v-Myc inhibits C/EBPβ activity by preventing C/EBPβ-induced phosphorylation of the co-activator p300

Steinmann, Simone; Schulte, Katharina; Beck, Kristina Barbara; Chachra, S; Bujnicki, Tuyen; Kh, Klempnauer

doi:10.1038/onc.2009.90

Cited by 10 publications

(23 citation statements)

References 56 publications

(90 reference statements)

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“…Subsequently, we have identified the protein kinase Hipk2 as the kinase that is responsible for these C/EBP␤-induced phosphorylation events. We have found that Hipk2 is itself recruited to the C/EBP␤ to phosphorylate the C/EBP␤-bound p300 (33). To better understand the interplay between C/EBP␤, p300, and Hipk2, we were interested to know whether C/EBP␤ serves mainly as a scaffold (or adapter) that allows Hipk2 and p300 to come into close proximity or whether C/EBP␤ is itself also phosphorylated by Hipk2.…”

Section: Resultsmentioning

confidence: 99%

“…p300-specific antibodies (RW128) were obtained from Upstate Biotechnology, Inc. Antibodies against the HA and FLAG tags were from Hiss-Diagnostics and Sigma, respectively. Rabbit antiserum against phosphorylated Ser-2280 of p300 was raised against the peptide VQPNPMSPQQHMC where the underlined serine was phosphorylated (33). Antiserum against human C/EBP␤ (H-7) was obtained from St. Cruz Biotechnology.…”

Section: Methodsmentioning

confidence: 99%

“…Subclones of the mouse 3T3-L1 stably transfected with an expression vector for Hipk2-specific shRNA or with a control vector have been described (33). Adipocyte differentiation of 3T3-L1 cells was induced by published procedures (34).…”

Section: Methodsmentioning

confidence: 99%

“…Expression Vectors-Expression vectors for full-length and truncated C/EBP␤, pCDNA3-CCR, and pCDNA3-CCR-⌬N21 and for a mutant in which amino acids Phe-27, Tyr-28, and Tyr-29 of full-length C/EBP␤ are replaced by alanine, pCDNA3-CCR-mut1, have been described (33,35). A pCDNA3-based expression vector for full-length human C/EBP␤ was obtained from G. Steger (Institute of Virology, University of Cologne).…”

Section: Methodsmentioning

confidence: 99%

“…The homeodomain interacting kinase 2 (Hipk2) has been identified as a key player in the C/EBP␤-induced phosphorylation of p300; Hipk2 interacts with C/EBP␤ and stimulates the phosphorylation of C/EBP␤-bound p300 (33). The C/EBP␤-induced phosphorylation of p300 itself is subject to regulation by other factors; the transcription factor Myc inhibits the phosphorylation of C/EBP␤-bound p300 by binding itself to C/EBP␤ and displacing Hipk2, thereby inhibiting the acetylation and the activity of C/EBP␤ (33).…”

mentioning

confidence: 99%

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Interaction and Cooperation of the CCAAT-box Enhancer-binding Protein β (C/EBPβ) with the Homeodomain-interacting Protein Kinase 2 (Hipk2)

Steinmann

Coulibaly

Ohnheiser

et al. 2013

Journal of Biological Chemistry

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Background: C/EBP␤ is a bZip transcription factor that triggers phosphorylation of p300. Results: Protein kinase Hipk2 interacts with and phosphorylates the longest isoform of C/EBP␤, thereby facilitating recruitment and subsequent phosphorylation of p300. Conclusion: C/EBP␤ is a direct interaction partner and physiological substrate of Hipk2. Significance: Hipk2 cooperates with C/EBP␤ in an isoform-specific manner.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Interaction and Cooperation of the CCAAT-box Enhancer-binding Protein β (C/EBPβ) with the Homeodomain-interacting Protein Kinase 2 (Hipk2)

Steinmann

Coulibaly

Ohnheiser

et al. 2013

Journal of Biological Chemistry

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Complex regulation of CREB-binding protein by homeodomain-interacting protein kinase 2

Kovács

Steinmann

Halfon

et al. 2015

Cellular Signalling

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CREB-binding protein (CBP) and p300 are transcriptional coactivators involved in numerous biological processes that affect cell growth, transformation, differentiation, and development. In this study, we provide evidence of the involvement of homeodomain-interacting protein kinase 2 (HIPK2) in the regulation of CBP activity. We show that HIPK2 interacts with and phosphorylates several regions of CBP. We demonstrate that serines 2361, 2363, 2371, 2376, and 2381 are responsible for the HIPK2-induced mobility shift of CBP C-terminal activation domain. Moreover, we show that HIPK2 strongly potentiates the transcriptional activity of CBP.However, our data suggest that HIPK2 activates CBP mainly by counteracting the repressive action of cell cycle regulatory domain 1 (CRD1), located between amino acids 977 and 1076, independently of CBP phosphorylation. Our findings thus highlight a complex regulation of CBP activity by HIPK2, which might be relevant for the control of specific sets of target genes involved in cellular proliferation, differentiation and apoptosis.

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C/EBPβ and C/EBPδ transcription factors: Basic biology and roles in the CNS

Pulido-Salgado

Vidal-Taboada

Saura

2015

Progress in Neurobiology

141

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v-Myc inhibits C/EBPβ activity by preventing C/EBPβ-induced phosphorylation of the co-activator p300

Cited by 10 publications

References 56 publications

Interaction and Cooperation of the CCAAT-box Enhancer-binding Protein β (C/EBPβ) with the Homeodomain-interacting Protein Kinase 2 (Hipk2)

Interaction and Cooperation of the CCAAT-box Enhancer-binding Protein β (C/EBPβ) with the Homeodomain-interacting Protein Kinase 2 (Hipk2)

Complex regulation of CREB-binding protein by homeodomain-interacting protein kinase 2

C/EBPβ and C/EBPδ transcription factors: Basic biology and roles in the CNS

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