Regulation of the human fas promoter by YB-1, Purα and AP-1 transcription factors

Lasham, Annette; Lindridge, Erica; Rudert, Fritz; Onrust, René; Watson, James

doi:10.1016/s0378-1119(00)00220-1

Cited by 124 publications

(107 citation statements)

References 40 publications

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“…These results are consistent with recent results from Drosophila indicating that H1 interacts with multiple nuclear ribosomal proteins for more efficient repression of transcription (18). In further support of a repressive role for H1 in transcription, four of the proteins (YB1, FIR, PARP1, and PUR␣) present in the purified complex also belong to the corepressor family of proteins (22,(31)(32)(33). Somewhat surprisingly, however, we also found among the pulldown factors ASXL1, nucleolin, ␤-catenin, and CAPER␣, which were originally identified as coactivators in gene activation (34 -37).…”

Section: Linker Histone H12 Stably Associates With Multiple Regulatosupporting

confidence: 92%

Isolation and Characterization of a Novel H1.2 Complex That Acts as a Repressor of p53-mediated Transcription

Kim

Choi

Heo

et al. 2008

Journal of Biological Chemistry

110

109

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Linker histone H1 has been generally viewed as a global repressor of transcription by preventing the access of transcription factors to sites in chromatin. However, recent studies suggest that H1 can interact with other regulatory factors for its action as a negative modulator of specific genes. To investigate these aspects, we established a human cell line expressing H1.2, one of the H1 subtypes, for the purification of H1-interacting proteins. Our results showed that H1.2 can stably associate with sets of cofactors and ribosomal proteins that can significantly repress p53-dependent, p300-mediated chromatin transcription. This repressive action of H1.2 complex involves direct interaction of H1.2 with p53, which in turn blocks p300-mediated acetylation of chromatin. YB1 and PUR␣, two factors present in the H1.2 complex, together with H1.2 can closely recapitulate the repressive action of the entire H1.2 complex in transcription. Chromatin immunoprecipitation and RNA interference analyses further confirmed that the recruitment of YB1, PUR␣, and H1.2 to the p53 target gene Bax is required for repression of p53-induced transcription. Therefore, these results reveal a previously unrecognized function of H1 as a transcriptional repressor as well as the underlying mechanism involving specific sets of factors in this repression process.Histones are the major protein components to compact genomic DNA into the limited volume of the nucleus as a highly organized chromatin structure. The basic element of chromatin is the nucleosome, which consists of 146 base pairs of DNA wrapped around an octameric core of histones containing two molecules each of H2A, H2B, H3, and H4 (1-4). This repeating unit of chromatin is associated with another type of histone called linker histone H1 to achieve an additional level of compaction, making genes inaccessible to transcription factors and preventing their expression (5-9). Mammalian cells have at least eight histone H1 subtypes including H1.1 through H1.5 and somatic cell-specific H1o as well as germ cell-specific H1t and H1oo, all consisting of a highly conserved globular domain and less conserved N-and C-terminal domains (6,8,10). The existence of multiple H1 subtypes and the diversity of their amino acid sequences raise the possibility that individual subtypes have nonredundant functions in various cellular processes. In addition, the expression of each H1 subtype depends on the tissue, phase of the cell cycle, and developmental stage, further suggesting the specific contribution of linker histone subtypes for regulation of various cellular processes (6,8,11).Although most studies have focused on the contribution of H1 as a structural component of the nucleosome, it is becoming apparent that H1 also acts as a repressor for specific gene transcription (12)(13)(14)(15). This repressive capacity of H1 on transcription appears to be accomplished by its localization at particular chromosomal domains with specific transcription regulators. Msx1 recruits a linker histone H1 to the MyoD gene,...

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Section: Linker Histone H12 Stably Associates With Multiple Regulatosupporting

confidence: 92%

Isolation and Characterization of a Novel H1.2 Complex That Acts as a Repressor of p53-mediated Transcription

Kim

Choi

Heo

et al. 2008

Journal of Biological Chemistry

110

109

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“…In addition, several genes important for wound healing and cellular proliferation and survival are regulated by YB-1, including collagen alpha1 and alpha2 (Norman et al 2001;Higashi et al 2003), matrix metalloproteinase 2 (Mertens et al 1997), the B-chain isoform of plateletderived growth factor (Stenina et al 2000), vascular endothelial growth factor (Coles et al 2004), granulocyte-macrophage-colony stimulating factor (Coles et al 2000), and Fas death receptor (Lasham et al 2000); moreover, YB-1 can also regulate αSMA and human pulmonary myofibroblasts (Zhang et al 2005). Takahashi et al (2010) reported that YB-1 is increased in the angiogenic endothelial cells of various tumors and is involved in the growth of endothelial cells.…”

Section: Discussionmentioning

confidence: 99%

Increased Expression of Y-Box-Binding Protein-1 in Hind-Limb Muscles During Regeneration from Ischemic Injury in Mice

Fuke

Narita

Wada

et al. 2018

Tohoku J. Exp. Med.

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Critical limb ischemia (CLI) is the most severe complication of peripheral arterial disease (PAD). Understanding the molecular mechanisms underlying tissue repair after CLI is necessary for preventing PAD progression. Y-box binding protein-1 (YB-1) regulates the expression of many genes in response to environmental stresses. We aimed to determine whether YB-1 is involved in ischemic muscle regeneration. A mouse ischemic hind-limb model was generated; namely, the femoral, saphenous, and popliteal arteries in the left hind limb were ligated. The right hind limb, with skin incisions alone, served as control. Hind limbs (n = 3-5 for each time point) were examined on day 0 (before the operation) and on postoperative days 1, 2, 7, 10, and 14, and the biceps femoris, adductor, rectus femoris, and gracilis muscles were subjected to histopathological and immunohistochemical analyses. In ischemic limbs, myogenesis, triggered by an increase in myotubes, began on day 7; thereafter, regenerated muscles gradually increased in volume. RT-PCR analysis showed that YB-1 mRNA levels were increased in the limbs after ischemic injury, peaked on day 2, and subsequently decreased. On day 7, expression levels of MyoD and alphasmooth muscle actin (αSMA) mRNAs were significantly higher in ischemic muscles than in control muscles. Immunohistochemical analysis revealed increased YB-1 immunoreactivity in myoblasts and myotubes on day 7, which was decreased by day 14. The immunoreactive αSMA and smooth muscle myosin heavy chain were transiently increased in myotubes. This is the first report showing the increased expression of YB-1 during muscle regeneration after ischemic injury.

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“…Transcriptional targets of YB1 include genes associated with cell death such as FAS (Lasham et al, 2000), encoding a cell deathassociated receptor, and the tumor suppressor gene, TP53 (Okamoto et al, 2000;Lasham et al, 2003). YB1 also positively regulates genes associated with cell proliferation including epidermal growth factor receptor (EGFR or c-ERBB1) (Sakura et al, 1988), matrix metalloproteinase-2 (MMP-2) (Mertens et al, 1997(Mertens et al, , 1999, and DNA topoisomerase IIa (Shibao et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Y-box factor YB1 controls p53 apoptotic function

et al. 2005

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Nuclear localization and high levels of the Y-box-binding protein YB1 appear to be important indicators of drug resistance and tumor prognosis. YB1 also interacts with the p53 tumor suppressor protein. In this paper, we have continued to explore YB1/p53 interactions. We report that transcriptionally active p53 is required for nuclear localization of YB1. We go on to show that nuclear YB1 regulates p53 function. Our data demonstrate that YB1 inhibits the ability of p53 to cause cell death and to transactivate cell death genes, but does not interfere with the ability of p53 to transactivate the CDKN1A gene, encoding the kinase p21 WAF1/CIP1 required for cell cycle arrest, nor the MDM2 gene. We also show that nuclear YB1 is associated with a failure to increase the level of the Bax protein in normal mammary epithelial cells after stress activation of p53. Together these data suggest that (nuclear) YB1 selectively alters p53 activity, which may in part provide an explanation for the correlation of nuclear YB1 with drug resistance and poor tumor prognosis.

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Regulation of the human fas promoter by YB-1, Purα and AP-1 transcription factors

Cited by 124 publications

References 40 publications

Isolation and Characterization of a Novel H1.2 Complex That Acts as a Repressor of p53-mediated Transcription

Isolation and Characterization of a Novel H1.2 Complex That Acts as a Repressor of p53-mediated Transcription

Increased Expression of Y-Box-Binding Protein-1 in Hind-Limb Muscles During Regeneration from Ischemic Injury in Mice

Y-box factor YB1 controls p53 apoptotic function

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