ArticleMolecular and cellular biology1996
The extracellular signal-regulated kinase pathway phosphorylates AML1, an acute myeloid leukemia gene product, and potentially regulates its transactivation ability.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 150 citations in OpenAlex.
- Cytogenetic and Molecular Analysis of a "Double-Hit" RUNX1 Including a RUNX1 p.Trp279* and a Cryptic Novel t(6;21)(q25;q22)/RUNX1::ARID1B in Acute Myeloid Leukemia.Genes, chromosomes & cancer · 2026Article
- CDK9 phosphorylates RUNX1 to promote megakaryocytic fate in megakaryocytic-erythroid progenitors.Blood · 2024Article
- Pharmacological inhibition of RAS overcomes FLT3 inhibitor resistance in FLT3-ITD+ AML through AP-1 and RUNX1.iScience · 2024Article
- Review
- Runx Transcription Factors in T Cells-What Is Beyond Thymic Development?Frontiers in immunology · 2021Review
- Alprazolam Prompts HIV-1 Transcriptional Reactivation and Enhances CTL Response Through RUNX1 Inhibition and STAT5 Activation.Frontiers in neurology · 2021Article
- RUNX1: an emerging therapeutic target for cardiovascular disease.Cardiovascular research · 2020Review
- Inflammatory and mitogenic signals drive interleukin 23 subunit alpha (IL23A) secretion independent of IL12B in intestinal epithelial cells.The Journal of biological chemistry · 2020Article
- RUNX1 Dosage in Development and Cancer.Molecules and cells · 2020Review
- RUNX family: Oncogenes or tumor suppressors (Review).Oncology reports · 2019Review
- Activated MEK/ERK Pathway Drives Widespread and Coordinated Overexpression of UHRF1 and DNMT1 in Cancer cells.Scientific reports · 2019Article
- Alk5/Runx1 signaling mediated by extracellular vesicles promotes vascular repair in acute respiratory distress syndrome.Clinical and translational medicine · 2018Article
- Article
- RUNX1: A Regulator of NF-kB Signaling in Pulmonary Diseases.Current protein & peptide science · 2018Review
- RUNX1 contributes to higher-order chromatin organization and gene regulation in breast cancer cells.Biochimica et biophysica acta · 2016Article
- Role of Runx2 phosphorylation in prostate cancer and association with metastatic disease.Oncogene · 2016Article
- Loss of RUNX1/AML1 arginine-methylation impairs peripheral T cell homeostasis.British journal of haematology · 2015Article
- Review
- Targeting IL-17B-IL-17RB signaling with an anti-IL-17RB antibody blocks pancreatic cancer metastasis by silencing multiple chemokines.The Journal of experimental medicine · 2015Article
- The RUNX family: developmental regulators in cancer.Nature reviews. Cancer · 2015Review
8 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AML1 (also called PEBP2alphaB, CBFA2, or CBFalpha2) is one of the most frequently disrupted genes in chromosome abnormalities seen in human leukemias. It has been reported that AML1 plays several pivotal roles in myeloid hematopoietic differentiation and other biological phenomena, probably through the transcriptional regulation of various relevant genes. Here, we investigated the mechanism of regulation of AML1 functions through signal transduction pathways. The results showed that AML1 is phosphorylated in vivo on two serine residues within the proline-, serine-, and threonine-rich region, with dependence on the activation of extracellular signal-regulated kinase (ERK) and with interleukin-3 stimulation in a hematopoietic cell line. These in vivo phosphorylation sites of AML1 were phosphorylated directly in vitro by ERK. Although differences between wild-type AML1 and phosphorylation site mutants in DNA-binding affinity were not observed, we have shown that ERK-dependent phosphorylation potentiates the transactivation ability of AML1. Furthermore the phosphorylation site mutations reduced the transforming capacity of AML1 in fibroblast cells. These data indicate that AML1 functions are potentially regulated by ERK, which is activated by cytokine and growth factor stimuli. This study provides some important clues for clarifying unidentified facets of the regulatory mechanism of AML1 function.
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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.