Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors. / Alemasova, Elizaveta E.; Naumenko, Konstantin N.; Kurgina, Tatyana A. и др.
в: Oncotarget, Том 9, № 34, 01.05.2018, стр. 23349-23365.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors
AU - Alemasova, Elizaveta E.
AU - Naumenko, Konstantin N.
AU - Kurgina, Tatyana A.
AU - Anarbaev, Rashid O.
AU - Lavrik, Olga I.
N1 - Publisher Copyright: © Alemasova et al.
PY - 2018/5/1
Y1 - 2018/5/1
N2 - Y-box-binding protein 1 (YB-1) is a multifunctional cellular factor overexpressed in tumors resistant to chemotherapy. An intrinsically disordered structure together with a high positive charge peculiar to YB-1 allows this protein to function in almost all cellular events related to nucleic acids including RNA, DNA and poly(ADP-ribose) (PAR). In the present study we show that YB-1 acts as a potent poly(ADP-ribose) polymerase 1 (PARP1) cofactor that can reduce the efficiency of PARP1 inhibitors. Similarly to that of histones or polyamines, stimulatory effect of YB-1 on the activity of PARP1 was significantly higher than the activator potential of Mg2+ and was independent of the presence of EDTA. The C-terminal domain of YB-1 proved to be indispensable for PARP1 stimulation. We also found that functional interactions of YB-1 and PARP1 can be mediated and regulated by poly(ADP-ribose).
AB - Y-box-binding protein 1 (YB-1) is a multifunctional cellular factor overexpressed in tumors resistant to chemotherapy. An intrinsically disordered structure together with a high positive charge peculiar to YB-1 allows this protein to function in almost all cellular events related to nucleic acids including RNA, DNA and poly(ADP-ribose) (PAR). In the present study we show that YB-1 acts as a potent poly(ADP-ribose) polymerase 1 (PARP1) cofactor that can reduce the efficiency of PARP1 inhibitors. Similarly to that of histones or polyamines, stimulatory effect of YB-1 on the activity of PARP1 was significantly higher than the activator potential of Mg2+ and was independent of the presence of EDTA. The C-terminal domain of YB-1 proved to be indispensable for PARP1 stimulation. We also found that functional interactions of YB-1 and PARP1 can be mediated and regulated by poly(ADP-ribose).
KW - Olaparib
KW - PARP1 inhibitors
KW - Poly(ADP-ribose) (PAR)
KW - Poly(ADP-ribose) polymerase 1 (PARP1)
KW - Y-box binding protein 1 (YB-1)
UR - http://www.scopus.com/inward/record.url?scp=85046802922&partnerID=8YFLogxK
U2 - 10.18632/oncotarget.25158
DO - 10.18632/oncotarget.25158
M3 - Article
C2 - 29805738
AN - SCOPUS:85046802922
VL - 9
SP - 23349
EP - 23365
JO - Oncotarget
JF - Oncotarget
SN - 1949-2553
IS - 34
ER -
ID: 13360286