2026-04-19T14:09:04Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/2206082025-12-04T19:32:11Zcom_2072_1057col_2072_478908col_2072_478917

00925njm 22002777a 4500 dc Ulsamer, Arnau author Martínez Limón, Adrián author Bader, S author Rodríguez Acebes, Sara author Freire, Raimundo author Méndez, Juan author Nadal Clanchet, Eulàlia de author Posas, Francesc author 2025-04-25T09:23:57Z 2025-04-25T09:23:57Z 2022-09-20 2025-04-23T07:18:57Z Stress-activated protein kinases (SAPKs) enhance survival in response to environmental changes. In yeast, the Hog1 SAPK and Mrc1, a protein required for DNA replication, define a safeguard mechanism that allows eukaryotic cells to prevent genomic instability upon stress during S-phase. Here we show that, in mammals, the p38 SAPK and Claspin-the functional homolog of Mrc1-protect cells from DNA damage upon osmostress during S-phase. We demonstrate that p38 phosphorylates Claspin and either the mutation of the p38-phosphorylation sites in Claspin or p38 inhibition suppresses the protective role of Claspin on DNA damage. In addition, wild-type Claspin but not the p38-unphosphorylatable mutant has a protective effect on cell survival in response to cisplatin treatment. These findings reveal a role of Claspin in response to chemotherapeutic drugs. Thus, this pathway protects S-phase integrity from different insults and it is conserved from yeast to mammals. ADN Estrès (Fisiologia) Cicle cel·lular Cisplatí DNA Stress (Physiology) Cell cycle Cisplatin Regulation of Claspin by the p38 stress-activated protein kinase protects cells from DNA damage