Premium
Chaperoning the DNA damage response
Author(s) -
Stracker Travis H.
Publication year - 2017
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14156
Subject(s) - dna damage , hsp90 , rad50 , dna , microbiology and biotechnology , dna repair , chaperone (clinical) , chemistry , biology , heat shock protein , dna binding protein , biochemistry , gene , medicine , transcription factor , pathology
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.