Open Access
Journal of Neurochemistry, volume 138, issue 4, pages 506-517
Post-translational protein arginylation in the normal nervous system and in neurodegeneration
1
Centro de Investigaciones de Química Biológica de Córdoba; CIQUIBIC; Departamento de Química Biológica; Facultad de Ciencias Químicas; CONICET; Universidad Nacional de Córdoba; Ciudad Universitaria; Córdoba Argentina
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Publication type: Journal Article
Publication date: 2016-07-05
Journal:
Journal of Neurochemistry
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 4.7
ISSN: 00223042, 14714159
Biochemistry
Cellular and Molecular Neuroscience
Abstract
Post‐translational arginylation of proteins is an important regulator of many physiological pathways in cells. This modification was originally noted in protein degradation during neurodegenerative processes, with an apparently different physiological relevance between central and peripheral nervous system. Subsequent studies have identified a steadily increasing number of proteins and proteolysis‐derived polypeptides as arginyltransferase (ATE1) substrates, including β‐amyloid, α‐synuclein, and TDP43 proteolytic fragments. Arginylation is involved in signaling processes of proteins and polypeptides that are further ubiquitinated and degraded by the proteasome. In addition, it is also implicated in autophagy/lysosomal degradation pathway. Recent studies using mutant mouse strains deficient in ATE1 indicate additional roles of this modification in neuronal physiology. As ATE1 is capable of modifying proteins either at the N‐terminus or middle‐chain acidic residues, determining which proteins function are modulated by arginylation represents a big challenge. Here, we review studies addressing various roles of ATE1 activity in nervous system function, and suggest future research directions that will clarify the role of post‐translational protein arginylation in brain development and various neurological disorders.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Galiano M. R., Goitea V. E., Hallak M. Post-translational protein arginylation in the normal nervous system and in neurodegeneration // Journal of Neurochemistry. 2016. Vol. 138. No. 4. pp. 506-517.
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Galiano M. R., Goitea V. E., Hallak M. Post-translational protein arginylation in the normal nervous system and in neurodegeneration // Journal of Neurochemistry. 2016. Vol. 138. No. 4. pp. 506-517.
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TY - JOUR
DO - 10.1111/jnc.13708
UR - https://doi.org/10.1111%2Fjnc.13708
TI - Post-translational protein arginylation in the normal nervous system and in neurodegeneration
T2 - Journal of Neurochemistry
AU - Hallak, Marta E.
AU - Galiano, Mauricio R.
AU - Goitea, Victor E
PY - 2016
DA - 2016/07/05 00:00:00
PB - Wiley
SP - 506-517
IS - 4
VL - 138
SN - 0022-3042
SN - 1471-4159
ER -
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@article{2016_Galiano,
author = {Marta E. Hallak and Mauricio R. Galiano and Victor E Goitea},
title = {Post-translational protein arginylation in the normal nervous system and in neurodegeneration},
journal = {Journal of Neurochemistry},
year = {2016},
volume = {138},
publisher = {Wiley},
month = {jul},
url = {https://doi.org/10.1111%2Fjnc.13708},
number = {4},
pages = {506--517},
doi = {10.1111/jnc.13708}
}
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Galiano, Mauricio R., et al. “Post-translational protein arginylation in the normal nervous system and in neurodegeneration.” Journal of Neurochemistry, vol. 138, no. 4, Jul. 2016, pp. 506-517. https://doi.org/10.1111%2Fjnc.13708.