scholarly journals The RNA-binding Protein Fused in Sarcoma (FUS) Functions Downstream of Poly(ADP-ribose) Polymerase (PARP) in Response to DNA Damage

2013 ◽  
Vol 288 (34) ◽  
pp. 24731-24741 ◽  
Author(s):  
Adam S. Mastrocola ◽  
Sang Hwa Kim ◽  
Anthony T. Trinh ◽  
Lance A. Rodenkirch ◽  
Randal S. Tibbetts
Keyword(s):  
Dna Damage ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Fused In Sarcoma

scholarly journals PARP-1–dependent recruitment of cold-inducible RNA-binding protein promotes double-strand break repair and genome stability

2018 ◽  
Vol 115 (8) ◽  
pp. E1759-E1768 ◽  
Author(s):  
Jung-Kuei Chen ◽  
Wen-Ling Lin ◽  
Zhang Chen ◽  
Hung-wen Liu
Keyword(s):  
Dna Damage ◽  
Genome Stability ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Strand Break ◽  
Double Strand Break ◽  
Dsb Repair ◽  
Active Involvement ◽  
Parp 1

Maintenance of genome integrity is critical for both faithful propagation of genetic information and prevention of mutagenesis induced by various DNA damage events. Here we report cold-inducible RNA-binding protein (CIRBP) as a newly identified key regulator in DNA double-strand break (DSB) repair. On DNA damage, CIRBP temporarily accumulates at the damaged regions and is poly(ADP ribosyl)ated by poly(ADP ribose) polymerase-1 (PARP-1). Its dissociation from the sites of damage may depend on its phosphorylation status as mediated by phosphatidylinositol 3-kinase-related kinases. In the absence of CIRBP, cells showed reduced γH2AX, Rad51, and 53BP1 foci formation. Moreover, CIRBP-depleted cells exhibited impaired homologous recombination, impaired nonhomologous end-joining, increased micronuclei formation, and higher sensitivity to gamma irradiation, demonstrating the active involvement of CIRBP in DSB repair. Furthermore, CIRBP depleted cells exhibited defects in DNA damage-induced chromatin association of the MRN complex (Mre11, Rad50, and NBS1) and ATM kinase. CIRBP depletion also reduced phosphorylation of a variety of ATM substrate proteins and thus impaired the DNA damage response. Taken together, these results reveal a previously unrecognized role for CIRBP in DSB repair.

Fused in sarcoma/translocated in liposarcoma: A multifunctional DNA/RNA binding protein

2010 ◽  
Vol 42 (9) ◽  
pp. 1408-1411 ◽  
Author(s):  
Shu Yang ◽  
Sadaf T. Warraich ◽  
Garth A. Nicholson ◽  
Ian P. Blair
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Fused In Sarcoma

Abstract A18: HuR, an RNA binding protein, is critical for the DNA damage response in pancreatic cancer cells.

2012 ◽  
Author(s):  
Shruti Lal ◽  
Vikram Bhattacharjee ◽  
Timothy Yen ◽  
Richard A. Burkhart ◽  
Danielle M. Pineda ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Dna Damage ◽  
Cancer Cells ◽  
Dna Damage Response ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Pancreatic Cancer Cells ◽  
Damage Response

scholarly journals PARP activation regulates the RNA-binding protein NONO in the DNA damage response to DNA double-strand breaks

2012 ◽  
Vol 40 (20) ◽  
pp. 10287-10301 ◽  
Author(s):  
Jana Krietsch ◽  
Marie-Christine Caron ◽  
Jean-Philippe Gagné ◽  
Chantal Ethier ◽  
Julien Vignard ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Response ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Double Strand Breaks ◽  
Dna Double Strand Breaks ◽  
Parp Activation ◽  
Strand Breaks ◽  
Damage Response

scholarly journals The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β cores

2021 ◽  
Vol 118 (42) ◽  
pp. e2114412118
Author(s):  
Masato Kato ◽  
Steven L. McKnight
Keyword(s):  
Phase Separation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Low Complexity ◽  
Terminal Region ◽  
Aqueous Environment ◽  
Fused In Sarcoma ◽  
Biochemical Assays ◽  
Biologic Function

The low-complexity (LC) domain of the fused in sarcoma (FUS) RNA binding protein self-associates in a manner causing phase separation from an aqueous environment. Incubation of the FUS LC domain under physiologically normal conditions of salt and pH leads to rapid formation of liquid-like droplets that mature into a gel-like state. Both examples of phase separation have enabled reductionist biochemical assays allowing discovery of an N-terminal region of 57 residues that assembles into a labile, cross-β structure. Here we provide evidence of a nonoverlapping, C-terminal region of the FUS LC domain that also forms specific cross-β interactions. We propose that biologic function of the FUS LC domain may operate via the mutually exclusive use of these N- and C-terminal cross-β cores. Neurodegenerative disease–causing mutations in the FUS LC domain are shown to imbalance the two cross-β cores, offering an unanticipated concept of LC domain function and dysfunction.

scholarly journals A genome-wide homologous recombination screen identifies the RNA-binding protein RBMX as a component of the DNA-damage response

2012 ◽  
Vol 14 (3) ◽  
pp. 318-328 ◽  
Author(s):  
Britt Adamson ◽  
Agata Smogorzewska ◽  
Frederic D. Sigoillot ◽  
Randall W. King ◽  
Stephen J. Elledge
Keyword(s):  
Dna Damage ◽  
Homologous Recombination ◽  
Dna Damage Response ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Genome Wide ◽  
A Genome ◽  
Damage Response
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