Expression of YB-1 enhances production of murine leukemia virus vectors by stabilizing genomic viral RNA

Li, Wei; Wang, Xinlu; Gao, Guangxia

doi:10.1007/s13238-012-2090-x

Cited by 9 publications

(15 citation statements)

References 22 publications

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“…YBX1 also binds hairpin-loops in a murine retrovirus, leading to stabilization of the viral RNA genome and increased particle production (Bann, Beyer, & Parent, 2014). YBX1 binding of viral RNA also increases production of other retroviruses, including HIV (Bann et al, 2014;W. Li, Wang, & Gao, 2012;Mu, Li, Wang, & Gao, 2013).…”

Section: Discussionmentioning

confidence: 99%

Y-box protein 1 is required to sort microRNAs into exosomes in cells and in a cell-free reaction

Shurtleff

Karfilis

Temoche-Diaz

et al. 2016

Preprint

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Exosomes are small vesicles that are secreted from metazoan cells and may convey selected membrane proteins and small RNAs to target cells for the control of cell migration, development and metastasis. To study the mechanisms of RNA packaging into exosomes, we devised a purification scheme based on the membrane marker CD63 to isolate a single exosome species secreted from HEK293T cells. Using immunoisolated CD63-containing exosomes we identified a set of miRNAs that are highly enriched with respect to their cellular levels. To explore the biochemical requirements for exosome biogenesis and RNA packaging, we devised a cell-free reaction that recapitulates the species-selective enclosure of miR-223 in isolated membranes supplemented with cytosol. We found that the RNA-binding protein Y-box protein I (YBX1) binds to and is required for the sorting of miR-223 in the cell-free reaction. Furthermore, YBX1 serves an important role in the secretion of miRNAs in exosomes by HEK293T cells.

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Section: Discussionmentioning

confidence: 99%

Y-box protein 1 is required to sort microRNAs into exosomes in cells and in a cell-free reaction

Shurtleff

Karfilis

Temoche-Diaz

et al. 2016

Preprint

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“…The Y-box binding protein 1 (YBX1) is a transcription/ translation factor involved in DNA repair (Kohno et al, 2003;Li et al, 2012). Loss of YBX1 is embryonically lethal for mice, resulting in embryos with major CNS malformations (Lu et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

Nanog RNA‐binding proteins YBX1 and ILF3 affect pluripotency of embryonic stem cells

Guo

Xue

Yang

et al. 2016

Cell Biology International

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Nanog is a well-known transcription factor that plays a fundamental role in stem cell self-renewal and the maintenance of their pluripotent cell identity. There remains a large data gap with respect to the spectrum of the key pluripotency transcription factors' interaction partners. Limited information is available concerning Nanog-associated RNA-binding proteins (RBPs), and the intrinsic protein-RNA interactions characteristic of the regulatory activities of Nanog. Herein, we used an improved affinity protocol to purify Nanog-interacting RBPs from mouse embryonic stem cells (ESCs), and 49 RBPs of Nanog were identified. Among them, the interaction of YBX1 and ILF3 with Nanog mRNA was further confirmed by in vitro assays, such as Western blot, RNA immunoprecipitation (RIP), and ex vivo methods, such as immunofluorescence staining and fluorescent in situ hybridization (FISH), MS2 in vivo biotin-tagged RNA affinity purification (MS2-BioTRAP). Interestingly, RNAi studies revealed that YBX1 and ILF3 positively affected the expression of Nanog and other pluripotency-related genes. Particularly, downregulation of YBX1 or ILF3 resulted in high expression of mesoderm markers. Thus, a reduction in the expression of YBX1 and ILF3 controls the expression of pluripotency-related genes in ESCs, suggesting their roles in further regulation of the pluripotent state of ESCs.

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“…YB-1 plays a different role in hepatitis C virus, where its recruitment to sites of virus assembly influences the balance between viral RNA replication and encapsidation (85). Recently, it was reported that YB-1 stabilizes intracellular levels of HIV-1 and murine leukemia virus RNAs, resulting in an increase in virus particle production (37,38).…”

Section: Discussionmentioning

confidence: 99%

“…Although YB-1 moves into stress granules during cellular stress, it is also a component of P bodies (alternatively called GW bodies) (17,34); therefore small YB-1 RNPs are constitutive and play a central role in mRNA utilization in nonstressed cells (35). Although YB-1 does have antiviral activity in some RNA viruses (36), the retroviruses HIV-1 and murine leukemia virus (MLV) were recently reported to utilize YB-1 to stabilize viral RNA and increase virus production (37,38).…”

mentioning

confidence: 99%

A Murine Retrovirus Co-Opts YB-1, a Translational Regulator and Stress Granule-Associated Protein, To Facilitate Virus Assembly

Bann

Beyer

Parent

2014

J Virol

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The Gag protein of the murine retrovirus mouse mammary tumor virus (MMTV) orchestrates the assembly of immature virus particles in the cytoplasm which are subsequently transported to the plasma membrane for release from the cell. The morphogenetic pathway of MMTV assembly is similar to that of Saccharomyces cerevisiae retrotransposons Ty1 and Ty3, which assemble virus-like particles (VLPs) in intracytoplasmic ribonucleoprotein (RNP) complexes. Assembly of Ty1 and Ty3 VLPs depends upon cellular mRNA processing factors, prompting us to examine whether MMTV utilizes a similar set of host proteins to facilitate viral capsid assembly. Our data revealed that MMTV Gag colocalized with YB-1, a translational regulator found in stress granules and P bodies, in intracytoplasmic foci. The association of MMTV Gag and YB-1 in cytoplasmic granules was not disrupted by cycloheximide treatment, suggesting that these sites were not typical stress granules. However, the association of MMTV Gag and YB-1 was RNA dependent, and an MMTV RNA reporter construct colocalized with Gag and YB-1 in cytoplasmic RNP complexes. Knockdown of YB-1 resulted in a significant decrease in MMTV particle production, indicating that YB-1 plays a role in MMTV capsid formation. Analysis by live-cell imaging with fluorescence recovery after photobleaching (FRAP) revealed that the population of Gag proteins localized within YB-1 complexes was relatively immobile, suggesting that Gag forms stable complexes in association with YB-1. Together, our data imply that the formation of intracytoplasmic Gag-RNA complexes is facilitated by YB-1, which promotes MMTV virus assembly. IMPORTANCECellular mRNA processing factors regulate the posttranscriptional fates of mRNAs, affecting localization and utilization of mRNAs under normal conditions and in response to stress. RNA viruses such as retroviruses interact with cellular mRNA processing factors that accumulate in ribonucleoprotein complexes known as P bodies and stress granules. This report shows for the first time that mouse mammary tumor virus (MMTV), a mammalian retrovirus that assembles intracytoplasmic virus particles, commandeers the cellular factor YB-1, a key regulator of translation involved in the cellular stress response. YB-1 is essential for the efficient production of MMTV particles, a process directed by the viral Gag protein. We found that Gag and YB-1 localize together in cytoplasmic granules. Functional studies of Gag/YB-1 granules suggest that they may be sites where virus particles assemble. These studies provide significant insights into the interplay between mRNA processing factors and retroviruses.

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Expression of YB-1 enhances production of murine leukemia virus vectors by stabilizing genomic viral RNA

Cited by 9 publications

References 22 publications

Y-box protein 1 is required to sort microRNAs into exosomes in cells and in a cell-free reaction

Y-box protein 1 is required to sort microRNAs into exosomes in cells and in a cell-free reaction

Nanog RNA‐binding proteins YBX1 and ILF3 affect pluripotency of embryonic stem cells

A Murine Retrovirus Co-Opts YB-1, a Translational Regulator and Stress Granule-Associated Protein, To Facilitate Virus Assembly

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