A quantitative 14-3-3 interaction screen connects the nuclear exosome targeting complex to the DNA damage response
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A quantitative 14-3-3 interaction screen connects the nuclear exosome targeting complex to the DNA damage response. / Blasius, Melanie; Wagner, Sebastian A; Choudhary, Chuna Ram; Bartek, Jiri; Jackson, Stephen P.
In: Genes & Development, Vol. 28, No. 18, 04.09.2014, p. 1977-1982.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - A quantitative 14-3-3 interaction screen connects the nuclear exosome targeting complex to the DNA damage response
AU - Blasius, Melanie
AU - Wagner, Sebastian A
AU - Choudhary, Chuna Ram
AU - Bartek, Jiri
AU - Jackson, Stephen P
N1 - © 2014 Blasius et al.; Published by Cold Spring Harbor Laboratory Press.
PY - 2014/9/4
Y1 - 2014/9/4
N2 - RNA metabolism is altered following DNA damage, but the underlying mechanisms are not well understood. Through a 14-3-3 interaction screen for DNA damage-induced protein interactions in human cells, we identified protein complexes connected to RNA biology. These include the nuclear exosome targeting (NEXT) complex that regulates turnover of noncoding RNAs termed promoter upstream transcripts (PROMPTs). We show that the NEXT subunit RBM7 is phosphorylated upon DNA damage by the MAPKAPK2 kinase and establish that this mediates 14-3-3 binding and decreases PROMPT binding. These findings and our observation that cells lacking RBM7 display DNA damage hypersensitivity link PROMPT turnover to the DNA damage response.
AB - RNA metabolism is altered following DNA damage, but the underlying mechanisms are not well understood. Through a 14-3-3 interaction screen for DNA damage-induced protein interactions in human cells, we identified protein complexes connected to RNA biology. These include the nuclear exosome targeting (NEXT) complex that regulates turnover of noncoding RNAs termed promoter upstream transcripts (PROMPTs). We show that the NEXT subunit RBM7 is phosphorylated upon DNA damage by the MAPKAPK2 kinase and establish that this mediates 14-3-3 binding and decreases PROMPT binding. These findings and our observation that cells lacking RBM7 display DNA damage hypersensitivity link PROMPT turnover to the DNA damage response.
U2 - 10.1101/gad.246272.114
DO - 10.1101/gad.246272.114
M3 - Journal article
C2 - 25189701
VL - 28
SP - 1977
EP - 1982
JO - Genes & Development
JF - Genes & Development
SN - 0890-9369
IS - 18
ER -
ID: 123734095