Phosphorylation of ICBP90 by protein kinase A enhances topoisomerase IIα expression

Trotzier, Marie-Aline; Bronner, Christian; Bathami, Kawtar; Mathieu, Éric; Abbady, Abdul Qader; Jeanblanc, Michaël; Muller, Christian D.; Rochette‐Egly, Cécile; Mousli, Marc

doi:10.1016/j.bbrc.2004.05.028

Cited by 30 publications

(18 citation statements)

References 26 publications

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“…UHRF1 undergoes PKA phosphorylation at S298, which is located at the junction (28). Our NMR and ITC experiments indicated that modulation of the linker:Tudor contacts by S298 phosphorylation changed the binding mode of UHRF1 to the histone H3 tail (Figs.…”

Section: Discussionmentioning

confidence: 71%

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Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1

Arita

Isogai

Oda

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

185

251

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Multiple covalent modifications on a histone tail are often recognized by linked histone reader modules. UHRF1 [ubiquitin-like, containing plant homeodomain (PHD) and really interesting new gene (RING) finger domains 1], an essential factor for maintenance of DNA methylation, contains linked two-histone reader modules, a tandem Tudor domain and a PHD finger, tethered by a 17-aa linker, and has been implicated to link histone modifications and DNA methylation. Here, we present the crystal structure of the linked histone reader modules of UHRF1 in complex with the amino-terminal tail of histone H3. Our structural and biochemical data provide the basis for combinatorial readout of unmodified Arg-2 (H3-R2) and methylated Lys-9 (H3-K9) by the tandem tudor domain and the PHD finger. The structure reveals that the intermodule linker plays an essential role in the formation of a histone H3-binding hole between the reader modules by making extended contacts with the tandem tudor domain. The histone H3 tail fits into the hole by adopting a compact fold harboring a central helix, which allows both of the reader modules to simultaneously recognize the modification states at H3-R2 and H3-K9. Our data also suggest that phosphorylation of a linker residue can modulate the relative position of the reader modules, thereby altering the histone H3-binding mode. This finding implies that the linker region plays a role as a functional switch of UHRF1 involved in multiple regulatory pathways such as maintenance of DNA methylation and transcriptional repression.epigenetics | multidomain structure | posttranslational modification | X-ray crystallography

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Section: Discussionmentioning

confidence: 71%

“…S298, which is located at the junction and contacts the indole ring of W238 on the surface of TTD (Fig. 4A), is a target of PKA phosphorylation (28). The corresponding phosphorylation site in homologous proteins is highly conserved among mammals, birds, and reptiles, suggesting its functional importance (SI Appendix, Fig.…”

Section: Resultsmentioning

confidence: 99%

Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1

Arita

Isogai

Oda

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

185

251

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“…LY294002 is a commonly used pharmacologic inhibitor of PI3K. It acts at the ATP-binding site of the PI3K enzyme, thus selectively inhibiting the PI3K-Akt nexus [12]. Therefore, in the current study we used adriamycin as a positive control to observe the effects of deactivation of PI3K signalling on human T cell lymphoma cell growth, and to investigate the relationships between PI3K and ERK1/2 signals with ICBP90.…”

Section: Discussionmentioning

confidence: 99%

“…In a recent report, it has been demonstrated that overexpression of ICBP90 in normal cells is associated with an elevation of TopoIIa expression and an increase in cell proliferation rate. ICBP90 also has a function in cell-cycle regulation:expression of ICBP90 is observed throughout the cell cycle but peaks at late-phase G 1 and G 2 /M phases in noncancerous human cells [12]. ICBP90 inhibitors could inhibit the expression of ICBP90, arresting the cell cycle at the G 1 /G 0 stage and blocking its entrance from S phase to G 2 /M phase.…”

Section: Introductionmentioning

confidence: 99%

PI3K pathway inhibitor LY294002 alters Jurkat T cell biobehaviours via ERK1/2-ICBP90 mediation

et al. 2014

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Abstract:Little is known about whether there is a relationshipbetweenPI3K/AKT, ERK1/2 and an inverted CCAAT box binding protein (ICBP90) in biological behaviours of tumour cells. The aim of this study was to determine thisusing Jurkat T cells. Compared to PD98059 (an ERK1/2 signaling inhibitor), DAPT (a Notch signaling inhibitor) or adriamycin (a classical anti-tumour drug), the inhibition of Jurkat T cell growth by LY294002 (a PI3K/Akt signaling inhibitor) was more obvious. LY294002 combined with adriamycin appeared to have a synergistic effect. LY294002 strongly blocked Jurkat T cells at each phase of cell cycle with a decrease of DNA content, superior to adriamycin. Consistent with these changes, the expression of phosphorylated ERK1/2 was markedly decreased in the LY294002-treated Jurkat T cells, leading to the reduction of ICBP90 production, followed by moderate attenuation of TGF-β secretion. The results suggest that deactivation of PI3K/Akt signalling can surpress Jurkat T cell growth through inhibiting cell proliferation and blocking the cell cycle. ICBP90 may mediate the PI3K/AKT-ERK1/2 signalling to regulate leukemia cell growth.

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“…, which enhances its interaction with target DNA (29). Phospho-ICBP90 (pICBP90) showed increased 5′CATT 0-8 length-dependent binding, as revealed by reduced 5′CATT 5-8 -encoding ICBP90 and transfected it into human HEK293 target cells.…”

mentioning

confidence: 99%

Transcription factor ICBP90 regulates the MIF promoter and immune susceptibility locus

Yao¹,

Leng²,

Sauler³

et al. 2016

Journal of Clinical Investigation

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Phosphorylation of ICBP90 by protein kinase A enhances topoisomerase IIα expression

Cited by 30 publications

References 26 publications

Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1

Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1

PI3K pathway inhibitor LY294002 alters Jurkat T cell biobehaviours via ERK1/2-ICBP90 mediation

Transcription factor ICBP90 regulates the MIF promoter and immune susceptibility locus

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