Isolation and characterization of brain Y-box protein: developmentally regulated expression, polyribosomal association and dendritic localization

Funakoshi, Tomoko; Kobayashi, Shunsuke; Ohashi, Sachiyo; Sato, Taka Aki; Anzai, Kentaro

doi:10.1016/s0169-328x(03)00328-0

Cited by 17 publications

(17 citation statements)

References 53 publications

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“…Concomitantly, most of the FMRP is lost from the heavy sedimenting fractions of sucrose gradients (Khandjian et al, 2004). However, a small amount of Journal of Cell Science 119 (9) FMRP still sediments as a high molecular weight species (Ceman et al, 2003;Funakoshi et al, 2003;Mazroui et al, 2003). We also detected only minor amounts of FMRP in the pellet fraction following centrifugation through 50% sucrose after treating cell lysates with EDTA (lane 2).…”

Section: Fmrp and Fxr1p Co-translational Methylation Is Inhibited By mentioning

confidence: 81%

“…FMRP is found in small cytoplasmic granules As only dense objects sediment through 50% sucrose, the proteins found after EDTA or RNAse A treatment are assumed to be a type of granule (Funakoshi et al, 2003). To determine whether FMRP-containing granules could be visualized under normal cell culture conditions, HeLa cells were immunostained with anti-FMRP mAb and examined by fluorescence confocal microscopy.…”

Section: Fmrp and Fxr1p Co-translational Methylation Is Inhibited By mentioning

confidence: 99%

“…Twenty-four hours later, the cells were harvested and lysed. Equal amounts of each extract were treated or not treated for 5 minutes with 25 mM EDTA at 4°C to dissociate polyribosomes , or treated or not treated for 20 minutes at 4°C with 1 mg/ml RNAse A (Funakoshi et al, 2003). Polyribosomes and granules were subsequently sedimented by centrifugation through 50% sucrose pads.…”

Section: Polyribosome and Granule Isolationmentioning

confidence: 99%

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Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP

Dolzhanskaya¹,

Merz

Aletta

et al. 2006

Journal of Cell Science

103

101

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Section: Fmrp and Fxr1p Co-translational Methylation Is Inhibited By mentioning

confidence: 81%

Section: Fmrp and Fxr1p Co-translational Methylation Is Inhibited By mentioning

confidence: 99%

Section: Polyribosome and Granule Isolationmentioning

confidence: 99%

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Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP

Dolzhanskaya¹,

Merz

Aletta

et al. 2006

Journal of Cell Science

103

101

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“…Probing an independent immunoprecipitation revealed that the protein absent in both the DRGG and isoform 3 samples was Yb1. Like FMRP, Yb1 is an RNA-binding protein found on polyribosomes (Evdokimova et al, 1995;Funakoshi et al, 2003). It is also a core granule protein (Minich et al, 1993;Skabkin et al, 2004) whose association with FMRP is believed to be independent of RNA, suggesting a protein-protein interaction.…”

Section: Resultsmentioning

confidence: 99%

A new regulatory function of the region proximal to the RGG box in the Fragile X mental retardation protein

Blackwell

Ceman

2011

Journal of Cell Science

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SummaryFragile X mental retardation protein (FMRP) is required for normal cognition. FMRP has two autosomal paralogs, which although similar to FMRP, cannot compensate for the loss of FMRP expression in brain. The arginine-and glycine-rich region of FMRP (the RGG box) is unique; it is the high-affinity RNA-binding motif in FMRP and is encoded by exon 15. Alternative splicing occurs in the 59 end of exon 15, which is predicted to affect the structure of the distally encoded RGG box. Here, we provide evidence that isoform 3, which removes 25 amino acids from the 59 end of exon 15, has an altered conformation that reduces binding of a specific antibody and renders the RGG box unable to efficiently associate with polyribosomes. Isoform 3 is also compromised in its ability to form granules and to associate with a key messenger ribonucleoprotein Yb1 (also known as p50, NSEP1 and YBX1). Significantly, these functions are similarly compromised when the RGG box is absent from FMRP, suggesting an important regulatory role of the N-terminal region encoded by exon 15.

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“…Neuronal YB-1 expression in explicit brain areas ranges to the adult brain and amounts relevant altitudes in the adult rat, macaque and human brain (Unkrüer et al, 2009). However, a decline in the YB-1 brain expression in the postnatal phase has been described (Funakoshi et al, 2003). Main localization of YB-1 in the cytoplasm indicated existence of a large sub -fraction of YB-1 in an efficient reserve state which can be activated by various stress signals.…”

mentioning

confidence: 99%

Nuclear shuttling of Y Box binding protein-1, its clinical relevance in cancer and as a therapeutic target

Gunasekaran

Nishi

Ravikumar

et al. 2016

Bangladesh J Pharmacol

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Y-box binding protein 1 (YB-1) is an imperative biomarker for the clinical outcome of cancer patients. An overexpression of YB-1 in cancerous and adjoining tissues is an indication of aggressiveness and advanced stages. In normal resting cells, YB-1 is localized in cytoplasm while in stress conditions like cancer, nuclear shuttling of YB-1 takes place. In this review, the clinical importance of YB-1 in different cancers and the mechanism behind YB-1 nuclear shuttling have been discussed in detail. Targeted chemotherapies or molecularly targeted drugs of great importance can target and block specific molecules implicated in tumor growth and progression. YB-1 has been considered as a bonafide oncogene and accumulating evidences show the therapeutic importance of YB-1. Therapeutic strategies targeting YB-1 may improve the survival rate in cancer patients. This review extensively discusses the therapeutic importance of YB-1. Article InfoReceived:16 Mini-reviewThis article was downloaded by you on: Apr 30, 2016 In normal resting cells, full length YB-1 is mainly present in the cytoplasm of cells under stress during pathological conditions including inflammation, oxidative stress and cancer conditions. Particular segment of the YB-1 flips to the nucleus (Koike et al., 1997;Higashi et al., 2011).In this review, with the nuclear shuttling, clinical significance of YB-1 in cancer and as a therapeutic target have been evaluated from the existing literature. The present literature analysis shows the prospective role of YB-1 in cancer progression and drug resistance which could be harnessed to make it a promising therapeutic target. Nuclear shuttling of YB-1Since a number of functions have been assigned to YB-1, therefore, the sub-cellular protein shuttling needs to be highly stringent. In general, specific nuclear export signals and nuclear localization signals (NLS) contribute and direct the multifunctional shuttling and tasking (Bader and Vogt, 2005). Literature suggests three nuclear localization signals in YB-1 i.e. NLS1 (aa149-55), NLS2 (aa185-94) and NLS3 (276-92) (van Roeyen et al., 2013). The NLS3 is bipartite in composition and both the parts are essential for functionality. Irrespective of this, the changes of the spatial organization of 2 parts doesn't affect nuclear shuttling. Both NLS2 and NLS3 are essential for functionality and contain tyrosine residues which are required for phosphorylation. The full length YB-1 phosphorylated at tyrosine 281 in NLS3 has been found to be localized in the nucleus while the unphosphorylated YB-1 localized in the cytoplasm. This indicates that the phosphorylation at T-281 renders complete YB-1 to be localized in nucleus under normal conditions (van Roeyen et al., 2013). At the time of stress or cell stimulation, nuclear flipping of shortened YB-1 having N-terminal portion of the proteins takes place through a highly regulated process (Bader and Vogt, 2005;van Roeyen et al., 2013). Jürchott et al. (2003) suggested that the both C-terminal and cold shock domain of YB...

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Isolation and characterization of brain Y-box protein: developmentally regulated expression, polyribosomal association and dendritic localization

Cited by 17 publications

References 53 publications

Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP

Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP

A new regulatory function of the region proximal to the RGG box in the Fragile X mental retardation protein

Nuclear shuttling of Y Box binding protein-1, its clinical relevance in cancer and as a therapeutic target

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