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- Publisher Website: 10.1038/s41419-019-1592-3
- Scopus: eid_2-s2.0-85065191555
- PMID: 31043584
- WOS: WOS:000468667300010
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Article: SIRT1 deacetylated and stabilized XRCC1 to promote chemoresistance in lung cancer
Title | SIRT1 deacetylated and stabilized XRCC1 to promote chemoresistance in lung cancer |
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Authors | |
Issue Date | 2019 |
Publisher | Nature Publishing Group: Open Access Journals. The Journal's web site is located at http://www.nature.com/cddis/index.html |
Citation | Cell Death & Disease, 2019, v. 10 n. 5, article no. 363 How to Cite? |
Abstract | Chemoresistance is one of the most important challenges in the clinical management of lung cancer. SIRT1 is a NAD dependent protein deacetylase and implicated in diverse cellular processes such as DNA damage repair, and cancer progression. SIRT1 is upregulated in chemoresistant lung cancer cells, genetic knockdown or chemical inhibition of SIRT1 reversed chemoresistance by enhancing DNA damage and apoptosis activation, accompanied with XRCC1 degradation. E3 ligase β-TrCP catalyzed the poly-ubiquitination of XRCC1 to promote its proteasome-dependent degradation. SIRT1 bound and deacetylated XRCC1 at lysine K260, K298 and K431, preventing it from β-TrCP-dependent ubiquitination. Mutations of these three lysine sites in XRCC1 abrogated the interaction with β-TrCP and prolonged the half-life of XRCC1 protein. Here, we describes SIRT1 confers chemoresistance to lung cancer cells by deacetylating and stabilizing XRCC1. Therefore, targeting SIRT1 might be a new strategy to manage the chemoresistance of lung cancer, and probably other cancers. |
Persistent Identifier | http://hdl.handle.net/10722/301406 |
ISSN | 2023 Impact Factor: 8.1 2023 SCImago Journal Rankings: 2.447 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Yousafzai, NA | - |
dc.contributor.author | Zhou, Q | - |
dc.contributor.author | Xu, W | - |
dc.contributor.author | Shi, Q | - |
dc.contributor.author | Xu, J | - |
dc.contributor.author | Feng, L | - |
dc.contributor.author | Chen, H | - |
dc.contributor.author | Shin, VY | - |
dc.contributor.author | Jin, H | - |
dc.contributor.author | Wang, X | - |
dc.date.accessioned | 2021-07-27T08:10:35Z | - |
dc.date.available | 2021-07-27T08:10:35Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | Cell Death & Disease, 2019, v. 10 n. 5, article no. 363 | - |
dc.identifier.issn | 2041-4889 | - |
dc.identifier.uri | http://hdl.handle.net/10722/301406 | - |
dc.description.abstract | Chemoresistance is one of the most important challenges in the clinical management of lung cancer. SIRT1 is a NAD dependent protein deacetylase and implicated in diverse cellular processes such as DNA damage repair, and cancer progression. SIRT1 is upregulated in chemoresistant lung cancer cells, genetic knockdown or chemical inhibition of SIRT1 reversed chemoresistance by enhancing DNA damage and apoptosis activation, accompanied with XRCC1 degradation. E3 ligase β-TrCP catalyzed the poly-ubiquitination of XRCC1 to promote its proteasome-dependent degradation. SIRT1 bound and deacetylated XRCC1 at lysine K260, K298 and K431, preventing it from β-TrCP-dependent ubiquitination. Mutations of these three lysine sites in XRCC1 abrogated the interaction with β-TrCP and prolonged the half-life of XRCC1 protein. Here, we describes SIRT1 confers chemoresistance to lung cancer cells by deacetylating and stabilizing XRCC1. Therefore, targeting SIRT1 might be a new strategy to manage the chemoresistance of lung cancer, and probably other cancers. | - |
dc.language | eng | - |
dc.publisher | Nature Publishing Group: Open Access Journals. The Journal's web site is located at http://www.nature.com/cddis/index.html | - |
dc.relation.ispartof | Cell Death & Disease | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.title | SIRT1 deacetylated and stabilized XRCC1 to promote chemoresistance in lung cancer | - |
dc.type | Article | - |
dc.identifier.email | Shin, VY: vyshin@hku.hk | - |
dc.identifier.authority | Shin, VY=rp02000 | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1038/s41419-019-1592-3 | - |
dc.identifier.pmid | 31043584 | - |
dc.identifier.pmcid | PMC6494911 | - |
dc.identifier.scopus | eid_2-s2.0-85065191555 | - |
dc.identifier.hkuros | 323789 | - |
dc.identifier.volume | 10 | - |
dc.identifier.issue | 5 | - |
dc.identifier.spage | article no. 363 | - |
dc.identifier.epage | article no. 363 | - |
dc.identifier.isi | WOS:000468667300010 | - |
dc.publisher.place | United Kingdom | - |