research · 2021Article
- Comparative Analysis of Multiple Neurodegenerative Diseases Based on Advanced Epigenetic Aging Brain.Frontiers in genetics · 2021Article
- Characterization of Single Gene Deletion Mutants Affecting Alternative Oxidase Production inMicroorganisms · 2020Article
- Upregulation of DUSP14 Affects Proliferation, Invasion and Metastasis, Potentially via Epithelial-Mesenchymal Transition and Is Associated with Poor Prognosis in Pancreatic Cancer.Cancer management and research · 2020Article
- Dual Specificity Phosphatase 12 Regulates Hepatic Lipid Metabolism Through Inhibition of the Lipogenesis and Apoptosis Signal-Regulating Kinase 1 Pathways.Hepatology (Baltimore, Md.) · 2019Article
- Dual-Specificity Phosphatases in Immunity and Infection: An Update.International journal of molecular sciences · 2019Review
- The Atypical Dual Specificity Phosphatase hYVH1 Associates with Multiple Ribonucleoprotein Particles.The Journal of biological chemistry · 2017Article
- Blockade of dual-specificity phosphatase 28 decreases chemo-resistance and migration in human pancreatic cancer cells.Scientific reports · 2015Article
- Protein tyrosine phosphatase profiling studies during brown adipogenic differentiation of mouse primary brown preadipocytes.BMB reports · 2013Article
- Zinc and the modulation of redox homeostasis.Free radical biology & medicine · 2012Review
- DUSPs strike again.Cell cycle (Georgetown, Tex.) · 2011Article
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Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dual-specificity phosphatase hYVH1 (DUSP12) is an evolutionary conserved phosphatase that also contains a unique zinc-binding domain. Recent evidence suggests that this enzyme plays a role in cell survival and ribosome biogenesis. Here, we report that hYVH1 expression also affects cell cycle progression. Overexpression of hYVH1 caused a significant increase in polyploidy and in the G 2/M cell population, with a subsequent decrease in the G 0/G 1 population. Phosphatase activity is dispensable, while the zinc-binding domain is necessary and sufficient for hYVH1-mediated cell cycle changes. In agreement with this, siRNA-mediated silencing of hYVH1 expression resulted in a dramatic increase in the G 0/G 1 population and susceptibility to cellular senescence. Additionally, mass spectrometry-based methods identified novel hYVH1 phosphorylation sites, including a C-terminal modification at position Ser ( 335) in the zinc-binding domain. Interestingly, phosphorylation at Ser335 regulates subcellular targeting of hYVH1 and augments the hYVH1 G 2/M phenotype. Collectively we demonstrate that hYVH1 is a novel modulator of cell cycle progression; a function mainly mediated by its C-terminal zinc-binding domain.
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