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Heat shock proteins and DNA repair mechanisms: an updated overview
Mayra L Sottile1, Silvina B Nadin2
1Tumor Biology Laboratory, Institute of Medicine and Experimental Biology of Cuyo (IMBECU), National Scientific and Technical Research Council (CONICET), Av. Adrián Ruiz Leal s/n Parque Gral. San Martín, 5500, Mendoza, Argentina.
Abstract:
Heat shock proteins (HSPs), also known as molecular chaperones, participate in important cellular processes, such as protein aggregation, disaggregation, folding, and unfolding. HSPs have cytoprotective functions that are commonly explained by their antiapoptotic role. Their involvement in anticancer drug resistance has been the focus of intense research efforts, and the relationship between HSP induction and DNA repair mechanisms has been in the spotlight during the past decades. Because DNA is permanently subject to damage, many DNA repair pathways are involved in the recognition and removal of a diverse array of DNA lesions. Hence, DNA repair mechanisms are key to maintain genome stability. In addition, the interactome network of HSPs with DNA repair proteins has become an exciting research field and so their use as emerging targets for cancer therapy. This article provides a historical overview of the participation of HSPs in DNA repair mechanisms as part of their molecular chaperone capabilities.
Insights
Heat shock proteins (HSPs) are crucial molecular chaperones involved in protein maintenance and cellular protection. This review explores their role in DNA repair, highlighting their potential as cancer therapy targets.
Area of Science:
- Molecular Biology
- Cellular Biology
- Oncology
Background:
- Heat shock proteins (HSPs), or molecular chaperones, regulate critical cellular functions including protein folding and preventing aggregation.
- HSPs exhibit cytoprotective effects, primarily through their antiapoptotic activities.
- The role of HSPs in anticancer drug resistance and their connection to DNA repair mechanisms are areas of significant research interest.
Purpose of the Study:
- To provide a historical overview of the involvement of HSPs in DNA repair mechanisms.
- To explore the molecular chaperone capabilities of HSPs in the context of DNA repair.
- To highlight the potential of HSPs as therapeutic targets in cancer treatment.
Main Methods:
- Literature review and historical analysis of research on HSPs and DNA repair.
- Examination of the interactome network between HSPs and DNA repair proteins.
- Synthesis of findings on HSPs' role in maintaining genome stability.
Main Results:
- HSPs play a multifaceted role in cellular processes, including protein homeostasis and stress response.
- Evidence suggests a significant interplay between HSPs and various DNA repair pathways.
- The interaction network of HSPs with DNA repair proteins is a burgeoning field of study.
Conclusions:
- HSPs' molecular chaperone functions extend to supporting DNA repair mechanisms.
- The involvement of HSPs in DNA repair contributes to maintaining genome stability.
- HSPs represent promising emerging targets for novel cancer therapies due to their roles in DNA repair and drug resistance.
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