<scp>YB</scp>‐1 protein: functions and regulation

Lyabin, Dmitry N.; Eliseeva, Irina A.; Ovchinnikov, Lev P.

doi:10.1002/wrna.1200

Cited by 283 publications

(276 citation statements)

References 113 publications

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“…Interestingly, in light of its interaction with different DNA repair enzymes, it is considered as a non-canonical BER protein [88]. In addition, genome-wide analysis of YB-1-RNA interaction in glioblastoma cell line unraveled a novel role of YB-1 in the regulation of miRNA biogenesis during tumorigenesis.…”

Section: Ber Enzymes and Mirna Regulation: A New Paradigm In Gene Expmentioning

confidence: 99%

Unveiling the non-repair face of the Base Excision Repair pathway in RNA processing: A missing link between DNA repair and gene expression?

2017

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Section: Ber Enzymes and Mirna Regulation: A New Paradigm In Gene Expmentioning

confidence: 99%

Unveiling the non-repair face of the Base Excision Repair pathway in RNA processing: A missing link between DNA repair and gene expression?

2017

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“…Thus, we are interested in investigating the contribution of hYVH1 toward regulating the protein complement of the maturing mRNPs in response to a variety of extracellular stimuli. Moreover, FMRP/YB-1 expression elicits cytoprotective and cell cycle effects (41,42). These cellular phenotypes are postulated to be a result of temporal translational regulation of specific mRNAs involved in these cellular processes.…”

Section: Journal Of Biological Chemistrymentioning

confidence: 99%

The Atypical Dual Specificity Phosphatase hYVH1 Associates with Multiple Ribonucleoprotein Particles

Geng¹,

Xhabija²,

Knuckle

et al. 2017

Journal of Biological Chemistry

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Edited by Linda SpremulliHuman YVH1 (hYVH1), also known as dual specificity phosphatase 12 (DUSP12), is a poorly characterized atypical dual specificity phosphatase widely conserved throughout evolution. Recent findings have demonstrated that hYVH1 expression affects cellular DNA content and is a novel cell survival phosphatase preventing both thermal and oxidative stress-induced cell death, whereas studies in yeast have established YVH1 as a novel 60S ribosome biogenesis factor. In this study, we have isolated novel hYVH1-associating proteins from human U2OS osteosarcoma cells using affinity chromatography coupled to mass spectrometry employing ion mobility separation. Numerous ribosomal proteins were identified, confirming the work done in yeast. Furthermore, proteins known to be present on additional RNP particles were identified, including Y box-binding protein 1 (YB-1) and fragile X mental retardation protein, proteins that function in translational repression and stress granule regulation. Follow-up studies demonstrated that hYVH1 co-localizes with YB-1 and fragile X mental retardation protein on stress granules in response to arsenic treatment. Interestingly, hYVH1-positive stress granules were significantly smaller, whereas knocking down hYVH1 expression attenuated stress granule breakdown during recovery from arsenite stress, indicating a possible role for hYVH1 in stress granule disassembly. These results propagate a role for dual specificity phosphatases at RNP particles and suggest that hYVH1 may affect a variety of fundamental cellular processes by regulating messenger ribonucleoprotein (mRNP) dynamics. The protein tyrosine phosphatase (PTP)4 superfamily catalyzes phosphate hydrolysis by way of a thiol phosphate enzyme intermediate. The PTP superfamily can be subdivided into subgroups that include receptor PTPs, intracellular PTPs, phosphoinositol lipid phosphatases, and dual specificity phosphatases (DSPs) (1).The DSPs represent the most diverse group of PTPs. Their name denotes the extended substrate specificity of the group for serine/threonine and tyrosine phosphoresidues (2). Analogous to tyrosine phosphatases, DSPs contain the invariant catalytic sequence C(X) 5 R and use a thiol phosphate intermediate as a catalytic mechanism (3). The broader, more shallow active site pocket of DSPs compared with tyrosine-specific phosphatases results in stabilization of phosphoserine and phosphothreonine residues in addition to phosphotyrosine (4). Members of the DSP family can be further subdivided into unique subgroups. The best characterized, known as the mitogen-activated protein kinase phosphatases, are characterized by their specificity for the pTXpY signature sequence of MAPKs (5). Another well characterized group of DSPs are the cell division cycle phosphatases (Cdc14 and Cdc25), which participate in regulation of the cell cycle by dephosphorylating cell cycle regulators, including cell cycle-dependent kinases (6). Meanwhile, a subgroup known as the atypical DSPs is the least characterized subgroup o...

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“…YB-1 is a transcription factor promoting the expression of many genes involved in cell growth, including PCNA, EGFRα, and DNA polymerase A [15][16][17][18] that was regulated through either direct or indirect YB-1 interaction with the Y-box (inverted CCAAT-box) or other sequences in gene promoters. 19 Notably, the role of YB-1 in regulating transcription is influenced through interaction with mRNA and DNA and by co-transcriptional events (splicing, mRNA packaging and stabilization). 19 During tumor progression, YB-1 regulates transcription of genes such as MDR1, cyclin A, and cyclin B1 (ref.…”

mentioning

confidence: 99%

“…19 Notably, the role of YB-1 in regulating transcription is influenced through interaction with mRNA and DNA and by co-transcriptional events (splicing, mRNA packaging and stabilization). 19 During tumor progression, YB-1 regulates transcription of genes such as MDR1, cyclin A, and cyclin B1 (ref. 20,21).…”

mentioning

confidence: 99%

RSK-mediated nuclear accumulation of the cold-shock Y-box protein-1 controls proliferation of T cells and T-ALL blasts

et al. 2016

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Deregulated proliferation is key to tumor progression. Although unrestricted proliferation of solid tumor cells correlates with the cold-shock protein Y-box (YB)-binding protein-1 accumulation in the nuclei, little is known about its expression and function in hematopoietic malignancies, such as T-cell acute lymphoblastic leukemia (T-ALL). Here we show that YB-1 protein is highly enriched in the nuclei of activated T cells and malignant human T-ALL cell lines but not in resting T cells. YB-1 S 102 mutations that either mimic (S102D) or prevent phosphorylation (S102N) led to accumulation of YB-1 in the nucleus of T cells or strictly excluded it, respectively. Inactivation of ribosomal S6 kinase (RSK) was sufficient to abrogate T-cell and T-ALL cell proliferation, suggesting that RSK mediates cell-cycle progression, possibly dependent on YB-1-phosphorylation. Indeed, phosphomimetic YB-1 S102D enhanced proliferation implying that S 102 phosphorylation is a prerequisite for malignant T-cell proliferation. At initial diagnosis of T-ALL, YB-1 localization was significantly altered in the nuclei of tumor blasts derived from bone marrow or peripheral blood. Our data show deregulated YB-1 in the nucleus as a yet unreported characteristic of T-ALL blasts and may refine strategies to restrict progression of hematopoietic tumors.

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YB‐1 protein: functions and regulation

Cited by 283 publications

References 113 publications

Unveiling the non-repair face of the Base Excision Repair pathway in RNA processing: A missing link between DNA repair and gene expression?

Unveiling the non-repair face of the Base Excision Repair pathway in RNA processing: A missing link between DNA repair and gene expression?

The Atypical Dual Specificity Phosphatase hYVH1 Associates with Multiple Ribonucleoprotein Particles

RSK-mediated nuclear accumulation of the cold-shock Y-box protein-1 controls proliferation of T cells and T-ALL blasts

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