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Cell Stress and Chaperones

, Volume 23, Issue 3, pp 303–315 | Cite as

Heat shock proteins and DNA repair mechanisms: an updated overview

  • Mayra L. Sottile
  • Silvina B. Nadin
Mini Review

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.

Keywords

Heat shock proteins DNA repair DNA damage response Molecular chaperones 

Notes

Compliance with ethical standards

Financial & competing interest disclosure

This review was supported by grants from Alberto J. Roemmers Foundation (Dr. SB Nadin) and the National Agency for Scientific and Technological Promotion of Argentina (PICT 2015-1171, Préstamo BID, Dr. SB Nadin). The authors have no financial interest in or financial conflict with the subject matter or materials discussed in the manuscript.

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© Cell Stress Society International 2017

Authors and Affiliations

  1. 1.Tumor Biology Laboratory, Institute of Medicine and Experimental Biology of Cuyo (IMBECU)National Scientific and Technical Research Council (CONICET)MendozaArgentina

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