Acetylation and MAPK phosphorylation cooperate to regulate the degradation of active GATA-1

Hernández‐Hernández, Ángel; Ray, Priyadip; Litos, Gabi; Cirò, Marco; Ottolenghi, Sergio; Beug, Hartmut; Boyes, Joan

doi:10.1038/sj.emboj.7601228

Cited by 89 publications

(83 citation statements)

References 35 publications

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“…Previous reports have shown that acetylation of nonhistone proteins may be linked to regulation of their stability (Hernandez-Hernandez et al, 2006;Leduc et al, 2006;Mateo et al, 2009 (Figure 2c). This observation implies that N3 IC is a substrate of HAT-dependent acetylation.…”

Section: Tsa Treatment Regulates Notch3 Signalingmentioning

confidence: 73%

“…Protein acetylation has been reported to prime subsequent ubiquitin-dependent stability of target proteins (Hernandez-Hernandez et al, 2006;Leduc et al, 2006). Although we and others suggested that proteasomal degradation of Notch intracellular domain (N IC ) may be required for repressing Notch signaling, the underlying mechanisms are still to be clarified.…”

Section: Acetylation Regulates Notch3 Ubiquitination Proteasomal Degmentioning

confidence: 95%

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Acetylation controls Notch3 stability and function in T-cell leukemia

Palermo

Checquolo²,

Giovenco

et al. 2011

Oncogene

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Section: Tsa Treatment Regulates Notch3 Signalingmentioning

confidence: 73%

Section: Acetylation Regulates Notch3 Ubiquitination Proteasomal Degmentioning

confidence: 95%

Acetylation controls Notch3 stability and function in T-cell leukemia

Palermo

Checquolo²,

Giovenco

et al. 2011

Oncogene

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“…Although serine phosphorylation of GATA-1 has been reported, its role on GATA-1 function remains unclear. [39][40][41] These observations indicate that study of the functional relevance of GATA-1 tyrosine phosphorylation is warranted in AMKL. …”

Section: Discussionmentioning

confidence: 99%

A novel fusion of RBM6 to CSF1R in acute megakaryoblastic leukemia

Mercher

Tyner

et al. 2007

Blood

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Activated tyrosine kinases have been frequently implicated in the pathogenesis of cancer, including acute myeloid leukemia (AML), and are validated targets for therapeutic intervention with small-molecule kinase inhibitors. To identify novel activated tyrosine kinases in AML, we used a discovery platform consisting of immunoaffinity profiling coupled to mass spectrometry that identifies large numbers of tyrosinephosphorylated proteins, including active kinases. This method revealed the presence of an activated colony-stimulating factor 1 receptor (CSF1R) kinase in the acute megakaryoblastic leukemia (AMKL) cell line MKPL-1. Further studies using siRNA and a small-molecule inhibitor showed that CSF1R is essential for the growth and survival of MKPL-1 cells. DNA sequence analysis of cDNA generated by 5RACE from CSF1R coding sequences identified a novel fusion of the RNA binding motif 6 (RBM6) gene to CSF1R gene generated presumably by a t(3;5)(p21;q33) translocation. Expression of the RBM6-CSF1R fusion protein conferred interleukin-3 (IL-3)-independent growth in BaF3 cells, and induces a myeloid proliferative disease (MPD) with features of megakaryoblastic leukemia in a murine transplant model. These findings identify a novel potential therapeutic target in leukemogenesis, and demonstrate the utility of phosphoproteomic strategies for discovery of tyrosine kinase alleles. (Blood.

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“…The function of GATA1 can be regulated by an array of posttranslational modifications, including phosphorylation and acetylation as well as SUMOylation (Boyes et al, 1998;Cantor and Orkin, 2002;Collavin et al, 2004;Yu et al, 2005;Hernandez-Hernandez et al, 2006;Lamonica et al, 2006;Zhao et al, 2006). Phosphorylation of GATA1 and its role in regulation of GATA1 function has been extensively adenovirus stock was a gift from F. Giordano (Yale University).…”

Section: Methodsmentioning

confidence: 99%

SENP1-mediated GATA1 deSUMOylation is critical for definitive erythropoiesis

Yu¹,

Ji²,

Zhang³

et al. 2010

J Cell Biol

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Small ubiquitin-like modifier (SUMO) modification of proteins (SUMOylation) and deSUMOylation have emerged as important regulatory mechanisms for protein function. SENP1 (SUMO-specific protease) deconjugates SUMOs from modified proteins. We have created SENP1 knockout (KO) mice based on a Cre-loxP system. Global deletion of SENP1 (SENP1 KO) causes anemia and embryonic lethality between embryonic day 13.5 and postnatal day 1, correlating with erythropoiesis defects in the fetal liver. Bone marrow transplantation of SENP1 KO fetal liver cells to irradiated adult recipients confers erythropoiesis defects. Protein analyses show that the GATA1 and GATA1-dependent genes are down-regulated in fetal liver of SENP1 KO mice. This down-regulation correlates with accumulation of a SUMOylated form of GATA1. We further show that SENP1 can directly deSUMOylate GATA1, regulating GATA1-dependent gene expression and erythropoiesis by in vitro assays. Moreover, we demonstrate that GATA1 SUMOylation alters its DNA binding, reducing its recruitment to the GATA1-responsive gene promoter. Collectively, we conclude that SENP1 promotes GATA1 activation and subsequent erythropoiesis by deSUMOylating GATA1.

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Acetylation and MAPK phosphorylation cooperate to regulate the degradation of active GATA-1

Cited by 89 publications

References 35 publications

Acetylation controls Notch3 stability and function in T-cell leukemia

Acetylation controls Notch3 stability and function in T-cell leukemia

A novel fusion of RBM6 to CSF1R in acute megakaryoblastic leukemia

SENP1-mediated GATA1 deSUMOylation is critical for definitive erythropoiesis

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