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The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors. / Alemasova, Elizaveta E.; Naumenko, Konstantin N.; Kurgina, Tatyana A. et al.

In: Oncotarget, Vol. 9, No. 34, 01.05.2018, p. 23349-23365.

Research output: Contribution to journal › Article › peer-review

Harvard

Alemasova, EE, Naumenko, KN, Kurgina, TA, Anarbaev, RO & Lavrik, OI 2018, 'The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors', Oncotarget, vol. 9, no. 34, pp. 23349-23365. https://doi.org/10.18632/oncotarget.25158

APA

Alemasova, E. E., Naumenko, K. N., Kurgina, T. A., Anarbaev, R. O., & Lavrik, O. I. (2018). The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors. Oncotarget, 9(34), 23349-23365. https://doi.org/10.18632/oncotarget.25158

Vancouver

Alemasova EE, Naumenko KN, Kurgina TA, Anarbaev RO, Lavrik OI. The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors. Oncotarget. 2018 May 1;9(34):23349-23365. doi: 10.18632/oncotarget.25158

Author

Alemasova, Elizaveta E. ; Naumenko, Konstantin N. ; Kurgina, Tatyana A. et al. / The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors. In: Oncotarget. 2018 ; Vol. 9, No. 34. pp. 23349-23365.

BibTeX

@article{80be6fbed84449f9976adcb138315dc5,
title = "The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors",
abstract = "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).",
keywords = "Olaparib, PARP1 inhibitors, Poly(ADP-ribose) (PAR), Poly(ADP-ribose) polymerase 1 (PARP1), Y-box binding protein 1 (YB-1)",
author = "Alemasova, {Elizaveta E.} and Naumenko, {Konstantin N.} and Kurgina, {Tatyana A.} and Anarbaev, {Rashid O.} and Lavrik, {Olga I.}",
note = "Publisher Copyright: {\textcopyright} Alemasova et al.",
year = "2018",
month = may,
day = "1",
doi = "10.18632/oncotarget.25158",
language = "English",
volume = "9",
pages = "23349--23365",
journal = "Oncotarget",
issn = "1949-2553",
publisher = "Impact Journals LLC",
number = "34",

}

RIS

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