Towards the mechanism(s) of YB-3 synthesis regulation by YB-1

Lyabin, Dmitry N.; Smolin, Egor A.; Budkina, Karina; Eliseeva, Irina A.; Ovchinnikov, Lev P.

doi:10.1080/15476286.2020.1859243

Cited by 7 publications

(5 citation statements)

References 33 publications

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“…E-cadherin and YB-1 expression appeared enhanced in the Ybx3 knockout. The latter finding is supported by observations that these cold shock proteins counter-regulate one another [39][40][41]. Immunohistochemistry showed that in healthy kidneys, DbpA was primarily expressed only in vascular smooth muscle cells, which is in agreement with our previous observation [7].…”

Section: Verification and Characterization Of The Ybx3 Knockoutsupporting

confidence: 91%

Cold Shock Domain Protein DbpA Orchestrates Tubular Cell Damage and Interstitial Fibrosis in Inflammatory Kidney Disease

Lindquist

Bernhardt

Reichardt

et al. 2023

Cells

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DNA-binding protein A (DbpA) belongs to the Y-box family of cold shock domain proteins that exert transcriptional and translational activities in the cell via their ability to bind and regulate mRNA. To investigate the role of DbpA in kidney disease, we utilized the murine unilateral ureter obstruction (UUO) model, which recapitulates many features of obstructive nephropathy seen in humans. We observed that DbpA protein expression is induced within the renal interstitium following disease induction. Compared with wild-type animals, obstructed kidneys from Ybx3-deficient mice are protected from tissue injury, with a significant reduction in the number of infiltrating immune cells as well as in extracellular matrix deposition. RNAseq data from UUO kidneys show that Ybx3 is expressed by activated fibroblasts, which reside within the renal interstitium. Our data support a role for DbpA in orchestrating renal fibrosis and suggest that strategies targeting DbpA may be a therapeutic option to slow disease progression.

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Section: Verification and Characterization Of The Ybx3 Knockoutsupporting

confidence: 91%

Cold Shock Domain Protein DbpA Orchestrates Tubular Cell Damage and Interstitial Fibrosis in Inflammatory Kidney Disease

Lindquist

Bernhardt

Reichardt

et al. 2023

Cells

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“…First, we obtained derivatives of the double knockout HEK293T∆YB-1∆YB-3 (∆∆) cells stably expressing full-length (with the untranslated region) YB-1 and/or YB-3 mRNA. It could be expected that in such cells with YB-1 mRNA and YB-3 mRNA containing native UTRs, the proteins would be synthesized in quantities comparable to the amount of endogenous proteins in wild-type HEK293T since the translation of YB-1 mRNA and YB-3 mRNA is controlled by the YB-1 protein, as we described previously [10,11]. Indeed, the immunoblot analysis of cell lysates showed that the YB-1 protein is expressed in HEK293T∆∆ + YB-1 (∆∆ + YB-1) and HEK293T∆∆ + YB-1 + YB-3 cells (∆∆ + YB-1 + YB-3) at the same level as in parental HEK293T cells (from which HEK293T∆∆ was derived).…”

Section: Yb-1 and Yb-3 Expressions Partially Restore Translation In H...mentioning

confidence: 80%

“…Also, it was proposed that YB-1 can stimulate global translation by displacing initiation factors from the mRNA's "body" and concentrating them at the 5 ′ UTR [13]. However, the addition of YB-1 to a cell-free translation system based on either ∆∆ cells or ∆YB-1 cells does not stimulate the translation of reporter mRNAs [11]. This suggests that the main reason for the enhanced translation observed in YB-expressing cells is different from that proposed previously.…”

Section: Discussionmentioning

confidence: 99%

Y-Box-Binding Proteins Have a Dual Impact on Cellular Translation

Eliseeva,

Buyan,

Smolin

et al. 2024

IJMS

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Y-box-binding proteins (YB proteins) are multifunctional DNA- and RNA-binding proteins that play an important role in the regulation of gene expression. The high homology of their cold shock domains and the similarity between their long, unstructured C-terminal domains suggest that Y-box-binding proteins may have similar functions in a cell. Here, we consider the functional interchangeability of the somatic YB proteins YB-1 and YB-3. RNA-seq and Ribo-seq are used to track changes in the mRNA abundance or mRNA translation in HEK293T cells solely expressing YB-1, YB-3, or neither of them. We show that YB proteins have a dual effect on translation. Although the expression of YB proteins stimulates global translation, YB-1 and YB-3 inhibit the translation of their direct CLIP-identified mRNA targets. The impact of YB-1 and YB-3 on the translation of their mRNA targets is similar, which suggests that they can substitute each other in inhibiting the translation of their mRNA targets in HEK293T cells.

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“…Among these MS‐identified proteins, YBX1 caught our attention (Figure 4B) and was confirmed by western blot analysis (Figure 4C). As a DNA‐ and RNA‐binding protein, it regulates transcription, translation, DNA repair, mRNA packaging, and pre‐mRNA splicing, among other processes to participate in tumor progression 32,33 . The RIP assay revealed that the YBX1 antibody significantly enriched HIF1A‐AS3 in OC cells (Figure 4D).…”

Section: Resultsmentioning

confidence: 99%

“…As a DNAand RNA-binding protein, it regulates transcription, translation, DNA repair, mRNA packaging, and pre-mRNA splicing, among other processes to participate in tumor progression. 32,33 The RIP assay revealed that the YBX1 antibody significantly enriched HIF1A-AS3 in OC cells (Figure 4D). In addition, RT-qPCR and western blot analyses suggested that the knockdown of HIF1A-AS3 might not affect YBX1 expression (Figures 4E,F).…”

Section: Role Of Hif1a-as3 As a Tumor Suppressor In Hypoxic Oc Progre...mentioning

confidence: 99%

A novel hypoxia‐stimulated lncRNA HIF1A‐AS3 binds with YBX1 to promote ovarian cancer tumorigenesis by suppressing p21 and AJAP1 transcription

Xie,

Wang,

Meng

et al. 2023

Molecular Carcinogenesis

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Hypoxia is characteristic of the ovarian tumor (OC) microenvironment and profoundly affects tumorigenesis and therapeutic response. Long noncoding RNAs (lncRNAs) play various roles in tumor progression; however, the characteristics of lncRNAs in pathological responses of the OC microenvironment are not entirely understood. Through high‐throughput sequencing, lncRNA expression in hypoxia (1% O2) and normoxia (21% O2) SKOV3 cells was explored and analyzed. The 5′‐ and 3′‐rapid amplification of complementary DNA ends was used to detect the full length of the novel HIF1A‐AS3 transcript. Real‐time quantitative polymerase chain reaction was used to assess HIF1A‐AS3 expression in OC cells and tissues. In vitro and in vivo evaluations of the biological functions of hypoxic HIF1A‐AS3 were conducted. To clarify the underlying mechanisms of HIF1A‐AS3 in hypoxic OC, a dual‐luciferase assay, chromatin immunoprecipitation, RNA pull‐down, RNA immunoprecipitation, and RNA‐sequencing were used. We used high‐throughput sequencing to investigate a novel lncRNA, HIF1A‐AS3, as a hypoxic candidate significantly elevated in OC cells/tissues. HIF1A‐AS3 was predominantly localized in the nucleus and promoted in vitro and in vivo OC growth and tumorigenesis. Hypoxia‐inducible factor 1α bound to hypoxia response elements in the HIF1A‐AS3 promoter region and stimulated its expression in hypoxia. Under hypoxia, HIF1A‐AS3 directly integrated with Y‐Box binding protein 1 and inhibited its ability to bind to the promoters of p21 and AJAP1 to repress their transcriptional activity, thereby promoting hypoxic OC progression. Our results revealed the crucial role and mechanism of the novel hypoxic HIF1A‐AS3 in the oncogenesis of OC. The novel HIF1A‐AS3 could be a crucial biomarker and therapeutic target for future OC treatments.

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Towards the mechanism(s) of YB-3 synthesis regulation by YB-1

Cited by 7 publications

References 33 publications

Cold Shock Domain Protein DbpA Orchestrates Tubular Cell Damage and Interstitial Fibrosis in Inflammatory Kidney Disease

Cold Shock Domain Protein DbpA Orchestrates Tubular Cell Damage and Interstitial Fibrosis in Inflammatory Kidney Disease

Y-Box-Binding Proteins Have a Dual Impact on Cellular Translation

A novel hypoxia‐stimulated lncRNA HIF1A‐AS3 binds with YBX1 to promote ovarian cancer tumorigenesis by suppressing p21 and AJAP1 transcription

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