Y-box-binding protein 1 as a non-canonical factor of base excision repair

Alemasova, Elizaveta E.; Moor, Nina; Naumenko, Konstantin N.; Kutuzov, Mikhail M.; Sukhanova, Maria V.; Pestryakov, P. E.; Lavrik, Olga I.

doi:10.1016/j.bbapap.2016.08.012

Cited by 39 publications

(54 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…5C) [221], while NEIL1 stimulates the activity of OGG1 on DNA containing OG [222]. These proteins activate transcription or the stress response, leading to the possibility that NEIL1 plays a more important role in the cell beyond removal of damaged bases.…”

Section: The Biology Of the Neils And Hydantoinsmentioning

confidence: 99%

Formation and processing of DNA damage substrates for the hNEIL enzymes

Fleming

Burrows

2017

Free Radical Biology and Medicine

112

135

View full text Add to dashboard Cite

Reactive oxygen species (ROS) are harnessed by the cell for signaling at the same time as being detrimental to cellular components such as DNA. The genome and transcriptome contain instructions that can alter cellular processes when oxidized. The guanine (G) heterocycle in the nucleotide pool, DNA, or RNA is the base most prone to oxidation. The oxidatively-derived products of G consistently observed in high yields from hydroxyl radical, carbonate radical, or singlet oxygen oxidations under conditions modeling the cellular reducing environment are discussed. The major G base oxidation products are 8-oxo-7,8-dihydroguanine (OG), 5-carboxamido-5-formamido-2-iminohydantoin (2Ih), spiroiminodihydantoin (Sp), and 5-guanidinohydantoin (Gh). The yields of these products show dependency on the oxidant and the reaction context that includes nucleoside, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA), and G-quadruplex DNA (G4-DNA) structures. Upon formation of these products in cells, they are recognized by the DNA glycosylases in the base excision repair (BER) pathway. This review focuses on initiation of BER by the mammalian Nei-like1-3 (NEIL1-3) glycosylases for removal of 2Ih, Sp, and Gh. The unique ability of the human NEILs to initiate removal of the hydantoins in ssDNA, bulge-DNA, bubble-DNA, dsDNA, and G4-DNA is outlined. Additionally, when Gh exists in a G4 DNA found in a gene promoter, NEIL-mediated repair is modulated by the plasticity of the G4-DNA structure provided by additional G-runs flanking the sequence. On the basis of these observations and cellular studies from the literature, the interplay between DNA oxidation and BER to alter gene expression is discussed.

show abstract

Section: The Biology Of the Neils And Hydantoinsmentioning

confidence: 99%

Formation and processing of DNA damage substrates for the hNEIL enzymes

Fleming

Burrows

2017

Free Radical Biology and Medicine

112

135

View full text Add to dashboard Cite

show abstract

“…YB-1 binds to a wide range of DNA repair enzymes: base excision repair enzymes (NEIL2 [177], APE1 [184], DNA polymerase β [177], DNA polymerase δ [185], PCNA [186], DNA-ligase IIIα [177], NEIL1, PARP1, and PARP2 [187]), mismatch repair enzymes (MSH2 [185]), and DNA double-stranded breaks repair enzymes (Ku80 [185]). YB-1 is required for the recognition of bulky lesions by NER factor XPC-HR23b [188] and modulates the activity of key and regulatory BER enzymes [177, 187, 189-191]. …”

Section: Y-box-binding Proteinmentioning

confidence: 99%

“…The emergence of these membraneless compartments, as well as the formation of repair complexes at sites of DNA lesions, is orchestrated by poly(ADP-ribose) [155, 156, 195]. Recent findings have demonstrated that YB-1 is able to modulate PAR biosynthesis depending on the level of DNA damage [187] and acts as a target for poly(ADP-ribosyl)ation [187, 196]. Another feature is the fact that YB-1 protects PAR from cleavage by PARG, extending the half-life of the polymer [187].…”

Section: Y-box-binding Proteinmentioning

confidence: 99%

See 1 more Smart Citation

At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair

Alemasova

Lavrik

2017

Acta Naturae

View full text Add to dashboard Cite

RNA-binding proteins (RBPs) regulate RNA metabolism, from synthesis to decay. When bound to RNA, RBPs act as guardians of the genome integrity at different levels, from DNA damage prevention to the post-transcriptional regulation of gene expression. Recently, RBPs have been shown to participate in DNA repair. This fact is of special interest as DNA repair pathways do not generally involve RNA. DNA damage in higher organisms triggers the formation of the RNA-like polymer – poly(ADP-ribose) (PAR). Nucleic acid-like properties allow PAR to recruit DNA- and RNA-binding proteins to the site of DNA damage. It is suggested that poly(ADP-ribose) and RBPs not only modulate the activities of DNA repair factors, but that they also play an important role in the formation of transient repairosome complexes in the nucleus. Cytoplasmic biomolecules are subjected to similar sorting during the formation of RNA assemblages by functionally related mRNAs and promiscuous RBPs. The Y-box-binding protein 1 (YB-1) is the major component of cytoplasmic RNA granules. Although YB-1 is a classic RNA-binding protein, it is now regarded as a non-canonical factor of DNA repair.

show abstract

“…Radiation-induced DSBs are repaired by either homologous recombination or nonhomologous end-joining [16,17]. YB-1 participates in repair of damaged DNA, such as DSB repair [18] and base excision repair [19]. So far, the mechanism by which YB-1 stimulates DSB repair is not known.…”

Section: Introductionmentioning

confidence: 99%

Stress-Induced Phosphorylation of Nuclear YB-1 Depends on Nuclear Trafficking of p90 Ribosomal S6 Kinase

Tiwari

Rebholz

Maier

et al. 2018

IJMS

View full text Add to dashboard Cite

Ionizing radiation (IR) and epidermal growth factor (EGF) stimulate Y-box binding protein-1 (YB-1) phosphorylation at Ser-102 in KRAS wild-type (KRASwt) cells, whereas in KRAS mutated (KRASmut) cells, YB-1 is constitutively phosphorylated, independent of IR or EGF. YB-1 activity stimulates the repair of IR-induced DNA double-strand breaks (DSBs) in the nucleus. Thus far, the YB-1 nuclear translocation pattern after cell exposure to various cellular stressors is not clear. In the present study, we investigated the pattern of YB-1 phosphorylation and its possible translocation to the nucleus in KRASwt cells after exposure to IR, EGF treatment, and conditional expression of mutated KRAS(G12V). IR, EGF, and conditional KRAS(G12V) expression induced YB-1 phosphorylation in both the cytoplasmic and nuclear fractions of KRASwt cells. None of the stimuli induced YB-1 nuclear translocation, while p90 ribosomal s6 kinase (RSK) translocation was enhanced in KRASwt cells after any of the stimuli. EGF-induced RSK translocation to the nucleus and nuclear YB-1 phosphorylation were completely blocked by the EGF receptor kinase inhibitor erlotinib. Likewise, RSK inhibition blocked RSK nuclear translocation and nuclear YB-1 phosphorylation after irradiation and KRAS(G12V) overexpression. In summary, acute stimulation of YB-1 phosphorylation does not lead to YB-1 translocation from the cytoplasm to the nucleus. Rather, irradiation, EGF treatment, or KRAS(G12V) overexpression induces RSK activation, leading to its translocation to the nucleus, where it activates already-existing nuclear YB-1. Our novel finding illuminates the signaling pathways involved in nuclear YB-1 phosphorylation and provides a rationale for designing appropriate targeting strategies to block YB-1 in oncology as well as in radiation oncology.

show abstract

Y-box-binding protein 1 as a non-canonical factor of base excision repair

Cited by 39 publications

References 54 publications

Formation and processing of DNA damage substrates for the hNEIL enzymes

Formation and processing of DNA damage substrates for the hNEIL enzymes

At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair

Stress-Induced Phosphorylation of Nuclear YB-1 Depends on Nuclear Trafficking of p90 Ribosomal S6 Kinase

Contact Info

Product

Resources

About