Ski can negatively regulates macrophage differentiation through its interaction with PU.1

Ueki, Nobuhide; Zhang, L; Haymann, M J

doi:10.1038/sj.onc.1210654

Cited by 23 publications

(22 citation statements)

References 35 publications

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“…Taken together, these results suggest that PU.1 and HDAC1 recognize two separate regions of EVI1, and we concluded that recruitment of corepressor to a PU.1-dependent promoter is not the major mechanism of repression by EVI1. To further confirm these results and to determine whether the interaction between EVI1 and PU.1 contributes to the repression of PU.1-dependent genes, we used a reporter plasmid that contains one PU.1-binding site in the M-CSFR promoter linked to the luciferase gene (7,41). This reporter plasmid and a plasmid expressing PU.1 were used in transient transfections of NIH3T3 cells.…”

Section: Resultsmentioning

confidence: 95%

EVI1 Impairs Myelopoiesis by Deregulation of PU.1 Function

et al. 2009

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EVI1 is an oncogene inappropriately expressed in the bone marrow (BM) of f10% of myelodysplastic syndrome (MDS) patients. This disease is characterized by severe anemia and multilineage myeloid dysplasia that are thought to be a major cause of mortality in MDS patients. We earlier reported on a mouse model that constitutive expression of EVI1 in the BM led to fatal anemia and myeloid dysplasia, as observed in MDS patients, and we subsequently showed that EVI1 interaction with GATA1 blocks proper erythropoiesis. Whereas this interaction could provide the basis for the erythroid defects in EVI1-positive MDS, it does not explain the alteration of myeloid differentiation. Here, we have examined the expression of several genes activated during terminal myelopoiesis in BM cells and identified a group of them that are altered by EVI1. A common feature of these genes is their regulation by the transcription factor PU

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Section: Resultsmentioning

confidence: 95%

EVI1 Impairs Myelopoiesis by Deregulation of PU.1 Function

et al. 2009

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“…SHARPIN dimerization and its interaction with both the N and C SKI repressor activity. For this, we expressed WT or R8 mutant SKI and examined (i) their recruitment to the SOX10 and PAX3 enhancers, (ii) HDAC activity, (iii) histone acetylation (H3K27ac), and (iv) cooccupancy of BRD4 (31)(32)(33). These studies revealed that, compared with WT SKI, R8 mutant SKI displayed enhanced recruitment at the SOX10 and PAX3 enhancers, increased HDAC, reduced H3K27ac, and reduced BRD4 recruitment ( Figure 5J).…”

Section: Discussionmentioning

confidence: 99%

SHARPIN-mediated regulation of protein arginine methyltransferase 5 controls melanoma growth

Tamiya¹,

Kim²,

Klymenko³

et al. 2017

Journal of Clinical Investigation

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“…15 Enhanced PU.1 activity favors monocytic commitment of the granulocyte-monocyte progenitor. 44 Proteins (such as Ski 45 ) and microRNAs (such as miR-424 46 ) are reported through interaction with PU.1 to antagonize or synergize its transcriptional activity and finally affect monocyte/macrophage differentiation. Here, we reported that onzin interacted with PU.1 and partially inhibited PU.1 transcriptional activity, which may explain how onzin negatively partially regulated PMA-induced leukemia cell differentiation.…”

Section: Discussionmentioning

confidence: 99%

The downregulation of onzin expression by PKCɛ-ERK2 signaling and its potential role in AML cell differentiation

Huang

Hou

et al. 2010

Leukemia

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Onzin is a small, novel, and highly conserved protein with unique structure and tissue-restricted expression. The regulation of its expression and biological roles remain greatly elusive. Here, we provide the first demonstration that onzin expression is significantly downregulated during differentiation induction of acute myeloid leukemic (AML) cell lines and primary cells by all-trans retinoic acid (ATRA) and especially by phorbol 12-myristate 13-acetate (PMA). Applying chemical inhibitions, RNA interferences, and transfected expressions of dominant negative mutants or constitutive catalytic forms of the related kinases, we show that protein kinase C-e (PKCe)-extracellular signal-regulated protein kinase 2 (ERK2) signaling axis is required for PMA-induced downregulation of onzin expression. The ectopic expression of onzin partially inhibits PMA-induced monocytic differentiation of AML cells, whereas suppression of onzin by specific short hairpin RNAs enhances PMA-induced differentiation to a degree. Furthermore, onzin partially inhibits the transcriptional activity of hematopoiesisrelated important transcription factor PU.1 via their interaction. Taken together, our results show that PMA downregulates onzin expression through PKCe-ERK2 signaling pathway, which favors monocytic differentiation of leukemic cells.

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Ski can negatively regulates macrophage differentiation through its interaction with PU.1

Cited by 23 publications

References 35 publications

EVI1 Impairs Myelopoiesis by Deregulation of PU.1 Function

EVI1 Impairs Myelopoiesis by Deregulation of PU.1 Function

SHARPIN-mediated regulation of protein arginine methyltransferase 5 controls melanoma growth

The downregulation of onzin expression by PKCɛ-ERK2 signaling and its potential role in AML cell differentiation

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