Current Understanding of RAD52 Functions: Fundamental and Therapeutic Insights

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...

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Main Authors: Vanesa Gottifredi, Lisa Wiesmüller
Format: Article
Language:English
Published: MDPI AG 2020-03-01
Series:Cancers
Subjects:
Online Access:https://www.mdpi.com/2072-6694/12/3/705
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author Vanesa Gottifredi
Lisa Wiesmüller
author_facet Vanesa Gottifredi
Lisa Wiesmüller
author_sort Vanesa Gottifredi
collection DOAJ
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.
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spelling doaj.art-5f7d0f0f0f5d4386a17c572bf8644e1a2023-09-02T14:23:32ZengMDPI AGCancers2072-66942020-03-0112370510.3390/cancers12030705cancers12030705Current Understanding of RAD52 Functions: Fundamental and Therapeutic InsightsVanesa Gottifredi0Lisa Wiesmüller1Fundación Instituto Leloir, IIBBA-Consejo Nacional de Investigaciones Científicas y Técnicas. Av. Patricias Argentinas 435, 1405 Buenos Aires, ArgentinaDivision of Gynecological Oncology, Department of Obstetrics and Gynecology of the University of Ulm Prittwitzstrasse 43, 89075 Ulm, GermanyIn 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.https://www.mdpi.com/2072-6694/12/3/705dna double-strand break repaircommon fragile sitestalled replication forktelomeresfork reversalr loopsnucleasesgenome integrity
spellingShingle Vanesa Gottifredi
Lisa Wiesmüller
Current Understanding of RAD52 Functions: Fundamental and Therapeutic Insights
Cancers
dna double-strand break repair
common fragile site
stalled replication fork
telomeres
fork reversal
r loops
nucleases
genome integrity
title 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_short Current Understanding of RAD52 Functions: Fundamental and Therapeutic Insights
title_sort current understanding of rad52 functions fundamental and therapeutic insights
topic dna double-strand break repair
common fragile site
stalled replication fork
telomeres
fork reversal
r loops
nucleases
genome integrity
url https://www.mdpi.com/2072-6694/12/3/705
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