ArticleHaematologica2014
Loss of ATE1-mediated arginylation leads to impaired platelet myosin phosphorylation, clot retraction, and in vivo thrombosis formation.
Article in Haematologica, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Reconstitution of protein arginylation pathways in bacteria for robust identification and quantification.Communications biology · 2026Article
- Trypsin exhibits exopeptidase-like activity toward N-terminal arginine that biases proteomic analyses.bioRxiv : the preprint server for biology · 2026Article
- Actin arginylation alters myosin engagement and F-actin patterning despite structural conservation.The Journal of cell biology · 2026Article
- An unbiased proteomic platform for ATE1-based arginylation profiling.Nature chemical biology · 2025Article
- Method Overview for Discovering ATE1 Substrates and their Arginylation Sites.Chembiochem : a European journal of chemical biology · 2025Review
- Oligomerization and a distinct tRNA-binding loop are important regulators of human arginyl-transferase function.Nature communications · 2024Article
- A novel technique to quantify the kinetics of blood clot contraction based on the expulsion of fluorescently labeled albumin into serum.Journal of thrombosis and haemostasis : JTH · 2024Article
- Integrin-Dependent Transient Density Increase in Detergent-Resistant Membrane Rafts in Platelets Activated by Thrombin.Biomedicines · 2023Article
- A comprehensive Drosophila resource to identify key functional interactions between SARS-CoV-2 factors and host proteins.Cell reports · 2023Article
- The structural basis of tRNA recognition by arginyl-tRNA-protein transferase.Nature communications · 2023Article
- Iron-sulfur clusters are involved in post-translational arginylation.Nature communications · 2023Article
- Blood clot contraction: Mechanisms, pathophysiology, and disease.Research and practice in thrombosis and haemostasis · 2023Article
- Identification of Arginylated Proteins by Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Platelets derived citrullinated proteins and microparticles are potential autoantibodies ACPA targets in RA patients.Frontiers in immunology · 2023Article
- Arginyl-tRNA-protein transferase 1 (ATE1) promotes melanoma cell growth and migration.FEBS letters · 2022Article
- Article
- Ate1-mediated posttranslational arginylation affects substrate adhesion and cell migration in Dictyostelium discoideum.Molecular biology of the cell · 2019Article
- Inhibition of arginyltransferase 1 induces transcriptional activity of myocardin-related transcription factor A (MRTF-A) and promotes directional migration.The Journal of biological chemistry · 2014Article
- Protein arginylation, a global biological regulator that targets actin cytoskeleton and the muscle.Anatomical record (Hoboken, N.J. : 2007) · 2014Review
- Post-translational arginylation as a novel regulator of platelet function.Haematologica · 2014Article
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10 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein arginylation by arginyl-transfer RNA protein transferase (ATE1) is emerging as a regulator protein function that is reminiscent of phosphorylation. For example, arginylation of β-actin has been found to regulate lamellipodial formation at the leading edge in fibroblasts. This finding suggests that similar functions of β-actin in other cell types may also require arginylation. Here, we have tested the hypothesis that ATE1 regulates the cytoskeletal dynamics essential for in vivo platelet adhesion and thrombus formation. To test this hypothesis, we generated conditional knockout mice specifically lacking ATE1 in their platelets and in their megakaryocytes and analyzed the role of arginylation during platelet activation. Surprisingly, rather than finding an impairment of the actin cytoskeleton structure and its rearrangement during platelet activation, we observed that the platelet-specific ATE1 knockout led to enhanced clot retraction and in vivo thrombus formation. This effect might be regulated by myosin II contractility since it was accompanied by enhanced phosphorylation of the myosin regulatory light chain on Ser19, which is an event that activates myosin in vivo. Furthermore, ATE1 and myosin co-immunoprecipitate from platelet lysates. This finding suggests that these proteins directly interact within platelets. These results provide the first evidence that arginylation is involved in phosphorylation-dependent protein regulation, and that arginylation affects myosin function in platelets during clot retraction.
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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.