Proteomic Analysis Identifies ATE1-Dependent Arginylation Dysregulation across Meningioma Grades.
Overview
- GlycoProteomics Laboratory, Department of Parasitology, ICB, University of São Paulo, Sao Paulo CEP: 05508-900, Brazil
- Laboratory of Molecular and Cellular Biology (LIM 15), Department of Neurology, Faculdade de Medicina FMUSP, Universidade de São Paulo, São Paulo CEP: 01246-903, Brazil
- Motor Neuron Disease Research Centre, Faculty of Medicine, Health and Human Sciences, Macquarie Medical School, Sydney, New South Wales 2109, Australia
Abstract
Meningiomas are the most common primary brain tumors, yet the molecular pathways that distinguish grade 1 from grade 2 lesions remain insufficiently understood. Among post-translational modifications, N-terminal arginylationcatalyzed by ATE1regulates protein stability and cellular stress responses, but its role in meningioma biology has not been explored. Here, we integrated mass-spectrometry–based proteomics, immunoblotting, and transcriptomic reanalysis to investigate pathway regulation across tumor grades. Grade 1 meningiomas displayed higher ATE1 expression and increased arginylation of key chaperones, accompanied by activation of the PERK branch of the unfolded protein response (UPR), enhanced autophagy, and greater engagement of apoptotics pathways. In contrast, grade 2 tumors showed reduced ATE1 levels, diminished BIP arginylation, attenuated UPR-PERK signaling, impaired autophagy, and increased proliferative signaling. Proteins predicted to be substrates of ATE1-mediated degradation were upregulated in grade 2 tumors, suggesting that loss of arginylation may stabilize pro-oncogenic factors. Together, these findings reveal grade-specific remodeling of the N-degron/
Reproduced under the paper's license (CC BY), from the paper cited above.
Code
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Data
Datasets cited
- geo:GSE136661, at NCBI GEO; found in the text, “RNA-Seq Data Reanalysis”
Data Availability Statement
Project Name: Proteomic analysis identifies ATE1-dependent arginylation dysregulation across meningioma grades Project Accession: PXD071919 Project DOI: Not applicable
Reproduced under the paper's license (CC BY), from the paper cited above.
Versions
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Version 3, 28 September 2026
- Publisher: n/a → American Chemical Society
Version 1, 27 September 2026: the first record
Recorded: type, language, journal, volume, issue, pages, dates, 7 authors, 6 keywords, 13 MeSH terms, 3 funders, 44 references.
Cite
This paper
Macedo-da-Silva, J., Pereira, B. J. A., Mule, S. N., Oba-Shinjo, S. M., Rosa-Fernandes, L., Marie, S. K. N., & Palmisano, G. (2026). Proteomic Analysis Identifies ATE1-Dependent Arginylation Dysregulation across Meningioma Grades. Journal of proteome research, 25(8), 3926-3936. https://
BibTeX
@article{macedodasilva20
author = {Macedo-da-Silva, Janaina and Pereira, Benedito Jamilson Araújo and Mule, Simon Ngao and Oba-Shinjo, Sueli Mieko and Rosa-Fernandes, Livia and Marie, Suely K N and Palmisano, Giuseppe},
title = {{Proteomic Analysis Identifies ATE1-Dependent Arginylation Dysregulation across Meningioma Grades}},
journal = {Journal of proteome research},
year = {2026},
month = aug,
volume = {25},
number = {8},
pages = {3926--3936},
publisher = {American Chemical Society},
issn = {1535-3893},
doi = {10.1021/
url = {https://
pmid = {42372081},
pmcid = {PMC13459535}
}
RIS
TY - JOUR
AU - Macedo-da-Silva, Janaina
AU - Pereira, Benedito Jamilson Araújo
AU - Mule, Simon Ngao
AU - Oba-Shinjo, Sueli Mieko
AU - Rosa-Fernandes, Livia
AU - Marie, Suely K N
AU - Palmisano, Giuseppe
TI - Proteomic Analysis Identifies ATE1-Dependent Arginylation Dysregulation across Meningioma Grades
T2 - Journal of proteome research
J2 - J Proteome Res
PY - 2026
DA - 2026/
VL - 25
IS - 8
SP - 3926
EP - 3936
SN - 1535-3893
PB - American Chemical Society
DO - 10.1021/
UR - https://
LA - en
ER -
CSL-JSON
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"language": "en",
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