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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/140148
Acceder
id CONICETDig_7a6c7658dc670d6d9c6aece249ba4b5c
oai_identifier_str oai:ri.conicet.gov.ar:11336/140148
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T11:43:37Zoai: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:34982025-10-22 11:43:38.175CONICET 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/
eu_rights_str_mv 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
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846782128768942080
score 12.982451

Publicaciones similares