Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications

Autores
Chelban, Viorica; Aksnes, Henriette; Maroofian, Reza; LaMonica, Lauren C.; Seabra, Luis; Siggervåg, Anette; Devic, Perrine; Shamseldin, Hanan E.; Vandrovcova, Jana; Murphy, David; Richard, Anne Claire; Quenez, Olivier; Bonnevalle, Antoine; Zanetti, Maria Natalia; Kaiyrzhanov, Rauan; Salpietro, Vincenzo; Efthymiou, Stephanie; Schottlaender, Lucia Valentina; Morsy, Heba; Scardamaglia, Annarita; Tariq, Ambreen; Pagnamenta, Alistair T.; Pennavaria, Ajia; Krogstad, Liv S.; Bekkelund, Åse K.; Crow, Yanick J.; Alkuraya, Fowzan S.; Nicolas, Gaël; Arnesen, Thomas; Houlden, Henry
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Primary familial brain calcification (PFBC) is characterized by calcium deposition in the brain, causing progressive movement disorders, psychiatric symptoms, and cognitive decline. PFBC is a heterogeneous disorder currently linked to variants in six different genes, but most patients remain genetically undiagnosed. Here, we identify biallelic NAA60 variants in ten individuals from seven families with autosomal recessive PFBC. The NAA60 variants lead to loss-of-function with lack of protein N-terminal (Nt)-acetylation activity. We show that the phosphate importer SLC20A2 is a substrate of NAA60 in vitro. In cells, loss of NAA60 caused reduced surface levels of SLC20A2 and a reduction in extracellular phosphate uptake. This study establishes NAA60 as a causal gene for PFBC, provides a possible biochemical explanation of its disease-causing mechanisms and underscores NAA60-mediated Nt-acetylation of transmembrane proteins as a fundamental process for healthy neurobiological functioning.
Fil: Chelban, Viorica. State University of Medicine and Pharmacy; Moldavia. University College London; Reino Unido
Fil: Aksnes, Henriette. University of Bergen; Noruega
Fil: Maroofian, Reza. University College London; Reino Unido
Fil: LaMonica, Lauren C.. University of Yale; Estados Unidos
Fil: Seabra, Luis. Université Paris Cité; Francia
Fil: Siggervåg, Anette. University of Bergen; Noruega
Fil: Devic, Perrine. Hospices Civils de Lyon; Francia
Fil: Shamseldin, Hanan E.. King Faisal Specialist Hospital and Research Center; Arabia Saudita
Fil: Vandrovcova, Jana. University College London; Reino Unido
Fil: Murphy, David. University College London; Reino Unido
Fil: Richard, Anne Claire. Université de Rouen-Normandie ; Francia
Fil: Quenez, Olivier. Université de Rouen-Normandie ; Francia
Fil: Bonnevalle, Antoine. Université de Rouen-Normandie ; Francia
Fil: Zanetti, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina. University College London; Reino Unido
Fil: Kaiyrzhanov, Rauan. University College London; Reino Unido
Fil: Salpietro, Vincenzo. University College London; Reino Unido
Fil: Efthymiou, Stephanie. University College London; Reino Unido
Fil: Schottlaender, Lucia Valentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina. University College London; Reino Unido
Fil: Morsy, Heba. University College London; Reino Unido. Alexandria University; Egipto
Fil: Scardamaglia, Annarita. University College London; Reino Unido
Fil: Tariq, Ambreen. University College London; Reino Unido
Fil: Pagnamenta, Alistair T.. University of Oxford. Wellcome Genome Campus. Centre for Genomic Pathogen Surveillance; Reino Unido
Fil: Pennavaria, Ajia. University of Bergen; Noruega
Fil: Krogstad, Liv S.. University of Bergen; Noruega
Fil: Bekkelund, Åse K.. University of Bergen; Noruega
Fil: Crow, Yanick J.. Université Paris Cité; Francia. University of Edinburgh; Reino Unido
Fil: Alkuraya, Fowzan S.. Alfaisal University; Arabia Saudita
Fil: Nicolas, Gaël. Université de Rouen Normandie; Francia
Fil: Arnesen, Thomas. University of Bergen; Noruega. Haukeland University Hospital; Noruega
Fil: Houlden, Henry. University College London Hospitals; Reino Unido
Materia
NAA60
Acetylation
Brain calcification
Movement disorders
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/276461

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spelling Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcificationsChelban, VioricaAksnes, HenrietteMaroofian, RezaLaMonica, Lauren C.Seabra, LuisSiggervåg, AnetteDevic, PerrineShamseldin, Hanan E.Vandrovcova, JanaMurphy, DavidRichard, Anne ClaireQuenez, OlivierBonnevalle, AntoineZanetti, Maria NataliaKaiyrzhanov, RauanSalpietro, VincenzoEfthymiou, StephanieSchottlaender, Lucia ValentinaMorsy, HebaScardamaglia, AnnaritaTariq, AmbreenPagnamenta, Alistair T.Pennavaria, AjiaKrogstad, Liv S.Bekkelund, Åse K.Crow, Yanick J.Alkuraya, Fowzan S.Nicolas, GaëlArnesen, ThomasHoulden, HenryNAA60AcetylationBrain calcificationMovement disordershttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Primary familial brain calcification (PFBC) is characterized by calcium deposition in the brain, causing progressive movement disorders, psychiatric symptoms, and cognitive decline. PFBC is a heterogeneous disorder currently linked to variants in six different genes, but most patients remain genetically undiagnosed. Here, we identify biallelic NAA60 variants in ten individuals from seven families with autosomal recessive PFBC. The NAA60 variants lead to loss-of-function with lack of protein N-terminal (Nt)-acetylation activity. We show that the phosphate importer SLC20A2 is a substrate of NAA60 in vitro. In cells, loss of NAA60 caused reduced surface levels of SLC20A2 and a reduction in extracellular phosphate uptake. This study establishes NAA60 as a causal gene for PFBC, provides a possible biochemical explanation of its disease-causing mechanisms and underscores NAA60-mediated Nt-acetylation of transmembrane proteins as a fundamental process for healthy neurobiological functioning.Fil: Chelban, Viorica. State University of Medicine and Pharmacy; Moldavia. University College London; Reino UnidoFil: Aksnes, Henriette. University of Bergen; NoruegaFil: Maroofian, Reza. University College London; Reino UnidoFil: LaMonica, Lauren C.. University of Yale; Estados UnidosFil: Seabra, Luis. Université Paris Cité; FranciaFil: Siggervåg, Anette. University of Bergen; NoruegaFil: Devic, Perrine. Hospices Civils de Lyon; FranciaFil: Shamseldin, Hanan E.. King Faisal Specialist Hospital and Research Center; Arabia SauditaFil: Vandrovcova, Jana. University College London; Reino UnidoFil: Murphy, David. University College London; Reino UnidoFil: Richard, Anne Claire. Université de Rouen-Normandie ; FranciaFil: Quenez, Olivier. Université de Rouen-Normandie ; FranciaFil: Bonnevalle, Antoine. Université de Rouen-Normandie ; FranciaFil: Zanetti, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina. University College London; Reino UnidoFil: Kaiyrzhanov, Rauan. University College London; Reino UnidoFil: Salpietro, Vincenzo. University College London; Reino UnidoFil: Efthymiou, Stephanie. University College London; Reino UnidoFil: Schottlaender, Lucia Valentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina. University College London; Reino UnidoFil: Morsy, Heba. University College London; Reino Unido. Alexandria University; EgiptoFil: Scardamaglia, Annarita. University College London; Reino UnidoFil: Tariq, Ambreen. University College London; Reino UnidoFil: Pagnamenta, Alistair T.. University of Oxford. Wellcome Genome Campus. Centre for Genomic Pathogen Surveillance; Reino UnidoFil: Pennavaria, Ajia. University of Bergen; NoruegaFil: Krogstad, Liv S.. University of Bergen; NoruegaFil: Bekkelund, Åse K.. University of Bergen; NoruegaFil: Crow, Yanick J.. Université Paris Cité; Francia. University of Edinburgh; Reino UnidoFil: Alkuraya, Fowzan S.. Alfaisal University; Arabia SauditaFil: Nicolas, Gaël. Université de Rouen Normandie; FranciaFil: Arnesen, Thomas. University of Bergen; Noruega. Haukeland University Hospital; NoruegaFil: Houlden, Henry. University College London Hospitals; Reino UnidoNature2024-03-13info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/276461Chelban, Viorica; Aksnes, Henriette; Maroofian, Reza; LaMonica, Lauren C.; Seabra, Luis; et al.; Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications; Nature; Nature Communications; 15; 1; 13-3-2024; 1-202041-1723CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41467-024-46354-0info:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-024-46354-0info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T13:33:15Zoai:ri.conicet.gov.ar:11336/276461instacron: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:34982025-12-23 13:33:15.654CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications
title Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications
spellingShingle Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications
Chelban, Viorica
NAA60
Acetylation
Brain calcification
Movement disorders
title_short Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications
title_full Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications
title_fullStr Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications
title_full_unstemmed Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications
title_sort Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications
dc.creator.none.fl_str_mv Chelban, Viorica
Aksnes, Henriette
Maroofian, Reza
LaMonica, Lauren C.
Seabra, Luis
Siggervåg, Anette
Devic, Perrine
Shamseldin, Hanan E.
Vandrovcova, Jana
Murphy, David
Richard, Anne Claire
Quenez, Olivier
Bonnevalle, Antoine
Zanetti, Maria Natalia
Kaiyrzhanov, Rauan
Salpietro, Vincenzo
Efthymiou, Stephanie
Schottlaender, Lucia Valentina
Morsy, Heba
Scardamaglia, Annarita
Tariq, Ambreen
Pagnamenta, Alistair T.
Pennavaria, Ajia
Krogstad, Liv S.
Bekkelund, Åse K.
Crow, Yanick J.
Alkuraya, Fowzan S.
Nicolas, Gaël
Arnesen, Thomas
Houlden, Henry
author Chelban, Viorica
author_facet Chelban, Viorica
Aksnes, Henriette
Maroofian, Reza
LaMonica, Lauren C.
Seabra, Luis
Siggervåg, Anette
Devic, Perrine
Shamseldin, Hanan E.
Vandrovcova, Jana
Murphy, David
Richard, Anne Claire
Quenez, Olivier
Bonnevalle, Antoine
Zanetti, Maria Natalia
Kaiyrzhanov, Rauan
Salpietro, Vincenzo
Efthymiou, Stephanie
Schottlaender, Lucia Valentina
Morsy, Heba
Scardamaglia, Annarita
Tariq, Ambreen
Pagnamenta, Alistair T.
Pennavaria, Ajia
Krogstad, Liv S.
Bekkelund, Åse K.
Crow, Yanick J.
Alkuraya, Fowzan S.
Nicolas, Gaël
Arnesen, Thomas
Houlden, Henry
author_role author
author2 Aksnes, Henriette
Maroofian, Reza
LaMonica, Lauren C.
Seabra, Luis
Siggervåg, Anette
Devic, Perrine
Shamseldin, Hanan E.
Vandrovcova, Jana
Murphy, David
Richard, Anne Claire
Quenez, Olivier
Bonnevalle, Antoine
Zanetti, Maria Natalia
Kaiyrzhanov, Rauan
Salpietro, Vincenzo
Efthymiou, Stephanie
Schottlaender, Lucia Valentina
Morsy, Heba
Scardamaglia, Annarita
Tariq, Ambreen
Pagnamenta, Alistair T.
Pennavaria, Ajia
Krogstad, Liv S.
Bekkelund, Åse K.
Crow, Yanick J.
Alkuraya, Fowzan S.
Nicolas, Gaël
Arnesen, Thomas
Houlden, Henry
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv NAA60
Acetylation
Brain calcification
Movement disorders
topic NAA60
Acetylation
Brain calcification
Movement disorders
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Primary familial brain calcification (PFBC) is characterized by calcium deposition in the brain, causing progressive movement disorders, psychiatric symptoms, and cognitive decline. PFBC is a heterogeneous disorder currently linked to variants in six different genes, but most patients remain genetically undiagnosed. Here, we identify biallelic NAA60 variants in ten individuals from seven families with autosomal recessive PFBC. The NAA60 variants lead to loss-of-function with lack of protein N-terminal (Nt)-acetylation activity. We show that the phosphate importer SLC20A2 is a substrate of NAA60 in vitro. In cells, loss of NAA60 caused reduced surface levels of SLC20A2 and a reduction in extracellular phosphate uptake. This study establishes NAA60 as a causal gene for PFBC, provides a possible biochemical explanation of its disease-causing mechanisms and underscores NAA60-mediated Nt-acetylation of transmembrane proteins as a fundamental process for healthy neurobiological functioning.
Fil: Chelban, Viorica. State University of Medicine and Pharmacy; Moldavia. University College London; Reino Unido
Fil: Aksnes, Henriette. University of Bergen; Noruega
Fil: Maroofian, Reza. University College London; Reino Unido
Fil: LaMonica, Lauren C.. University of Yale; Estados Unidos
Fil: Seabra, Luis. Université Paris Cité; Francia
Fil: Siggervåg, Anette. University of Bergen; Noruega
Fil: Devic, Perrine. Hospices Civils de Lyon; Francia
Fil: Shamseldin, Hanan E.. King Faisal Specialist Hospital and Research Center; Arabia Saudita
Fil: Vandrovcova, Jana. University College London; Reino Unido
Fil: Murphy, David. University College London; Reino Unido
Fil: Richard, Anne Claire. Université de Rouen-Normandie ; Francia
Fil: Quenez, Olivier. Université de Rouen-Normandie ; Francia
Fil: Bonnevalle, Antoine. Université de Rouen-Normandie ; Francia
Fil: Zanetti, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina. University College London; Reino Unido
Fil: Kaiyrzhanov, Rauan. University College London; Reino Unido
Fil: Salpietro, Vincenzo. University College London; Reino Unido
Fil: Efthymiou, Stephanie. University College London; Reino Unido
Fil: Schottlaender, Lucia Valentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina. University College London; Reino Unido
Fil: Morsy, Heba. University College London; Reino Unido. Alexandria University; Egipto
Fil: Scardamaglia, Annarita. University College London; Reino Unido
Fil: Tariq, Ambreen. University College London; Reino Unido
Fil: Pagnamenta, Alistair T.. University of Oxford. Wellcome Genome Campus. Centre for Genomic Pathogen Surveillance; Reino Unido
Fil: Pennavaria, Ajia. University of Bergen; Noruega
Fil: Krogstad, Liv S.. University of Bergen; Noruega
Fil: Bekkelund, Åse K.. University of Bergen; Noruega
Fil: Crow, Yanick J.. Université Paris Cité; Francia. University of Edinburgh; Reino Unido
Fil: Alkuraya, Fowzan S.. Alfaisal University; Arabia Saudita
Fil: Nicolas, Gaël. Université de Rouen Normandie; Francia
Fil: Arnesen, Thomas. University of Bergen; Noruega. Haukeland University Hospital; Noruega
Fil: Houlden, Henry. University College London Hospitals; Reino Unido
description Primary familial brain calcification (PFBC) is characterized by calcium deposition in the brain, causing progressive movement disorders, psychiatric symptoms, and cognitive decline. PFBC is a heterogeneous disorder currently linked to variants in six different genes, but most patients remain genetically undiagnosed. Here, we identify biallelic NAA60 variants in ten individuals from seven families with autosomal recessive PFBC. The NAA60 variants lead to loss-of-function with lack of protein N-terminal (Nt)-acetylation activity. We show that the phosphate importer SLC20A2 is a substrate of NAA60 in vitro. In cells, loss of NAA60 caused reduced surface levels of SLC20A2 and a reduction in extracellular phosphate uptake. This study establishes NAA60 as a causal gene for PFBC, provides a possible biochemical explanation of its disease-causing mechanisms and underscores NAA60-mediated Nt-acetylation of transmembrane proteins as a fundamental process for healthy neurobiological functioning.
publishDate 2024
dc.date.none.fl_str_mv 2024-03-13
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/11336/276461
Chelban, Viorica; Aksnes, Henriette; Maroofian, Reza; LaMonica, Lauren C.; Seabra, Luis; et al.; Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications; Nature; Nature Communications; 15; 1; 13-3-2024; 1-20
2041-1723
CONICET Digital
CONICET
url http://hdl.handle.net/11336/276461
identifier_str_mv Chelban, Viorica; Aksnes, Henriette; Maroofian, Reza; LaMonica, Lauren C.; Seabra, Luis; et al.; Biallelic NAA60 variants with impaired N-terminal acetylation capacity cause autosomal recessive primary familial brain calcifications; Nature; Nature Communications; 15; 1; 13-3-2024; 1-20
2041-1723
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-024-46354-0
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dc.publisher.none.fl_str_mv Nature
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