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- W2112639893 abstract "DNA damage triggers a complex signaling cascade involving a multitude of phosphorylation events. We found that the threonine 7 (Thr-7) residue of heat shock protein 90α (Hsp90α) was phosphorylated immediately after DNA damage. The phosphorylated Hsp90α then accumulated at sites of DNA double strand breaks and formed repair foci with slow kinetics, matching the repair kinetics of complex DNA damage. The phosphorylation of Hsp90α was dependent on phosphatidylinositol 3-kinase-like kinases, including the DNA-dependent protein kinase (DNA-PK) in particular. DNA-PK plays an essential role in the repair of DNA double strand breaks by nonhomologous end-joining and in the signaling of DNA damage. It is also present in the cytoplasm of the cell and has been suggested to play a role in cytoplasmic signaling pathways. Using stabilized double-stranded DNA molecules to activate DNA-PK, we showed that an active DNA-PK complex could be assembled in the cytoplasm, resulting in phosphorylation of the cytoplasmic pool of Hsp90α. In vivo, reverse phase protein array data for tumors revealed that basal levels of Thr-7-phosphorylated Hsp90α were correlated with phosphorylated histone H2AX levels. The Thr-7 phosphorylation of the ubiquitously produced and secreted Hsp90α may therefore serve as a surrogate biomarker of DNA damage. These findings shed light on the interplay between central DNA repair enzymes and an essential molecular chaperone." @default.
- W2112639893 created "2016-06-24" @default.
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- W2112639893 date "2012-03-01" @default.
- W2112639893 modified "2023-10-17" @default.
- W2112639893 title "Heat Shock Protein 90α (Hsp90α) Is Phosphorylated in Response to DNA Damage and Accumulates in Repair Foci" @default.
- W2112639893 cites W1493386189 @default.
- W2112639893 cites W1499226315 @default.
- W2112639893 cites W1596822567 @default.
- W2112639893 cites W191454705 @default.
- W2112639893 cites W1967630964 @default.
- W2112639893 cites W1969321347 @default.
- W2112639893 cites W1969888906 @default.
- W2112639893 cites W1979303367 @default.
- W2112639893 cites W1988173009 @default.
- W2112639893 cites W1989480741 @default.
- W2112639893 cites W1998959684 @default.
- W2112639893 cites W2001580102 @default.
- W2112639893 cites W2004726009 @default.
- W2112639893 cites W2007571492 @default.
- W2112639893 cites W2009746447 @default.
- W2112639893 cites W2011804883 @default.
- W2112639893 cites W2014342962 @default.
- W2112639893 cites W2015275751 @default.
- W2112639893 cites W2020151423 @default.
- W2112639893 cites W2022531767 @default.
- W2112639893 cites W2023078019 @default.
- W2112639893 cites W2025180762 @default.
- W2112639893 cites W2029065442 @default.
- W2112639893 cites W2032020572 @default.
- W2112639893 cites W2037108126 @default.
- W2112639893 cites W2039143648 @default.
- W2112639893 cites W2041400263 @default.
- W2112639893 cites W2043959346 @default.
- W2112639893 cites W2044204464 @default.
- W2112639893 cites W2046044279 @default.
- W2112639893 cites W2052701304 @default.
- W2112639893 cites W2055137027 @default.
- W2112639893 cites W2057574712 @default.
- W2112639893 cites W2059823430 @default.
- W2112639893 cites W2060902443 @default.
- W2112639893 cites W2069448508 @default.
- W2112639893 cites W2073067473 @default.
- W2112639893 cites W2077436902 @default.
- W2112639893 cites W2087790047 @default.
- W2112639893 cites W2091068450 @default.
- W2112639893 cites W2093298277 @default.
- W2112639893 cites W2096540333 @default.
- W2112639893 cites W2096753300 @default.
- W2112639893 cites W2096782300 @default.
- W2112639893 cites W2105488316 @default.
- W2112639893 cites W2106018842 @default.
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- W2112639893 cites W2107029023 @default.
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- W2112639893 cites W2136927373 @default.
- W2112639893 cites W2140886363 @default.
- W2112639893 cites W2145676287 @default.
- W2112639893 cites W2145812105 @default.
- W2112639893 cites W2150144069 @default.
- W2112639893 cites W2150634191 @default.
- W2112639893 cites W2152440925 @default.
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- W2112639893 doi "https://doi.org/10.1074/jbc.m111.320887" @default.
- W2112639893 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3308794" @default.
- W2112639893 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22270370" @default.
- W2112639893 hasPublicationYear "2012" @default.
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