An Acidic Protein, YBAP1, Mediates the Release of YB-1 from mRNA and Relieves the Translational Repression Activity of YB-1

Matsumoto, Ken; Tanaka, Kimio; Tsujimoto, Masafumi

doi:10.1128/mcb.25.5.1779-1792.2005

Cited by 53 publications

(47 citation statements)

References 80 publications

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“…To identify the proteins that retain YB-1 in the cytoplasm, we performed immunoprecipitation of HSc025-treated cytoplasmic extracts with anti-YB-1 antibodies. Consistent with the results of a previous study (22), a number of proteins that interact with YB-1 were detected by silver staining (Fig. 3A).…”

Section: Hsc025 Suppresses Collagen Gene Expression In Activatedsupporting

confidence: 81%

A Novel Small Compound That Promotes Nuclear Translocation of YB-1 Ameliorates Experimental Hepatic Fibrosis in Mice

Higashi

Tomigahara

Shiraki

et al. 2011

Journal of Biological Chemistry

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Section: Hsc025 Suppresses Collagen Gene Expression In Activatedsupporting

confidence: 81%

A Novel Small Compound That Promotes Nuclear Translocation of YB-1 Ameliorates Experimental Hepatic Fibrosis in Mice

Higashi

Tomigahara

Shiraki

et al. 2011

Journal of Biological Chemistry

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“…1). RNase treatment prior to immunoprecipitation revealed that the association between FRGY2 and most proteins is likely to be mediated primarily by their binding to the same RNA molecules, with the notable exception of YBAP1, a chicken homologue of which has been shown to bind directly to the Y-box protein YB-1 (39). We identified some of the FRGY2-associated proteins by mass spectrometry, as listed in Fig.…”

Section: Identification Of the Components Of Frgy2-associatedmentioning

confidence: 99%

“…In Vitro Translation-␤-Actin and chloramphenicol acetyltransferase mRNAs ( 32 P-labeled) were prepared using plasmids pSPcACT1 and pSPCAT, respectively, as described previously (39). 500 fmol of ␤-actin or chloramphenicol acetyltransferase mRNA was incubated with various amounts of GST-xRAP55 or Xp54-His 6 at 30°C for 20 min in a 9.5-l reaction mixture consisting of 10 mM triethanolamine (pH 7.9), 50 mM KCl, 4 mM MgCl 2 , 1 mM DTT, and 2 units/l RNase inhibitor.…”

Section: Methodsmentioning

confidence: 99%

RAP55, a Cytoplasmic mRNP Component, Represses Translation in Xenopus Oocytes

Tanaka

Ogawa

Takagi

et al. 2006

Journal of Biological Chemistry

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128

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mRNAs in eukaryotic cells are presumed to always associate with a set of proteins to form mRNPs. In Xenopus oocytes, a large pool of maternal mRNAs is masked from the translational apparatus as storage mRNPs. Here we identified Xenopus RAP55 (xRAP55) as a component of RNPs that associate with FRGY2, the principal component of maternal mRNPs. RAP55 is a member of the Scd6 or Lsm14 family. RAP55 localized to cytoplasmic foci in Xenopus oocytes and the processing bodies (P-bodies) in cultured human cells: in the latter cells, RAP55 is an essential constituent of the P-bodies. We isolated xRAP55-containing complexes from Xenopus oocytes and identified xRAP55-associated proteins, including a DEAD-box protein, Xp54, and a protein arginine methyltransferase, PRMT1. Recombinant xRAP55 repressed translation, together with Xp54, in an in vitro translation system. In addition, xRAP55 repressed translation in oocytes when tethered with a reporter mRNA. Domain analyses revealed that the N-terminal region of RAP55, including the Lsm domain, is important for the localization to P-bodies and translational repression. Taken together, our results suggest that xRAP55 is involved in translational repression of mRNA as a component of storage mRNPs.

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“…In general, the cold-shock response includes growth arrest and a reduction in protein synthesis in bacteria (Jolly and Morimoto, 2000). The eukaryotic Y-box-binding proteins have been not known to be involved in the cold-shock response; however, recent study indicated a block in cell proliferation after low-temperature shift in YB-1 knockout chicken cell line (Matsumoto et al, 2005).…”

mentioning

confidence: 99%

Expression of Y-box-binding protein dbpC/contrin, a potentially new cancer/testis antigen

et al. 2006

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Y-box-binding proteins are members of the human cold-shock domain protein superfamily, which includes dbpA, dbpB/YB-1, and dbpC/contrin. dbpC/contrin is a germ cell-specific Y-box-binding protein and is suggested to function as a nuclear transcription factor and RNA-binding protein in the cytoplasm. Whereas ubiquitous dbpB/YB-1 expression has been well studied in various types of human carcinomas as a prognostic or predictive marker, the dbpC/contrin expression in human tumour cells has not been reported. In this report, we provide the first evidence showing that dbpC was highly expressed in human testicular seminoma and ovarian dysgerminomas, and in carcinomas in other tissues and that its expression in normal tissues is nearly restricted to germ cells and placental trophoblasts. These results indicate that dbpC/contrin would be a potentially novel cancer/testis antigen.

show abstract

An Acidic Protein, YBAP1, Mediates the Release of YB-1 from mRNA and Relieves the Translational Repression Activity of YB-1

Cited by 53 publications

References 80 publications

A Novel Small Compound That Promotes Nuclear Translocation of YB-1 Ameliorates Experimental Hepatic Fibrosis in Mice

A Novel Small Compound That Promotes Nuclear Translocation of YB-1 Ameliorates Experimental Hepatic Fibrosis in Mice

RAP55, a Cytoplasmic mRNP Component, Represses Translation in Xenopus Oocytes

Expression of Y-box-binding protein dbpC/contrin, a potentially new cancer/testis antigen

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