TY - JOUR
T1 - E3 ligase RFWD3 participates in replication checkpoint control
AU - Gong, Zihua
AU - Chen, Junjie
PY - 2011/6/24
Y1 - 2011/6/24
N2 - RFWD3 has E3 ligase activity in vitro, but its in vivo function remains unknown. In this study we identified RFWD3 as a novel replication protein A (RPA)-associated protein. Using purified proteins, we observed a direct interaction between RPA2 and RFWD3. Further analysis showed that RFWD3 is recruited to stalled replication forks and co-localizes with RPA2 in response to replication stress. Moreover, RFWD3 is important for ATR-dependent Chk1 activation in response to replication stress. Upon replication stress, deletion of RPA2 binding region on RFWD3 impairs its localization to stalled replication forks and decreases Chk1 activation. Taken together, our results suggest that RFWD3 and RPA2 functionally interact and participate in replication checkpoint control.
AB - RFWD3 has E3 ligase activity in vitro, but its in vivo function remains unknown. In this study we identified RFWD3 as a novel replication protein A (RPA)-associated protein. Using purified proteins, we observed a direct interaction between RPA2 and RFWD3. Further analysis showed that RFWD3 is recruited to stalled replication forks and co-localizes with RPA2 in response to replication stress. Moreover, RFWD3 is important for ATR-dependent Chk1 activation in response to replication stress. Upon replication stress, deletion of RPA2 binding region on RFWD3 impairs its localization to stalled replication forks and decreases Chk1 activation. Taken together, our results suggest that RFWD3 and RPA2 functionally interact and participate in replication checkpoint control.
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U2 - 10.1074/jbc.M111.222869
DO - 10.1074/jbc.M111.222869
M3 - Article
C2 - 21504906
AN - SCOPUS:79959346617
SN - 0021-9258
VL - 286
SP - 22308
EP - 22313
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 25
ER -