ArticleFrontiers in cell and developmental biology2020
Regulation of Mitochondrial Respiratory Chain Complex Levels, Organization, and Function by Arginyltransferase 1.
Article in Frontiers in cell and developmental biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 29 citations in OpenAlex.
- Early life factors and genetic interactions in allergic rhinitis: a genome-wide study.BMC pediatrics · 2026Article
- Review
- Implementing N-terminomics and machine learning to probe Nt-arginylation.Nature communications · 2025Article
- Targeting endoplasmic reticulum stress and nitroso-redox imbalance in neuroendocrine prostate cancer: the therapeutic role of nitric oxide.Cell death discovery · 2025Article
- Identification of candidate gene networks affecting the number of somatic cells count and milk production in Iranian Holstein cows using Genome-wide association study.Scientific reports · 2025Article
- Arginyltransferase1 drives a mitochondria-dependent program to induce cell death.Cell death & disease · 2025Article
- Oligomerization and a distinct tRNA-binding loop are important regulators of human arginyl-transferase function.Nature communications · 2024Article
- Article
- The N-degron pathway mediates lipophagy: The chemical modulation of lipophagy in obesity and NAFLD.Metabolism: clinical and experimental · 2023Article
- A comprehensive Drosophila resource to identify key functional interactions between SARS-CoV-2 factors and host proteins.Cell reports · 2023Article
- Structures of Tetrahymena thermophila respiratory megacomplexes on the tubular mitochondrial cristae.Nature communications · 2023Article
- The structural basis of tRNA recognition by arginyl-tRNA-protein transferase.Nature communications · 2023Article
- Article
- The preparation of recombinant arginyltransferase 1 (ATE1) for biophysical characterization.Methods in enzymology · 2023Article
- Comparative analysis of the DNA methylation landscape in CD4, CD8, and B memory lineages.Clinical epigenetics · 2022Article
- Arginylation Regulates Cytoskeleton Organization and Cell Division and Affects Mitochondria in Fission Yeast.Molecular and cellular biology · 2022Article
- Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase.International journal of molecular sciences · 2022Article
- Arginyl-tRNA-protein transferase 1 (ATE1) promotes melanoma cell growth and migration.FEBS letters · 2022Article
- The evolutionarily conserved arginyltransferase 1 mediates a pVHL-independent oxygen-sensing pathway in mammalian cells.Developmental cell · 2022Article
- Liquiritin Attenuates Angiotensin II-Induced Cardiomyocyte Hypertrophy via ATE1/TAK1-JNK1/2 Pathway.Evidence-based complementary and alternative medicine : eCAM · 2022Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
Arginyltransferase 1 (ATE1) is an evolutionary-conserved eukaryotic protein that localizes to the cytosol and nucleus. It is the only known enzyme in metazoans and fungi that catalyzes posttranslational arginylation. Lack of arginylation has been linked to an array of human disorders, including cancer, by altering the response to stress and the regulation of metabolism and apoptosis. Although mitochondria play relevant roles in these processes in health and disease, a causal relationship between ATE1 activity and mitochondrial biology has yet to be established. Here, we report a phylogenetic analysis that traces the roots of ATE1 to alpha-proteobacteria, the mitochondrion microbial ancestor. We then demonstrate that a small fraction of ATE1 localizes within mitochondria. Furthermore, the absence of ATE1 influences the levels, organization, and function of respiratory chain complexes in mouse cells. Specifically,
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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.