Heat shock proteins and DNA repair mechanisms: an updated overview

• Published in: Cell stress & chaperones Vol. 23; no. 3; pp. 303 - 315
• Main Authors: Sottile, Mayra L., Nadin, Silvina B.
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer 01.05.2018; Springer Netherlands; Springer Nature B.V
• Subjects: Animals; Bacterial proteins; Biochemistry; Biomedical and Life Sciences; Biomedicine; Cancer; Cancer Research; Cell Biology; Cell lines; Chaperones; Deoxyribonucleic acid; Disaggregation; DNA; DNA Damage; DNA mismatch repair; DNA Repair; Drug resistance; Gene expression; Genomes; Heat shock proteins; Heat-Shock Proteins - metabolism; HeLa cells; Humans; Immunology; Lesions; MINI REVIEW; Models, Biological; Neurosciences; Protein folding; Protein interaction; Proteins; Repair; Signal Transduction; Heat shock proteins; Molecular chaperones; DNA damage response; DNA repair
• ISSN: 1355-8145; 1466-1268; 1466-1268
• DOI: 10.1007/s12192-017-0843-4

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.