Current understanding of RAD52 functions: Fundamental and therapeutic insights

Autores
Gottifredi, Vanesa; Wiesmüller, Lisa
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this Special Issue, we would like to focus on the various functions of the RAD52 helicase-like protein and the current implications of such findings for cancer treatment. Over the last few years, various laboratories have discovered particular activities of mammalian RAD52—both in S and M phase—that are distinct from the auxiliary role of yeast RAD52 in homologous recombination. At DNA double-strand breaks, RAD52 was demonstrated to spur alternative pathways to compensate for the loss of homologous recombination functions. At collapsed replication forks, RAD52 activates break-induced replication. In the M phase, RAD52 promotes the finalization of DNA replication. Its compensatory role in the resolution of DNA double-strand breaks has put RAD52 in the focus of synthetic lethal strategies, which is particularly relevant for cancer treatment.
Fil: Gottifredi, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Wiesmüller, Lisa. Universitat Ulm; Alemania
Materia
COMMON FRAGILE SITE
DNA DOUBLE-STRAND BREAK REPAIR
FORK REVERSAL
GENOME INTEGRITY
NUCLEASES
R LOOPS
STALLED REPLICATION FORK
TELOMERES
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:11336/139004
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/139004
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Current understanding of RAD52 functions: Fundamental and therapeutic insightsGottifredi, VanesaWiesmüller, LisaCOMMON FRAGILE SITEDNA DOUBLE-STRAND BREAK REPAIRFORK REVERSALGENOME INTEGRITYNUCLEASESR LOOPSSTALLED REPLICATION FORKTELOMEREShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In this Special Issue, we would like to focus on the various functions of the RAD52 helicase-like protein and the current implications of such findings for cancer treatment. Over the last few years, various laboratories have discovered particular activities of mammalian RAD52—both in S and M phase—that are distinct from the auxiliary role of yeast RAD52 in homologous recombination. At DNA double-strand breaks, RAD52 was demonstrated to spur alternative pathways to compensate for the loss of homologous recombination functions. At collapsed replication forks, RAD52 activates break-induced replication. In the M phase, RAD52 promotes the finalization of DNA replication. Its compensatory role in the resolution of DNA double-strand breaks has put RAD52 in the focus of synthetic lethal strategies, which is particularly relevant for cancer treatment.Fil: Gottifredi, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Wiesmüller, Lisa. Universitat Ulm; AlemaniaMolecular Diversity Preservation International2020-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/139004Gottifredi, Vanesa; Wiesmüller, Lisa; Current understanding of RAD52 functions: Fundamental and therapeutic insights; Molecular Diversity Preservation International; Cancers; 12; 3; 3-2020; 1-82072-66942072-6694CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2072-6694/12/3/705info:eu-repo/semantics/altIdentifier/doi/10.3390/cancers12030705info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:29:59Zoai:ri.conicet.gov.ar:11336/139004instacron: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 10:30:00.202CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Current understanding of RAD52 functions: Fundamental and therapeutic insights
title Current understanding of RAD52 functions: Fundamental and therapeutic insights
spellingShingle Current understanding of RAD52 functions: Fundamental and therapeutic insights
Gottifredi, Vanesa
COMMON FRAGILE SITE
DNA DOUBLE-STRAND BREAK REPAIR
FORK REVERSAL
GENOME INTEGRITY
NUCLEASES
R LOOPS
STALLED REPLICATION FORK
TELOMERES
title_short Current understanding of RAD52 functions: Fundamental and therapeutic insights
title_full Current understanding of RAD52 functions: Fundamental and therapeutic insights
title_fullStr Current understanding of RAD52 functions: Fundamental and therapeutic insights
title_full_unstemmed Current understanding of RAD52 functions: Fundamental and therapeutic insights
title_sort Current understanding of RAD52 functions: Fundamental and therapeutic insights
dc.creator.none.fl_str_mv Gottifredi, Vanesa
Wiesmüller, Lisa
author Gottifredi, Vanesa
author_facet Gottifredi, Vanesa
Wiesmüller, Lisa
author_role author
author2 Wiesmüller, Lisa
author2_role author
dc.subject.none.fl_str_mv COMMON FRAGILE SITE
DNA DOUBLE-STRAND BREAK REPAIR
FORK REVERSAL
GENOME INTEGRITY
NUCLEASES
R LOOPS
STALLED REPLICATION FORK
TELOMERES
topic COMMON FRAGILE SITE
DNA DOUBLE-STRAND BREAK REPAIR
FORK REVERSAL
GENOME INTEGRITY
NUCLEASES
R LOOPS
STALLED REPLICATION FORK
TELOMERES
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In this Special Issue, we would like to focus on the various functions of the RAD52 helicase-like protein and the current implications of such findings for cancer treatment. Over the last few years, various laboratories have discovered particular activities of mammalian RAD52—both in S and M phase—that are distinct from the auxiliary role of yeast RAD52 in homologous recombination. At DNA double-strand breaks, RAD52 was demonstrated to spur alternative pathways to compensate for the loss of homologous recombination functions. At collapsed replication forks, RAD52 activates break-induced replication. In the M phase, RAD52 promotes the finalization of DNA replication. Its compensatory role in the resolution of DNA double-strand breaks has put RAD52 in the focus of synthetic lethal strategies, which is particularly relevant for cancer treatment.
Fil: Gottifredi, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Wiesmüller, Lisa. Universitat Ulm; Alemania
description In this Special Issue, we would like to focus on the various functions of the RAD52 helicase-like protein and the current implications of such findings for cancer treatment. Over the last few years, various laboratories have discovered particular activities of mammalian RAD52—both in S and M phase—that are distinct from the auxiliary role of yeast RAD52 in homologous recombination. At DNA double-strand breaks, RAD52 was demonstrated to spur alternative pathways to compensate for the loss of homologous recombination functions. At collapsed replication forks, RAD52 activates break-induced replication. In the M phase, RAD52 promotes the finalization of DNA replication. Its compensatory role in the resolution of DNA double-strand breaks has put RAD52 in the focus of synthetic lethal strategies, which is particularly relevant for cancer treatment.
publishDate 2020
dc.date.none.fl_str_mv 2020-03
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/11336/139004
Gottifredi, Vanesa; Wiesmüller, Lisa; Current understanding of RAD52 functions: Fundamental and therapeutic insights; Molecular Diversity Preservation International; Cancers; 12; 3; 3-2020; 1-8
2072-6694
2072-6694
CONICET Digital
CONICET
url http://hdl.handle.net/11336/139004
identifier_str_mv Gottifredi, Vanesa; Wiesmüller, Lisa; Current understanding of RAD52 functions: Fundamental and therapeutic insights; Molecular Diversity Preservation International; Cancers; 12; 3; 3-2020; 1-8
2072-6694
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2072-6694/12/3/705
info:eu-repo/semantics/altIdentifier/doi/10.3390/cancers12030705
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 Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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
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score 13.070432

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