ArticlePloS one2013
Mitogen- and stress-activated protein kinases 1 and 2 are required for maximal trefoil factor 1 induction.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Sulforaphene suppresses oesophageal cancer growth through mitogen- and stress-activated kinase 2 in a PDX mouse model.American journal of cancer research · 2023Article
- Rebelled epigenome: histone H3S10 phosphorylation and H3S10 kinases in cancer biology and therapy.Clinical epigenetics · 2020Review
- The nuclear phosphoinositide response to stress.Cell cycle (Georgetown, Tex.) · 2020Review
- High nuclear MSK1 is associated with longer survival in breast cancer patients.Journal of cancer research and clinical oncology · 2018Article
- Mechanisms of Antiulcer Effect of an Active Ingredient Group of Modified Xiao Chaihu Decoction.Evidence-based complementary and alternative medicine : eCAM · 2018Article
- Mitogen-induced distinct epialleles are phosphorylated at either H3S10 or H3S28, depending on H3K27 acetylation.Molecular biology of the cell · 2017Article
- Gastric Proteins MUC5AC and TFF1 as Potential Diagnostic Markers of Colonic Sessile Serrated Adenomas/Polyps.American journal of clinical pathology · 2016Article
- The cyclic AMP response element-binding protein (CREB) mediates smooth muscle cell proliferation in response to angiotensin II.Journal of cell communication and signaling · 2014Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Mitogen- and stress-activated protein kinases 1 and 2 (MSK1 and MSK2), activated downstream of the ERK- and p38-mitogen-activated protein kinase pathways are involved in cell survival, proliferation and differentiation. Following mitogenic or stress stimuli, they mediate the nucleosomal response, which includes phosphorylation of histone H3 at serine 10 (H3S10ph) coupled with transcriptional activation of immediate-early genes. While MSK1 and MSK2 are closely related, their relative roles may vary with cellular context and/or stimuli. However, our knowledge of MSK2 recruitment to immediate-early genes is limited, as research has primarily focused on MSK1. Here, we demonstrate that both MSK1 and MSK2, regulate the phorbol ester 12-O-tetradecanoylphorbol-13-acetate induced expression of the breast cancer marker gene, trefoil factor 1 (TFF1), by phosphorylating H3S10 at its 5' regulatory regions. The MSK-mediated phosphorylation of H3S10 promotes the recruitment of 14-3-3 isoforms and BRG1, the ATPase subunit of the BAF/PBAF remodeling complex, to the enhancer and upstream promoter elements of TFF1. The recruited chromatin remodeling activity leads to the RNA polymerase II carboxy-terminal domain phosphorylation at the TFF1 promoter, initiating TFF1 expression in MCF-7 breast cancer cells. Moreover, we show that MSK1 or MSK2 is recruited to TFF1 regulatory regions, but as components of different multiprotein complexes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.