TY - JOUR
T1 - Barrier-to-autointegration factor 1 (Banf1) regulates poly [ADP-ribose] polymerase 1 (PARP1) activity following oxidative DNA damage
AU - Bolderson, Emma
AU - Burgess, Joshua T.
AU - Li, Jun
AU - Gandhi, Neha S.
AU - Boucher, Didier
AU - Croft, Laura V.
AU - Beard, Samuel
AU - Plowman, Jennifer J.
AU - Suraweera, Amila
AU - Adams, Mark N.
AU - Naqi, Ali
AU - Zhang, Shu Dong
AU - Sinclair, David A.
AU - O’Byrne, Kenneth J.
AU - Richard, Derek J.
PY - 2019/12/3
Y1 - 2019/12/3
N2 - The DNA repair capacity of human cells declines with age, in a process that is not clearly understood. Mutation of the nuclear envelope protein barrier-to-autointegration factor 1 (Banf1) has previously been shown to cause a human progeroid disorder, Néstor–Guillermo progeria syndrome (NGPS). The underlying links between Banf1, DNA repair and the ageing process are unknown. Here, we report that Banf1 controls the DNA damage response to oxidative stress via regulation of poly [ADP-ribose] polymerase 1 (PARP1). Specifically, oxidative lesions promote direct binding of Banf1 to PARP1, a critical NAD+-dependent DNA repair protein, leading to inhibition of PARP1 auto-ADP-ribosylation and defective repair of oxidative lesions, in cells with increased Banf1. Consistent with this, cells from patients with NGPS have defective PARP1 activity and impaired repair of oxidative lesions. These data support a model whereby Banf1 is crucial to reset oxidative-stress-induced PARP1 activity. Together, these data offer insight into Banf1-regulated, PARP1-directed repair of oxidative lesions.
AB - The DNA repair capacity of human cells declines with age, in a process that is not clearly understood. Mutation of the nuclear envelope protein barrier-to-autointegration factor 1 (Banf1) has previously been shown to cause a human progeroid disorder, Néstor–Guillermo progeria syndrome (NGPS). The underlying links between Banf1, DNA repair and the ageing process are unknown. Here, we report that Banf1 controls the DNA damage response to oxidative stress via regulation of poly [ADP-ribose] polymerase 1 (PARP1). Specifically, oxidative lesions promote direct binding of Banf1 to PARP1, a critical NAD+-dependent DNA repair protein, leading to inhibition of PARP1 auto-ADP-ribosylation and defective repair of oxidative lesions, in cells with increased Banf1. Consistent with this, cells from patients with NGPS have defective PARP1 activity and impaired repair of oxidative lesions. These data support a model whereby Banf1 is crucial to reset oxidative-stress-induced PARP1 activity. Together, these data offer insight into Banf1-regulated, PARP1-directed repair of oxidative lesions.
UR - https://pure.ulster.ac.uk/en/publications/barrier-to-autointegration-factor-1-banf1-regulates-poly-adp-ribo
UR - http://www.scopus.com/inward/record.url?scp=85075940827&partnerID=8YFLogxK
U2 - 10.1038/s41467-019-13167-5
DO - 10.1038/s41467-019-13167-5
M3 - Article
C2 - 31796734
AN - SCOPUS:85075940827
SN - 2041-1723
VL - 10
SP - 1
EP - 12
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 5501
ER -
