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FUS RRM regulates poly(ADP-ribose) levels after transcriptional arrest and PARP-1 activation on DNA damage. / Mamontova, Evgeniya M; Clément, Marie-Jeanne; Sukhanova, Maria V и др.

в: Cell Reports, Том 42, № 10, 113199, 31.10.2023.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

Harvard

Mamontova, EM, Clément, M-J, Sukhanova, MV, Joshi, V, Bouhss, A, Rengifo-Gonzalez, JC, Desforges, B, Hamon, L, Lavrik, OI & Pastré, D 2023, 'FUS RRM regulates poly(ADP-ribose) levels after transcriptional arrest and PARP-1 activation on DNA damage', Cell Reports, Том. 42, № 10, 113199. https://doi.org/10.1016/j.celrep.2023.113199

APA

Mamontova, E. M., Clément, M-J., Sukhanova, M. V., Joshi, V., Bouhss, A., Rengifo-Gonzalez, J. C., Desforges, B., Hamon, L., Lavrik, O. I., & Pastré, D. (2023). FUS RRM regulates poly(ADP-ribose) levels after transcriptional arrest and PARP-1 activation on DNA damage. Cell Reports, 42(10), [113199]. https://doi.org/10.1016/j.celrep.2023.113199

Vancouver

Mamontova EM, Clément M-J, Sukhanova MV, Joshi V, Bouhss A, Rengifo-Gonzalez JC и др. FUS RRM regulates poly(ADP-ribose) levels after transcriptional arrest and PARP-1 activation on DNA damage. Cell Reports. 2023 окт. 31;42(10):113199. Epub 2023 окт. 5. doi: 10.1016/j.celrep.2023.113199

Author

Mamontova, Evgeniya M ; Clément, Marie-Jeanne ; Sukhanova, Maria V и др. / FUS RRM regulates poly(ADP-ribose) levels after transcriptional arrest and PARP-1 activation on DNA damage. в: Cell Reports. 2023 ; Том 42, № 10.

BibTeX

@article{dea0c18494b04790ac7ffe07d16ed03e,
title = "FUS RRM regulates poly(ADP-ribose) levels after transcriptional arrest and PARP-1 activation on DNA damage",
abstract = "PARP-1 activation at DNA damage sites leads to the synthesis of long poly(ADP-ribose) (PAR) chains, which serve as a signal for DNA repair. Here we show that FUS, an RNA-binding protein, is specifically directed to PAR through its RNA recognition motif (RRM) to increase PAR synthesis by PARP-1 in HeLa cells after genotoxic stress. Using a structural approach, we also identify specific residues located in the FUS RRM, which can be PARylated by PARP-1 to control the level of PAR synthesis. Based on the results of this work, we propose a model in which, following a transcriptional arrest that releases FUS from nascent mRNA, FUS can be recruited by PARP-1 activated by DNA damage to stimulate PAR synthesis. We anticipate that this model offers new perspectives to understand the role of FET proteins in cancers and in certain neurodegenerative diseases such as amyotrophic lateral sclerosis.",
keywords = "ALS, CP: Molecular biology, DNA damage response, DNA repair, FUS/TLS, RNA, RNA-binding proteins, cancer, liquid-liquid phase separation, poly(ADP-ribose), poly(ADP-ribose) polymerase 1",
author = "Mamontova, {Evgeniya M} and Marie-Jeanne Cl{\'e}ment and Sukhanova, {Maria V} and Vandana Joshi and Ahmed Bouhss and Rengifo-Gonzalez, {Juan Carlos} and B{\'e}n{\'e}dicte Desforges and Loic Hamon and Lavrik, {Olga I} and David Pastr{\'e}",
note = "This work was supported in part by the Re´gion Ile-de-France (SESAME grant no. 15013102) and Genopole (SATURNE grant 2020). This study was supported by the Russian Science Foundation (RSF 22-14-00112 to O.I.L. and RSF 20-14-00086 to M.V.S.) and the International doctoral action (ADI2019) program of Paris-Saclay Universite´ (PhD grant to E.M.M.). The graphical abstract was created with BioRender.com Copyright {\textcopyright} 2023 The Authors. Published by Elsevier Inc. All rights reserved.",
year = "2023",
month = oct,
day = "31",
doi = "10.1016/j.celrep.2023.113199",
language = "English",
volume = "42",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "10",

}

RIS

TY - JOUR

T1 - FUS RRM regulates poly(ADP-ribose) levels after transcriptional arrest and PARP-1 activation on DNA damage

AU - Mamontova, Evgeniya M

AU - Clément, Marie-Jeanne

AU - Sukhanova, Maria V

AU - Joshi, Vandana

AU - Bouhss, Ahmed

AU - Rengifo-Gonzalez, Juan Carlos

AU - Desforges, Bénédicte

AU - Hamon, Loic

AU - Lavrik, Olga I

AU - Pastré, David

N1 - This work was supported in part by the Re´gion Ile-de-France (SESAME grant no. 15013102) and Genopole (SATURNE grant 2020). This study was supported by the Russian Science Foundation (RSF 22-14-00112 to O.I.L. and RSF 20-14-00086 to M.V.S.) and the International doctoral action (ADI2019) program of Paris-Saclay Universite´ (PhD grant to E.M.M.). The graphical abstract was created with BioRender.com Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.

PY - 2023/10/31

Y1 - 2023/10/31

N2 - PARP-1 activation at DNA damage sites leads to the synthesis of long poly(ADP-ribose) (PAR) chains, which serve as a signal for DNA repair. Here we show that FUS, an RNA-binding protein, is specifically directed to PAR through its RNA recognition motif (RRM) to increase PAR synthesis by PARP-1 in HeLa cells after genotoxic stress. Using a structural approach, we also identify specific residues located in the FUS RRM, which can be PARylated by PARP-1 to control the level of PAR synthesis. Based on the results of this work, we propose a model in which, following a transcriptional arrest that releases FUS from nascent mRNA, FUS can be recruited by PARP-1 activated by DNA damage to stimulate PAR synthesis. We anticipate that this model offers new perspectives to understand the role of FET proteins in cancers and in certain neurodegenerative diseases such as amyotrophic lateral sclerosis.

AB - PARP-1 activation at DNA damage sites leads to the synthesis of long poly(ADP-ribose) (PAR) chains, which serve as a signal for DNA repair. Here we show that FUS, an RNA-binding protein, is specifically directed to PAR through its RNA recognition motif (RRM) to increase PAR synthesis by PARP-1 in HeLa cells after genotoxic stress. Using a structural approach, we also identify specific residues located in the FUS RRM, which can be PARylated by PARP-1 to control the level of PAR synthesis. Based on the results of this work, we propose a model in which, following a transcriptional arrest that releases FUS from nascent mRNA, FUS can be recruited by PARP-1 activated by DNA damage to stimulate PAR synthesis. We anticipate that this model offers new perspectives to understand the role of FET proteins in cancers and in certain neurodegenerative diseases such as amyotrophic lateral sclerosis.

KW - ALS

KW - CP: Molecular biology

KW - DNA damage response

KW - DNA repair

KW - FUS/TLS

KW - RNA

KW - RNA-binding proteins

KW - cancer

KW - liquid-liquid phase separation

KW - poly(ADP-ribose)

KW - poly(ADP-ribose) polymerase 1

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85173685628&origin=inward&txGid=0a5d8648094c65f26f9626f53dbfc220

UR - https://www.mendeley.com/catalogue/223c3ca3-8c96-323e-967d-439fa79bdea4/

U2 - 10.1016/j.celrep.2023.113199

DO - 10.1016/j.celrep.2023.113199

M3 - Article

C2 - 37804508

VL - 42

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 10

M1 - 113199

ER -

ID: 55811135