Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c

17 pags., 9 figs., 1 tab.

Detalles Bibliográficos
Autores: Rivero-Rodríguez, Francisco, Díaz-Quintana, Antonio, Velázquez-Cruz, Alejandro, González-Arzola, Katiuska, Gavilán, María P., Velázquez-Campoy, Adrián, Ríos, Rosa M., Rosa, Miguel A. de la, Díaz-Moreno, Irene
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/256135
Acceso en línea:http://hdl.handle.net/10261/256135
Access Level:acceso abierto
Palabra clave:Cytochrome c
Histone chaperone
Nuclear magnetic resonance
Molecular dynamics
Protein-protein interactions
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spelling Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome cRivero-Rodríguez, FranciscoDíaz-Quintana, AntonioVelázquez-Cruz, AlejandroGonzález-Arzola, KatiuskaGavilán, María P.Velázquez-Campoy, AdriánRíos, Rosa M.Rosa, Miguel A. de laDíaz-Moreno, IreneCytochrome cHistone chaperoneNuclear magnetic resonanceMolecular dynamicsProtein-protein interactions17 pags., 9 figs., 1 tab.Repair of injured DNA relies on nucleosome dismantling by histone chaperones and de-phosphorylation events carried out by Protein Phosphatase 2A (PP2A). Typical histone chaperones are the Acidic leucine-rich Nuclear Phosphoprotein 32 family (ANP32) members, e.g. ANP32A, which is also a well-known PP2A inhibitor (a.k.a. IPP2A). Here we report the novel interaction between the endogenous family member B—so-called ANP32B—and endogenous cytochrome c in cells undergoing camptothecin-induced DNA damage. Soon after DNA lesions but prior to caspase cascade activation, the hemeprotein translocates to the nucleus to target the Low Complexity Acidic Region (LCAR) of ANP32B; in a similar way, our group recently reported that the hemeprotein targets the acidic domain of SET/Template Activating Factor-Iβ (SET/TAF-Iβ), which is another histone chaperone and PP2A inhibitor (a.k.a. IPP2A). The nucleosome assembly activity of ANP32B is indeed unaffected by cytochrome c binding. Like ANP32A, ANP32B inhibits PP2A activity and is thus herein referred to as IPP2A. Our data demonstrates that ANP32B-dependent inhibition of PP2A is regulated by respiratory cytochrome c, which induces long-distance allosteric changes in the structured N-terminal domain of ANP32B upon binding to the C-terminal LCAR. In agreement with the reported role of PP2A in the DNA damage response, we propose a model wherein cytochrome c is translocated from the mitochondria into the nucleus upon DNA damage to modulate PP2A activity via its interaction with ANP32B.This work was supported by the Spanish Ministry of Science, Innovation and Universities (BFU2012-31670, BFU2015-71017, PGC2018-096049- BI00), Spanish Ministry of Education and Professional Training (FPU013/04373 to FRR, FPU016/01513 to AVC), Regional Government of Andalusia (BIO198, US-1254317 US/JUNTA/FEDER,UE, US- 1257019 US/JUNTA/FEDER,UE, P18-FR-3487 and P18–HO-4091), Ramon Areces Foundation, Biointeractomics Platform (cicCartuja, Seville) and the Microscopy and NMR Services at CITIUS (University of Seville). MPG is funded by a postdoctoral grant from the Spanish Association Against Cancer Scientific Foundation (FC AECC)ElsevierMinisterio de Ciencia, Innovación y Universidades (España)Junta de AndalucíaFundación Ramón ArecesUniversidad de SevillaConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2021202120212021info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/256135reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MEC//DCT2006-0675 %2F 31670info:eu-repo/grantAgreement/MINECO//BFU2015-71017-Pinfo:eu-repo/grantAgreement/MICIU//PGC2018-096049- BI00http://dx.doi.org/10.1016/j.redox.2021.101967Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2561352026-05-22T06:33:51Z
dc.title.none.fl_str_mv Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
title Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
spellingShingle Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
Rivero-Rodríguez, Francisco
Cytochrome c
Histone chaperone
Nuclear magnetic resonance
Molecular dynamics
Protein-protein interactions
title_short Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
title_full Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
title_fullStr Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
title_full_unstemmed Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
title_sort Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c
dc.creator.none.fl_str_mv Rivero-Rodríguez, Francisco
Díaz-Quintana, Antonio
Velázquez-Cruz, Alejandro
González-Arzola, Katiuska
Gavilán, María P.
Velázquez-Campoy, Adrián
Ríos, Rosa M.
Rosa, Miguel A. de la
Díaz-Moreno, Irene
author Rivero-Rodríguez, Francisco
author_facet Rivero-Rodríguez, Francisco
Díaz-Quintana, Antonio
Velázquez-Cruz, Alejandro
González-Arzola, Katiuska
Gavilán, María P.
Velázquez-Campoy, Adrián
Ríos, Rosa M.
Rosa, Miguel A. de la
Díaz-Moreno, Irene
author_role author
author2 Díaz-Quintana, Antonio
Velázquez-Cruz, Alejandro
González-Arzola, Katiuska
Gavilán, María P.
Velázquez-Campoy, Adrián
Ríos, Rosa M.
Rosa, Miguel A. de la
Díaz-Moreno, Irene
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
Junta de Andalucía
Fundación Ramón Areces
Universidad de Sevilla
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Cytochrome c
Histone chaperone
Nuclear magnetic resonance
Molecular dynamics
Protein-protein interactions
topic Cytochrome c
Histone chaperone
Nuclear magnetic resonance
Molecular dynamics
Protein-protein interactions
description 17 pags., 9 figs., 1 tab.
publishDate 2021
dc.date.none.fl_str_mv 2021
2021
2021
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/256135
url http://hdl.handle.net/10261/256135
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MEC//DCT2006-0675 %2F 31670
info:eu-repo/grantAgreement/MINECO//BFU2015-71017-P
info:eu-repo/grantAgreement/MICIU//PGC2018-096049- BI00
http://dx.doi.org/10.1016/j.redox.2021.101967
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.812429

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