Heat shock proteins and DNA repair mechanisms: an updated overview

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 anticance...

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Veröffentlicht in:Cell Stress & Chaperones. - Elsevier. - 23(2018), 3, Seite 303-315
1. Verfasser: Sottile, Mayra L. (VerfasserIn)
Weitere Verfasser: Nadin, Silvina B.
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:Cell Stress & Chaperones
Schlagworte:Physical sciences Biological sciences Health sciences
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520 |a 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. 
540 |a © Cell Stress Society International 2018 
650 4 |a Physical sciences  |x Chemistry  |x Chemical compounds  |x Chemicals  |x Polymers  |x Biopolymers  |x Proteins  |x Heat shock proteins 
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