Chaperoning the DNA damage response

Travis H Stracker

doi:10.1111/febs.14156

Chaperoning the DNA damage response

FEBS J. 2017 Aug;284(15):2375-2377. doi: 10.1111/febs.14156.

Author

Travis H Stracker¹

Affiliation

¹ Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Spain.

PMID: 28782203
DOI: 10.1111/febs.14156

Abstract

The NBN component of the MRE11-RAD50-NBN (MRN) complex and the ATM kinase have been identified as clients of the HSP90α chaperone. Inhibition of HSP90 leads to reduced stability of NBN and ATM and an impaired DNA damage response. These results identify new regulatory details of the DNA damage response and further explain the chemosensitizing effects of HSP90 inhibitors.

Publication types

Comment

MeSH terms

Ataxia Telangiectasia Mutated Proteins / genetics
Cell Cycle Proteins / genetics*
DNA Damage
DNA Repair
DNA Repair Enzymes / genetics*
DNA-Binding Proteins / genetics
Humans
Nuclear Proteins / genetics
Protein Serine-Threonine Kinases / genetics
Tumor Suppressor Proteins / genetics

Substances

Cell Cycle Proteins
DNA-Binding Proteins
Nuclear Proteins
Tumor Suppressor Proteins
Ataxia Telangiectasia Mutated Proteins
Protein Serine-Threonine Kinases
DNA Repair Enzymes