Effects of alpha-synuclein post-translational modifications on metal binding
- Autores
- González, Nazareno; Arcos López, Trinidad; König, Annekatrin; Quintanar, Liliana; Menacho Márquez, Mauricio Ariel; Outeiro, Tiago F.; Fernandez, Claudio Oscar
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Parkinson’s disease is the second most common neurodegenerative disorder worldwide. Neurodegeneration in this pathology is characterized by the loss of dopaminergic neurons in the substantia nigra, coupled with cytoplasmic inclusions known as Lewy bodies containing α-synuclein. The brain is an organ that concentrates metal ions, and there is emerging evidence that a break-down in metal homeostasis may be a critical factor in a variety of neurodegenerative diseases. α-synuclein has emerged as an important metal-binding protein in the brain, whereas these interactions play an important role in its aggregation and might represent a link between protein aggregation, oxidative damage, and neuronal cell loss. Additionally, α-synuclein undergoes several post-translational modifications that regulate its structure and physiological function, and may be linked to the aggregation and/or oligomer formation. This review is focused on the interaction of this protein with physiologically relevant metal ions, highlighting the cases where metal-AS interactions profile as key modulators for its structural, aggregation, and membrane-binding properties. The impact of α-synuclein phosphorylation and N-terminal acetylation in the metal-binding properties of the protein are also discussed, underscoring a potential interplay between PTMs and metal ion binding in regulating α-synuclein physiological functions and its role in pathology.
Fil: González, Nazareno. Laboratorio Max Planck de Biología Estructural, Química y Biofísica Molecular de Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina
Fil: Arcos López, Trinidad. Center for Research and Advanced Studies; México
Fil: König, Annekatrin. University of Göttingen; Alemania
Fil: Quintanar, Liliana. Center for Research and Advanced Studies; México
Fil: Menacho Márquez, Mauricio Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina. Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario; Argentina
Fil: Outeiro, Tiago F.. University of Göttingen; Alemania. Max Planck Institute for Experimental Medicine; Alemania. University of Newcastle; Reino Unido
Fil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina. Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario; Argentina. Max Planck Institute for Biophysical Chemistry; Alemania - Materia
-
METAL IONS
NEURONS
PARKINSON DISEASE
POST-TRANSLATIONAL MODIFICATION
PROTEIN STRUCTURE
SYNUCLEIN - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/140148
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Effects of alpha-synuclein post-translational modifications on metal bindingGonzález, NazarenoArcos López, TrinidadKönig, AnnekatrinQuintanar, LilianaMenacho Márquez, Mauricio ArielOuteiro, Tiago F.Fernandez, Claudio OscarMETAL IONSNEURONSPARKINSON DISEASEPOST-TRANSLATIONAL MODIFICATIONPROTEIN STRUCTURESYNUCLEINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Parkinson’s disease is the second most common neurodegenerative disorder worldwide. Neurodegeneration in this pathology is characterized by the loss of dopaminergic neurons in the substantia nigra, coupled with cytoplasmic inclusions known as Lewy bodies containing α-synuclein. The brain is an organ that concentrates metal ions, and there is emerging evidence that a break-down in metal homeostasis may be a critical factor in a variety of neurodegenerative diseases. α-synuclein has emerged as an important metal-binding protein in the brain, whereas these interactions play an important role in its aggregation and might represent a link between protein aggregation, oxidative damage, and neuronal cell loss. Additionally, α-synuclein undergoes several post-translational modifications that regulate its structure and physiological function, and may be linked to the aggregation and/or oligomer formation. This review is focused on the interaction of this protein with physiologically relevant metal ions, highlighting the cases where metal-AS interactions profile as key modulators for its structural, aggregation, and membrane-binding properties. The impact of α-synuclein phosphorylation and N-terminal acetylation in the metal-binding properties of the protein are also discussed, underscoring a potential interplay between PTMs and metal ion binding in regulating α-synuclein physiological functions and its role in pathology.Fil: González, Nazareno. Laboratorio Max Planck de Biología Estructural, Química y Biofísica Molecular de Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; ArgentinaFil: Arcos López, Trinidad. Center for Research and Advanced Studies; MéxicoFil: König, Annekatrin. University of Göttingen; AlemaniaFil: Quintanar, Liliana. Center for Research and Advanced Studies; MéxicoFil: Menacho Márquez, Mauricio Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina. Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario; ArgentinaFil: Outeiro, Tiago F.. University of Göttingen; Alemania. Max Planck Institute for Experimental Medicine; Alemania. University of Newcastle; Reino UnidoFil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina. Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario; Argentina. Max Planck Institute for Biophysical Chemistry; AlemaniaWiley Blackwell Publishing, Inc2019-05-16info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/140148González, Nazareno; Arcos López, Trinidad; König, Annekatrin; Quintanar, Liliana; Menacho Márquez, Mauricio Ariel; et al.; Effects of alpha-synuclein post-translational modifications on metal binding; Wiley Blackwell Publishing, Inc; Journal of Neurochemistry; 150; 5; 16-5-2019; 507-5210022-3042CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/jnc.14721info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1111/jnc.14721info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:13:42Zoai:ri.conicet.gov.ar:11336/140148instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:13:42.44CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Effects of alpha-synuclein post-translational modifications on metal binding |
title |
Effects of alpha-synuclein post-translational modifications on metal binding |
spellingShingle |
Effects of alpha-synuclein post-translational modifications on metal binding González, Nazareno METAL IONS NEURONS PARKINSON DISEASE POST-TRANSLATIONAL MODIFICATION PROTEIN STRUCTURE SYNUCLEIN |
title_short |
Effects of alpha-synuclein post-translational modifications on metal binding |
title_full |
Effects of alpha-synuclein post-translational modifications on metal binding |
title_fullStr |
Effects of alpha-synuclein post-translational modifications on metal binding |
title_full_unstemmed |
Effects of alpha-synuclein post-translational modifications on metal binding |
title_sort |
Effects of alpha-synuclein post-translational modifications on metal binding |
dc.creator.none.fl_str_mv |
González, Nazareno Arcos López, Trinidad König, Annekatrin Quintanar, Liliana Menacho Márquez, Mauricio Ariel Outeiro, Tiago F. Fernandez, Claudio Oscar |
author |
González, Nazareno |
author_facet |
González, Nazareno Arcos López, Trinidad König, Annekatrin Quintanar, Liliana Menacho Márquez, Mauricio Ariel Outeiro, Tiago F. Fernandez, Claudio Oscar |
author_role |
author |
author2 |
Arcos López, Trinidad König, Annekatrin Quintanar, Liliana Menacho Márquez, Mauricio Ariel Outeiro, Tiago F. Fernandez, Claudio Oscar |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
METAL IONS NEURONS PARKINSON DISEASE POST-TRANSLATIONAL MODIFICATION PROTEIN STRUCTURE SYNUCLEIN |
topic |
METAL IONS NEURONS PARKINSON DISEASE POST-TRANSLATIONAL MODIFICATION PROTEIN STRUCTURE SYNUCLEIN |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Parkinson’s disease is the second most common neurodegenerative disorder worldwide. Neurodegeneration in this pathology is characterized by the loss of dopaminergic neurons in the substantia nigra, coupled with cytoplasmic inclusions known as Lewy bodies containing α-synuclein. The brain is an organ that concentrates metal ions, and there is emerging evidence that a break-down in metal homeostasis may be a critical factor in a variety of neurodegenerative diseases. α-synuclein has emerged as an important metal-binding protein in the brain, whereas these interactions play an important role in its aggregation and might represent a link between protein aggregation, oxidative damage, and neuronal cell loss. Additionally, α-synuclein undergoes several post-translational modifications that regulate its structure and physiological function, and may be linked to the aggregation and/or oligomer formation. This review is focused on the interaction of this protein with physiologically relevant metal ions, highlighting the cases where metal-AS interactions profile as key modulators for its structural, aggregation, and membrane-binding properties. The impact of α-synuclein phosphorylation and N-terminal acetylation in the metal-binding properties of the protein are also discussed, underscoring a potential interplay between PTMs and metal ion binding in regulating α-synuclein physiological functions and its role in pathology. Fil: González, Nazareno. Laboratorio Max Planck de Biología Estructural, Química y Biofísica Molecular de Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina Fil: Arcos López, Trinidad. Center for Research and Advanced Studies; México Fil: König, Annekatrin. University of Göttingen; Alemania Fil: Quintanar, Liliana. Center for Research and Advanced Studies; México Fil: Menacho Márquez, Mauricio Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina. Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario; Argentina Fil: Outeiro, Tiago F.. University of Göttingen; Alemania. Max Planck Institute for Experimental Medicine; Alemania. University of Newcastle; Reino Unido Fil: Fernandez, Claudio Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario. Universidad Nacional de Rosario. Instituto de Investigaciones para el Descubrimiento de Fármacos de Rosario; Argentina. Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario; Argentina. Max Planck Institute for Biophysical Chemistry; Alemania |
description |
Parkinson’s disease is the second most common neurodegenerative disorder worldwide. Neurodegeneration in this pathology is characterized by the loss of dopaminergic neurons in the substantia nigra, coupled with cytoplasmic inclusions known as Lewy bodies containing α-synuclein. The brain is an organ that concentrates metal ions, and there is emerging evidence that a break-down in metal homeostasis may be a critical factor in a variety of neurodegenerative diseases. α-synuclein has emerged as an important metal-binding protein in the brain, whereas these interactions play an important role in its aggregation and might represent a link between protein aggregation, oxidative damage, and neuronal cell loss. Additionally, α-synuclein undergoes several post-translational modifications that regulate its structure and physiological function, and may be linked to the aggregation and/or oligomer formation. This review is focused on the interaction of this protein with physiologically relevant metal ions, highlighting the cases where metal-AS interactions profile as key modulators for its structural, aggregation, and membrane-binding properties. The impact of α-synuclein phosphorylation and N-terminal acetylation in the metal-binding properties of the protein are also discussed, underscoring a potential interplay between PTMs and metal ion binding in regulating α-synuclein physiological functions and its role in pathology. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-05-16 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/140148 González, Nazareno; Arcos López, Trinidad; König, Annekatrin; Quintanar, Liliana; Menacho Márquez, Mauricio Ariel; et al.; Effects of alpha-synuclein post-translational modifications on metal binding; Wiley Blackwell Publishing, Inc; Journal of Neurochemistry; 150; 5; 16-5-2019; 507-521 0022-3042 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/140148 |
identifier_str_mv |
González, Nazareno; Arcos López, Trinidad; König, Annekatrin; Quintanar, Liliana; Menacho Márquez, Mauricio Ariel; et al.; Effects of alpha-synuclein post-translational modifications on metal binding; Wiley Blackwell Publishing, Inc; Journal of Neurochemistry; 150; 5; 16-5-2019; 507-521 0022-3042 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1111/jnc.14721 info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1111/jnc.14721 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
publisher.none.fl_str_mv |
Wiley Blackwell Publishing, Inc |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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