ArticleThe Journal of biological chemistry2014
Inhibition of arginyltransferase 1 induces transcriptional activity of myocardin-related transcription factor A (MRTF-A) and promotes directional migration.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- The Final Maturation State of β-actin Involves N-terminal Acetylation by NAA80, not N-terminal Arginylation by ATE1.Journal of molecular biology · 2022Article
- ATE1 Inhibits Liver Cancer Progression through RGS5-Mediated Suppression of Wnt/β-Catenin Signaling.Molecular cancer research : MCR · 2021Article
- Regulation of actin isoforms in cellular and developmental processes.Seminars in cell & developmental biology · 2020Review
- Posttranslational Arginylation Enzyme Arginyltransferase1 Shows Genetic Interactions With Specific Cellular PathwaysFrontiers in physiology · 2020Article
- Long non-coding RNA urothelial cancer associated 1 can regulate the migration and invasion of colorectal cancer cells (SW480) via myocardin-related transcription factor-A.Oncology letters · 2019Article
- Article
- Reduced Arginyltransferase 1 is a driver and a potential prognostic indicator of prostate cancer metastasis.Oncogene · 2019Article
- A regulation loop between Nrf1α and MRTF-A controls migration and invasion in MDA-MB-231 breast cancer cells.International journal of molecular medicine · 2018Article
- The p38/CYLD Pathway is Involved in Necroptosis Induced by Oxygen-glucose Deprivation Combined with ZVAD in Primary Cortical Neurons.Neurochemical research · 2017Article
- Arginyltransferase suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers.Oncogene · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myocardin-related transcription factor A (MRTF-A/MAL/MKL1/BSAC) regulates the expression of serum-response factor (SRF)-dependent target genes in response to the Rho-actin signaling pathway. Overexpression or activation of MRTF-A affects shape, migration, and invasion of cells and contributes to human malignancies, including cancer. In this study, we report that inhibition of arginyltransferase 1 (ATE1), an enzyme mediating post-transcriptional protein arginylation, is sufficient to increase MRTF-A activity in MCF-7 human breast carcinoma cells independently of external growth factor stimuli. In addition, silencing or inhibiting ATE1 disrupted E-cadherin-mediated cell-cell contacts, enhanced formation of actin-rich protrusions, and increased the number of focal adhesions, subsequently leading to elevated chemotactic migration. Although arginylated actin did not differentially affect MRTF-A, a rapid loss of E-cadherin and F-actin reorganization preceded MRTF-A activation upon ATE1 inhibition. Conversely, ectopic ATE1 expression was sufficient to render MRTF-A inactive, both in resting cells and in cells with exogenously activated RhoA-actin pathways. In this study, we provide a critical link between protein arginylation and MRTF-A activity and place ATE1 upstream of myocardin-related transcription factor.
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