EBP1 protein modulates the expression of human MHC class II molecules in non-hematopoietic cancer cells

Pisapia, Laura; Barba, Pasquale; Cortese, Angela; Cicatiello, Valeria; Morelli, Francesco; Pozzo, Giovanna Del

doi:10.3892/ijo.2015.3051

Cited by 14 publications

(12 citation statements)

References 40 publications

(57 reference statements)

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“…The biological effects of EBP1 vary depending on cell type and context, although the precise mechanisms for the differential roles and regulation of EBP1 in different tissues have not been defined (Miao et al 2015;Pisapia et al 2015;Hwang et al 2016). Previous study showed that Ebp1 is weakly expressed in mouse skeletal muscles, and its expression is higher in activated versus quiescent satellite cells (Squatrito et al 2004;Pallafacchina et al 2010;Figeac et al 2014).…”

Section: Discussionmentioning

confidence: 99%

“…EBP1 belongs to the PA2G4 family of transcription factors, which appears to fulfill multiple diverse biological functions (Pisapia et al . ; Hwang et al . ; Ko et al .…”

Section: Introductionmentioning

confidence: 99%

“…EBP1 belongs to the PA2G4 family of transcription factors, which appears to fulfill multiple diverse biological functions (Pisapia et al 2015;Hwang et al 2016;Ko et al 2016). EBP1 has active involvement of cell growth, apoptosis and differentiation in many cell types (Radomski & Jost 1995;Xia et al 2001;Ko et al 2015).…”

Section: Introductionmentioning

confidence: 99%

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Ebp1 regulates myogenic differentiation of myoblast cells via SMAD2/3 signaling pathway

Wang

Liu

et al. 2017

Dev Growth Differ

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Regulation of skeletal muscle development requires many of the regulatory networks that are fundamental to developmental myogenesis. ErbB3 binding protein-1 (Ebp1) is involved in the control of myoblasts development in chicken. However, the expression and biological functions of Ebp1 in the progress of myogenesis are unclear. This study focused on determining the effect of Ebp1 on myogenic proliferation and differentiation using a primary myoblasts culture model. Ebp1 was found to upregulate in proliferating myoblasts and decrease at the early stage of myogenic differentiation. The level of endogenous Ebp1 increased from E9 to E20 chicken leg muscles. Knockdown of Ebp1 had no effect on myoblasts proliferation. However, myogenic differentiation into multinucleated myotubes was significantly reduced. The mRNA and protein expression of MRFs was decreased when Ebp1 was knocked down. Downregulation of Ebp1, accompanied by elevated levels of pSMAD2/3, suggests that Ebp1 is involved in regulating myogenic differentiation via SMAD2/3 inhibition. The phosphorylation of SMAD2/3 was activated and the expression of MYOD and MYOG was reduced in Ebp1 knockdown myoblasts, but addition of LY2109761 (an inhibitor specified to SMAD2/3) blocked these effects. Collectively, these results indicate that Ebp1 promotes myoblast differentiation by inhibition of SMAD2/3 signaling pathway during chicken myogenesis. These data provide new insights into the biological role of Ebp1 in embryonic chicken skeletal muscle development.

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Section: Discussionmentioning

confidence: 99%

“…EBP1 belongs to the PA2G4 family of transcription factors, which appears to fulfill multiple diverse biological functions (Pisapia et al . ; Hwang et al . ; Ko et al .…”

Section: Introductionmentioning

confidence: 99%

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Ebp1 regulates myogenic differentiation of myoblast cells via SMAD2/3 signaling pathway

Wang

Liu

et al. 2017

Dev Growth Differ

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“…It binds to rRNAs and ribosomes (Squatrito et al, 2006) and also supports ribosome biogenesis by interacting with the Pol I transcription factor TIF-IA (Nguyen le et al, 2015;Nguyen et al, 2019) and possibly with nucleolar nucleophosmin (Okada et al, 2007). Fourth, HsEbp1 also stabilizes several mRNAs by binding their 39UTRs (Bose et al, 2006;Zhou et al, 2010;Pisapia et al, 2015).…”

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confidence: 99%

ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem

et al. 2019

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The ErbB-3 BINDING PROTEIN 1 (EBP1) drives growth, but the mechanism of how it acts in plants is little understood. Here, we show that EBP1 expression and protein abundance in Arabidopsis (Arabidopsis thaliana) are predominantly confined to meristematic cells and are induced by sucrose and partially dependent on TARGET OF RAPAMYCIN (TOR) kinase activity. Consistent with being downstream of TOR, silencing of EBP1 restrains, while overexpression promotes, root growth, mostly under sucrose-limiting conditions. Inducible overexpression of RETINOBLASTOMA RELATED (RBR), a sugar-dependent transcriptional repressor of cell proliferation, depletes meristematic activity and causes precocious differentiation, which is attenuated by EBP1. To understand the molecular mechanism, we searched for EBP1-and RBR-interacting proteins by affinity purification and mass spectrometry. In line with the double-stranded RNA-binding activity of EBP1 in human (Homo sapiens) cells, the overwhelming majority of EBP1 interactors are part of ribonucleoprotein complexes regulating many aspects of protein synthesis, including ribosome biogenesis and mRNA translation. We confirmed that EBP1 associates with ribosomes and that EBP1 silencing hinders ribosomal RNA processing. We revealed that RBR also interacts with a set of EBP1-associated nucleolar proteins as well as factors that function in protein translation. This suggests EBP1 and RBR act antagonistically on common processes that determine the capacity for translation to tune meristematic activity in relation to available resources.

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“…Western blot analysis confirms the specific enrichment of EBP1 by A-ROD (Figure 8D) while we could not recapitulate the specificity for HNRNPK although this has been reported to bind specifically to some long ncRNAs (Gumireddy et al, 2013; Huarte et al, 2010) (Figure 8D). The EBP1 isoform p48 has been reported to act as a context-dependent transcriptional activator (Pisapia et al, 2015), and is found to bind RNA in the nucleus (Conrad et al, 2016). To address whether EBP1 can bind to the DKK1 locus and to which extent this is dependent on A-ROD we did ChIP for EBP1 with or without depletion of A-ROD using siRNA (Figure 8E).…”

Section: Resultsmentioning

confidence: 99%

Chromatin-release of the long ncRNA A-ROD is required for transcriptional activation of its target gene DKK1

Ntini

et al. 2017

Preprint

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Long non-coding RNAs (ncRNAs) are involved in both positive and negative regulation of transcription. Long ncRNAs are often enriched in the nucleus and at chromatin but whether chromatin-release plays a functional role is unknown. Here, we used epigenetic marks, expression level and strength of chromatin interactions to group long ncRNAs and find that those engaged in strong chromatin interactions are less enriched at chromatin in MCF-7 cells, suggesting a functional involvement of chromatin-release of long ncRNAs in transcriptional regulation. To study this further, we identify the long ncRNA A-ROD, an activating regulator of the Wnt signaling inhibitor DKK1. We show that A-ROD enhances transcription elongation of DKK1 in an RNA-dependent manner and that A-ROD recruits EBP1 to the DKK1 promoter. Our data suggest that the activating function depends on the release of A-ROD from chromatin, and further identify a functional regulatory interaction mediated by A-ROD in the transcription activation of DKK1. We propose that the release of a subset of long ncRNAs is important for their function, adding a new mechanistic perspective to the subcellular localization of long ncRNAs.

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EBP1 protein modulates the expression of human MHC class II molecules in non-hematopoietic cancer cells

Cited by 14 publications

References 40 publications

Ebp1 regulates myogenic differentiation of myoblast cells via SMAD2/3 signaling pathway

Ebp1 regulates myogenic differentiation of myoblast cells via SMAD2/3 signaling pathway

ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem

Chromatin-release of the long ncRNA A-ROD is required for transcriptional activation of its target gene DKK1

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