ArticleProceedings of the National Academy of Sciences of the United States of America2002
p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 112 citations in OpenAlex.
- White matter disorders at the intersection of transcription, RNA processing and translation.Nature reviews. Neurology · 2026Review
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- A disease-causing isoleucyl-tRNA synthetase variant leads to altered protein complex formation and cellular stress response.The Journal of biological chemistry · 2026Article
- Identification of the proteolytic signature in CVB3-infected cells.Journal of virology · 2024Article
- Identification and structure of AIMP2-DX2 for therapeutic perspectives.BMB reports · 2024Review
- Phosphocode-dependent glutamyl-prolyl-tRNA synthetase 1 signaling in immunity, metabolism, and disease.Experimental & molecular medicine · 2023Review
- EPRS1 Controls the TGF-Molecular and cellular biology · 2023Article
- Multimodal cotranslational interactions direct assembly of the human multi-tRNA synthetase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure and Dynamics of the Human Multi-tRNA Synthetase Complex.Sub-cellular biochemistry · 2022Article
- Drug targeting of aminoacyl-tRNA synthetases in Anopheles species and Aedes aegypti that cause malaria and dengue.Parasites & vectors · 2021Article
- Regulation of ex-translational activities is the primary function of the multi-tRNA synthetase complex.Nucleic acids research · 2021Article
- Single-cell analysis of AIMP2 splice variants informs on drug sensitivity and prognosis in hematologic cancer.Communications biology · 2020Article
- 3-Dimensional architecture of the human multi-tRNA synthetase complex.Nucleic acids research · 2020Article
- Deubiquitinase USP29 Governs MYBBP1A in the Brains of Parkinson's Disease Patients.Journal of clinical medicine · 2019Article
- Aminoacyl tRNA synthetases as potential drug targets of the Panthera pathogen Babesia.Parasites & vectors · 2019Article
- Newly acquired N-terminal extension targets threonyl-tRNA synthetase-like protein into the multiple tRNA synthetase complex.Nucleic acids research · 2019Article
- Evolution of the multi-tRNA synthetase complex and its role in cancer.The Journal of biological chemistry · 2019Review
- Fluorescence-Based Analysis of Noncanonical Functions of Aminoacyl-tRNA Synthetase-Interacting Multifunctional Proteins (AIMPs) in Peripheral Nerves.Materials (Basel, Switzerland) · 2019Article
- Homozygosity for a nonsense variant in AIMP2 is associated with a progressive neurodevelopmental disorder with microcephaly, seizures, and spastic quadriparesis.Journal of human genetics · 2018Article
- MicroRNA-95 promotes myogenic differentiation by down-regulation of aminoacyl-tRNA synthase complex-interacting multifunctional protein 2.Oncotarget · 2017Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian tRNA synthetases form a macromolecular complex with three nonenzyme factors: p43, p38, and p18. Here we introduced a mutation within the mouse p38 gene to understand its functional significance for the formation of the multi-tRNA synthetase complex. The complex was completely disintegrated by the deficiency of p38. In addition, the protein levels and catalytic activities of the component enzymes and cofactors were severely decreased. A partial truncation of the p38 polypeptide separated the associated components into different subdomains. The mutant mice showed lethality within 2 days of birth. Thus, this work provides the first evidence, to our knowledge, that p38 is essential for the structural integrity of the multi-tRNA synthetase complex and mouse viability.
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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.