Unique roles of tryptophanyl-tRNA synthetase in immune control and its therapeutic implications
Open accessAbstract
Tryptophanyl tRNA synthetase (WRS) is an essential enzyme as it catalyzes the ligation of tryptophan to its cognate tRNA during translation. Interestingly, mammalian WRS has evolved to acquire domains or motifs for novel functions beyond protein synthesis; WRS can also further expand its functions via alternative splicing and proteolytic cleavage. WRS is localized not only to the nucleus but also to the extracellular space, playing a key role in innate immunity, angiogenesis, and IFN-γ signaling. In addition, the expression of WRS varies significantly in different tissues and pathological states, implying that it plays unique roles in physiological homeostasis and immune defense. This review addresses the current knowledge regarding the evolution, structural features, and context-dependent functions of WRS, particularly focusing on its roles in immune regulation.
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Amyloid pathology typically develops early in AD whereas tau pathology occurs later but correlates more accurately with AD progression and cognitive impairment.
“Amyloid pathology typically develops early in AD whereas tau pathology occurs later but correlates more accurately with AD progression and cognitive impairment3–5.”
From <i>APOE3</i> - <i>R136S</i> mutation confers resilience against tau pathology via cGAS-STING-IFN inhibition (2024) · cites this paper as [4]
The Introduction discusses aminoacyl-tRNA synthetases, and the retrieved WRS signaling and clinical relevance passages discuss tryptophanyl-tRNA synthetase rather than Alzheimer’s disease. Searches for amyloid, tau, AD progression, and cognitive impairment found no passage addressing the claimed timing or correlation of these pathologies. (LLM, conf=0.76)
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Naguib, S., Lopez-Lee, C., Torres, E. R., Lee, S.-I., Zhu, J., Zhu, D., Ye, P., Norman, K., Zhao, M., Wong, M. Y., et al. (2024) · doi:10.1101/2024.04.25.591140 · Cited by 25 · see citing works
- Authors
- Jin, M.
- Affiliations
- Gachon University (KR)
- Corresponding author
- Jin, Mirim
- ORCID
- Jin, Mirim
- Venue
- Experimental & Molecular Medicine
- Published
- 2019-01
- Volume
- 51
- Issue
- 1
- Pages
- 1-10
- ISSN
- 1226-3613 (ISSN-L)
- 2092-6413
- PMC
- PMC6321835
- OpenAlex
- W2907665228
- Cited by
- 413
- References
- 0
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- FWCI
- 3.78
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Experimental & Molecular Medicine (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Research Foundation of Korea (NRF2015M3A6A4065732)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Health Sciences › Medicine › Oncology › Cancer Immunotherapy and Biomarkers
- Keywords
- tryptophanyl-tRNA synthetase, immune regulation, innate immunity, angiogenesis, interferon-gamma signaling, alternative splicing, proteolytic cleavage, enzyme evolution, therapeutic target
- MeSH terms
- Animals, Humans, Immune System Diseases, Tryptophan-tRNA Ligase, Signal Transduction
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