4.7 Article

SerpinB10, a Serine Protease Inhibitor, Is Implicated in UV-Induced Cellular Response

期刊

出版社

MDPI
DOI: 10.3390/ijms22168500

关键词

SerpinB10; Bomapin; serine protease inhibitor; replication; replication stress; UV damage

资金

  1. National Research, Development and Innovation Office [GINOP-2.2.1-15-2017-00052, GINOP-2.3.2-15-2016-00024, GINOP-2.3.2-15-2016-00026, NKFI-FK 132080]
  2. Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences [BO/27/20, uNKP-20-5-SZTE-265]
  3. EMBO short-term fellowship [8513]
  4. European Union [739593]
  5. [NTP-NFTo-20-B-400]

向作者/读者索取更多资源

UV-induced DNA damage response and repair processes are extensively studied, with SPB10 identified as a significantly upregulated gene following UV irradiation. While SPB10 is involved in the cellular response to UV-induced stress, it does not have an essential function in cell survival, but may play a role in delaying DNA repair in certain cell phases.
UV-induced DNA damage response and repair are extensively studied processes, as any malfunction in these pathways contributes to the activation of tumorigenesis. Although several proteins involved in these cellular mechanisms have been described, the entire repair cascade has remained unexplored. To identify new players in UV-induced repair, we performed a microarray screen, in which we found SerpinB10 (SPB10, Bomapin) as one of the most dramatically upregulated genes following UV irradiation. Here, we demonstrated that an increased mRNA level of SPB10 is a general cellular response following UV irradiation regardless of the cell type. We showed that although SPB10 is implicated in the UV-induced cellular response, it has no indispensable function in cell survival upon UV irradiation. Nonetheless, we revealed that SPB10 might be involved in delaying the duration of DNA repair in interphase and also in S-phase cells. Additionally, we also highlighted the interaction between SPB10 and H3. Based on our results, it seems that SPB10 protein is implicated in UV-induced stress as a quality control protein, presumably by slowing down the repair process.

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