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Article ; Online: FOXO1 forkhead domain mutants in B-cell lymphoma lack transcriptional activity.

Sablon, Ariane / Bollaert, Emeline / Pirson, Constance / Velghe, Amélie I / Demoulin, Jean-Baptiste

2022 Volume 12, Issue 1, Page(s) 1309

Abstract: Somatic point mutations of the FOXO1 transcription factor were reported in non-Hodgkin lymphoma including diffuse large B-cell lymphoma, follicular lymphoma and Burkitt lymphoma. These alterations were associated with a poor prognosis and resistance to ... ...

Abstract	Somatic point mutations of the FOXO1 transcription factor were reported in non-Hodgkin lymphoma including diffuse large B-cell lymphoma, follicular lymphoma and Burkitt lymphoma. These alterations were associated with a poor prognosis and resistance to therapy. Nearly all amino acid substitutions are localized in two major clusters, affecting either the N-terminal region (Nt mutations) or the forkhead DNA-binding domain (DBD mutations). While recent studies have focused on Nt mutations, we characterized FOXO1 DBD mutants. We analyzed their transcriptional activity, DNA binding, phosphorylation and protein-protein interaction. The majority of DBD mutants showed a decrease in activity and DNA binding, while preserving AKT phosphorylation and interaction with the cytoplasmic ATG7 protein. In addition, we investigated the importance of conserved residues of the α-helix 3 of the DBD. Amino acids I213, R214, H215 and L217 appeared to be crucial for FOXO1 activity. Our data underlined the key role of multiple amino-acid residues of the forkhead domain in FOXO1 transcriptional activity and revealed a new type of FOXO1 loss-of-function mutations in B-cell lymphoma.
MeSH term(s)	Amino Acids/metabolism ; DNA/metabolism ; Forkhead Box Protein O1/chemistry ; Forkhead Box Protein O1/genetics ; Forkhead Box Protein O1/metabolism ; HEK293 Cells ; Humans ; Loss of Function Mutation ; Lymphoma, B-Cell/genetics ; Lymphoma, B-Cell/metabolism ; Phosphorylation/genetics ; Point Mutation ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Domains/genetics ; Protein Interaction Maps/genetics ; Proto-Oncogene Proteins c-akt/metabolism ; Signal Transduction/genetics ; Transcriptional Activation ; Transfection
Chemical Substances	Amino Acids ; FOXO1 protein, human ; Forkhead Box Protein O1 ; DNA (9007-49-2) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2022-01-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-05334-4
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Article ; Online: Idiopathic basal ganglia calcification-associated PDGFRB mutations impair the receptor signalling.

Arts, Florence A / Velghe, Amélie I / Stevens, Monique / Renauld, Jean-Christophe / Essaghir, Ahmed / Demoulin, Jean-Baptiste

Journal of cellular and molecular medicine

2014 Volume 19, Issue 1, Page(s) 239–248

Abstract: Platelet-derived growth factors (PDGF) bind to two related receptor tyrosine kinases, which are encoded by the PDGFRA and PDGFRB genes. Recently, heterozygous PDGFRB mutations have been described in patients diagnosed with idiopathic basal ganglia ... ...

Abstract	Platelet-derived growth factors (PDGF) bind to two related receptor tyrosine kinases, which are encoded by the PDGFRA and PDGFRB genes. Recently, heterozygous PDGFRB mutations have been described in patients diagnosed with idiopathic basal ganglia calcification (IBGC or Fahr disease), a rare inherited neurological disorder. The goal of the present study was to determine whether these mutations had a positive or negative impact on the PDGFRB activity. We first showed that the E1071V mutant behaved like wild-type PDGFRB and may represent a polymorphism unrelated to IBGC. In contrast, the L658P mutant had no kinase activity and failed to activate any of the pathways normally stimulated by PDGF. The R987W mutant activated Akt and MAP kinases but did not induce the phosphorylation of signal transducer and activator of transcription 3 (STAT3) after PDGF stimulation. Phosphorylation of phospholipase Cγ was also decreased. Finally, we showed that the R987W mutant was more rapidly degraded upon PDGF binding compared to wild-type PDGFRB. In conclusion, PDGFRB mutations associated with IBGC impair the receptor signalling. PDGFRB loss of function in IBGC is consistent with recently described inactivating mutations in the PDGF-B ligand. These results raise concerns about the long-term safety of PDGF receptor inhibition by drugs such as imatinib.
MeSH term(s)	Amino Acid Substitution ; Basal Ganglia Diseases/genetics ; Calcinosis/genetics ; Cell Line, Tumor ; HEK293 Cells ; Humans ; Mutant Proteins/metabolism ; Mutation/genetics ; Neurodegenerative Diseases/genetics ; Phospholipase C gamma/metabolism ; Proteolysis/drug effects ; Proto-Oncogene Proteins c-sis/pharmacology ; Receptor, Platelet-Derived Growth Factor beta/genetics ; STAT3 Transcription Factor/metabolism ; Signal Transduction/drug effects ; Signal Transduction/genetics
Chemical Substances	Mutant Proteins ; Proto-Oncogene Proteins c-sis ; STAT3 Transcription Factor ; Receptor, Platelet-Derived Growth Factor beta (EC 2.7.10.1) ; Phospholipase C gamma (EC 3.1.4.3)
Language	English
Publishing date	2014-10-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2074559-X
ISSN	1582-4934 ; 1582-4934 ; 1582-1838
ISSN (online)	1582-4934
ISSN	1582-4934 ; 1582-1838
DOI	10.1111/jcmm.12443
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Article: PDGF‐induced fibroblast growth requires monounsaturated fatty acid production by stearoyl‐CoA desaturase

Coomans de Brachène, Alexandra / Dif, Nicolas / de Rocca Serra, Audrey / Bonnineau, Chloé / Velghe, Amélie I. / Larondelle, Yvan / Tyteca, Donatienne / Demoulin, Jean‐Baptiste

FEBS Open Bio. 2017 Mar., v. 7, no. 3

2017

Abstract: Stearoyl‐coenzyme A desaturase (SCD) catalyzes the Δ9‐cis desaturation of saturated fatty acids (SFA) to generate monounsaturated fatty acids (MUFA). This enzyme is highly up‐regulated by platelet‐derived growth factor (PDGF) in human fibroblasts. ... ...

Abstract	Stearoyl‐coenzyme A desaturase (SCD) catalyzes the Δ9‐cis desaturation of saturated fatty acids (SFA) to generate monounsaturated fatty acids (MUFA). This enzyme is highly up‐regulated by platelet‐derived growth factor (PDGF) in human fibroblasts. Accordingly, the analysis of cellular fatty acids by gas chromatography showed that PDGF significantly increased the proportion of MUFA, particularly palmitoleate, in cellular lipids. To further analyze the role of SCD in fibroblasts, we used small hairpin RNA targeting SCD (shSCD), which decreased the MUFA content. SCD down‐regulation blunted the proliferation of fibroblasts in response to PDGF. This was confirmed using a pharmacological inhibitor of SCD. In addition, proliferation was blocked by palmitate and stearate (two SCD substrates) but not by palmitoleate and oleate (two SCD products). In the presence of an equal amount of oleate, palmitate had no effect on cell proliferation. SCD inhibition or down‐regulation did not decrease PDGF receptor activity or signaling. However, by measuring plasma membrane lipid lateral diffusion by fluorescence recovery after photobleaching, we showed that the modulation of the MUFA/SFA ratio by PDGF and SCD inhibitor was related to modifications of membrane fluidity. Altogether, our data suggest that SCD is required for the response of normal fibroblasts to growth factors.
Keywords	RNA ; cell proliferation ; fibroblasts ; fluorescence recovery after photobleaching ; gas chromatography ; humans ; membrane fluidity ; oleic acid ; palmitates ; plasma membrane ; platelet-derived growth factor ; platelet-derived growth factor receptors ; stearic acid ; stearoyl-CoA desaturase
Language	English
Dates of publication	2017-03
Size	p. 414-423.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	2651702-4
ISSN	2211-5463
ISSN	2211-5463
DOI	10.1002/2211-5463.12194
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Article ; Online: Atomistic mechanism of the constitutive activation of PDGFRA via its transmembrane domain.

Polyansky, Anton A / Bocharov, Eduard V / Velghe, Amélie I / Kuznetsov, Andrey S / Bocharova, Olga V / Urban, Anatoly S / Arseniev, Alexander S / Zagrovic, Bojan / Demoulin, Jean-Baptiste / Efremov, Roman G

Biochimica et biophysica acta. General subjects

2018 Volume 1863, Issue 1, Page(s) 82–95

Abstract: Single-point mutations in the transmembrane (TM) region of receptor tyrosine kinases (RTKs) can lead to abnormal ligand-independent activation. We use a combination of computational modeling, NMR spectroscopy and cell experiments to analyze in detail the ...

Abstract	Single-point mutations in the transmembrane (TM) region of receptor tyrosine kinases (RTKs) can lead to abnormal ligand-independent activation. We use a combination of computational modeling, NMR spectroscopy and cell experiments to analyze in detail the mechanism of how TM domains contribute to the activation of wild-type (WT) PDGFRA and its oncogenic V536E mutant. Using a computational framework, we scan all positions in PDGFRA TM helix for identification of potential functional mutations for the WT and the mutant and reveal the relationship between the receptor activity and TM dimerization via different interfaces. This strategy also allows us design a novel activating mutation in the WT (I537D) and a compensatory mutation in the V536E background eliminating its constitutive activity (S541G). We show both computationally and experimentally that single-point mutations in the TM region reshape the TM dimer ensemble and delineate the structural and dynamic determinants of spontaneous activation of PDGFRA via its TM domain. Our atomistic picture of the coupling between TM dimerization and PDGFRA activation corroborates the data obtained for other RTKs and provides a foundation for developing novel modulators of the pathological activity of PDGFRA.
MeSH term(s)	Allosteric Site ; Computational Biology ; Computer Simulation ; Humans ; Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Mutagenesis ; Phosphatidylcholines/chemistry ; Point Mutation ; Protein Domains ; Protein Multimerization ; Receptor, Platelet-Derived Growth Factor alpha/chemistry ; Receptor, Platelet-Derived Growth Factor alpha/genetics
Chemical Substances	Ligands ; Phosphatidylcholines ; Receptor, Platelet-Derived Growth Factor alpha (EC 2.7.10.1) ; 1-palmitoyl-2-oleoylphosphatidylcholine (TE895536Y5)
Language	English
Publishing date	2018-09-22
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2018.09.011
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Article: PDGF-induced fibroblast growth requires monounsaturated fatty acid production by stearoyl-CoA desaturase.

Coomans de Brachène, Alexandra / Dif, Nicolas / de Rocca Serra, Audrey / Bonnineau, Chloé / Velghe, Amélie I / Larondelle, Yvan / Tyteca, Donatienne / Demoulin, Jean-Baptiste

FEBS open bio

2017 Volume 7, Issue 3, Page(s) 414–423

Abstract: Stearoyl-coenzyme A desaturase (SCD) catalyzes the Δ9-cis desaturation of saturated fatty acids (SFA) to generate monounsaturated fatty acids (MUFA). This enzyme is highly up-regulated by platelet-derived growth factor (PDGF) in human fibroblasts. ... ...

Abstract	Stearoyl-coenzyme A desaturase (SCD) catalyzes the Δ9-cis desaturation of saturated fatty acids (SFA) to generate monounsaturated fatty acids (MUFA). This enzyme is highly up-regulated by platelet-derived growth factor (PDGF) in human fibroblasts. Accordingly, the analysis of cellular fatty acids by gas chromatography showed that PDGF significantly increased the proportion of MUFA, particularly palmitoleate, in cellular lipids. To further analyze the role of SCD in fibroblasts, we used small hairpin RNA targeting SCD (shSCD), which decreased the MUFA content. SCD down-regulation blunted the proliferation of fibroblasts in response to PDGF. This was confirmed using a pharmacological inhibitor of SCD. In addition, proliferation was blocked by palmitate and stearate (two SCD substrates) but not by palmitoleate and oleate (two SCD products). In the presence of an equal amount of oleate, palmitate had no effect on cell proliferation. SCD inhibition or down-regulation did not decrease PDGF receptor activity or signaling. However, by measuring plasma membrane lipid lateral diffusion by fluorescence recovery after photobleaching, we showed that the modulation of the MUFA/SFA ratio by PDGF and SCD inhibitor was related to modifications of membrane fluidity. Altogether, our data suggest that SCD is required for the response of normal fibroblasts to growth factors.
Language	English
Publishing date	2017-03
Publishing country	England
Document type	Journal Article
ISSN	2211-5463
ISSN	2211-5463
DOI	10.1002/2211-5463.12194
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Article ; Online: PDGFRB gain-of-function mutations in sporadic infantile myofibromatosis.

Arts, Florence A / Sciot, Raf / Brichard, Bénédicte / Renard, Marleen / de Rocca Serra, Audrey / Dachy, Guillaume / Noël, Laura A / Velghe, Amélie I / Galant, Christine / Debiec-Rychter, Maria / Van Damme, An / Vikkula, Miikka / Helaers, Raphaël / Limaye, Nisha / Poirel, Hélène A / Demoulin, Jean-Baptiste

Human molecular genetics

2017 Volume 26, Issue 10, Page(s) 1801–1810

Abstract: Infantile myofibromatosis is one of the most prevalent soft tissue tumors of infancy and childhood. Multifocal nodules with visceral lesions are associated with a poor prognosis. A few familial cases have been linked to mutations in various genes ... ...

Abstract	Infantile myofibromatosis is one of the most prevalent soft tissue tumors of infancy and childhood. Multifocal nodules with visceral lesions are associated with a poor prognosis. A few familial cases have been linked to mutations in various genes including PDGFRB. In this study, we sequenced PDGFRB, which encodes a receptor tyrosine kinase, in 16 cases of myofibromatosis or solitary myofibroma. Mutations in the coding sequence of PDGFRB were identified in 6 out of 8 patients with the sporadic multicentric form of the disease and in 1 out of 8 patients with isolated myofibroma. Two patients had the same mutation in multiple separated lesions. By contrast, a third patient had three different PDGFRB mutations in the three nodules analyzed. Mutations were located in the transmembrane, juxtamembrane and kinase domains of the receptor. We showed that these mutations activated receptor signaling in the absence of ligand and transformed fibroblasts. In one case, a weakly-activating germline variant was associated with a stronger somatic mutation, suggesting a two-hit model for familial myofibromatosis. Furthermore, the mutant receptors were sensitive to the tyrosine kinase inhibitor imatinib, except D850V, which was inhibited by dasatinib and ponatinib, suggesting a targeted therapy for severe myofibromatosis. In conclusion, we identified gain-of-function PDGFRB mutations in the majority of multifocal infantile myofibromatosis cases, shedding light on the mechanism of disease development, which is reminiscent of multifocal venous malformations induced by TIE2 mutations. Our results provide a genetic test to facilitate diagnosis, and preclinical data for development of molecular therapies.
MeSH term(s)	Child ; Child, Preschool ; Female ; Humans ; Infant ; Infant, Newborn ; Male ; Mutation ; Myofibromatosis/congenital ; Myofibromatosis/genetics ; Myofibromatosis/metabolism ; Receptor, Platelet-Derived Growth Factor beta/genetics ; Receptor, Platelet-Derived Growth Factor beta/metabolism ; Receptor, TIE-2/genetics
Chemical Substances	PDGFRB protein, human (EC 2.7.10.1) ; Receptor, Platelet-Derived Growth Factor beta (EC 2.7.10.1) ; Receptor, TIE-2 (EC 2.7.10.1)
Language	English
Publishing date	2017-05-15
Publishing country	England
Document type	Journal Article
ZDB-ID	1108742-0
ISSN	1460-2083 ; 0964-6906
ISSN (online)	1460-2083
ISSN	0964-6906
DOI	10.1093/hmg/ddx081
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Zs.A 3469: Show issues

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Article ; Online: ETV6-PDGFRB and FIP1L1-PDGFRA stimulate human hematopoietic progenitor cell proliferation and differentiation into eosinophils: the role of nuclear factor-κB.

Montano-Almendras, Carmen P / Essaghir, Ahmed / Schoemans, Hélène / Varis, Inci / Noël, Laura A / Velghe, Amélie I / Latinne, Dominique / Knoops, Laurent / Demoulin, Jean-Baptiste

Haematologica

2012 Volume 97, Issue 7, Page(s) 1064–1072

Abstract: Background: ETV6-PDGFRB (also called TEL-PDGFRB) and FIP1L1-PDGFRA are receptor-tyrosine kinase fusion genes that cause chronic myeloid malignancies associated with hypereosinophilia. The aim of this work was to gain insight into the mechanisms whereby ... ...

Abstract	Background: ETV6-PDGFRB (also called TEL-PDGFRB) and FIP1L1-PDGFRA are receptor-tyrosine kinase fusion genes that cause chronic myeloid malignancies associated with hypereosinophilia. The aim of this work was to gain insight into the mechanisms whereby fusion genes affect human hematopoietic cells and in particular the eosinophil lineage. Design and methods: We introduced ETV6-PDGFRB and FIP1L1-PDGFRA into human CD34(+) hematopoietic progenitor and stem cells isolated from umbilical cord blood. Results: Cells transduced with these oncogenes formed hematopoietic colonies even in the absence of cytokines. Both oncogenes also stimulated the proliferation of cells in liquid culture and their differentiation into eosinophils. This model thus recapitulated key features of the myeloid neoplasms induced by ETV6-PDGFRB and FIP1L1-PDGFRA. We next showed that both fusion genes activated the transcription factors STAT1, STAT3, STAT5 and nuclear factor-κB. Phosphatidylinositol-3 kinase inhibition blocked nuclear factor-κB activation in transduced progenitor cells and patients' cells. Nuclear factor-κB was also activated in the human FIP1L1-PDGFRA-positive leukemia cell line EOL1, the proliferation of which was blocked by bortezomib and the IκB kinase inhibitor BMS-345541. A mutant IκB that prevents nuclear translocation of nuclear factor-κB inhibited cell growth and the expression of eosinophil markers, such as the interleukin-5 receptor and eosinophil peroxidase, in progenitors transduced with ETV6-PDGFRB. In addition, several potential regulators of this process, including HES6, MYC and FOXO3 were identified using expression microarrays. Conclusions: We show that human CD34(+) cells expressing PDGFR fusion oncogenes proliferate autonomously and differentiate towards the eosinophil lineage in a process that requires nuclear factor-κB. These results suggest new treatment possibilities for imatinib-resistant myeloid neoplasms associated with PDGFR mutations.
MeSH term(s)	Antigens, CD34/genetics ; Antigens, CD34/metabolism ; Cell Differentiation/drug effects ; Cell Proliferation/drug effects ; Cells, Cultured ; Eosinophilia/complications ; Eosinophilia/genetics ; Eosinophilia/metabolism ; Eosinophilia/pathology ; Eosinophils/cytology ; Eosinophils/drug effects ; Eosinophils/metabolism ; Fetal Blood ; Gene Expression/drug effects ; Hematopoietic Stem Cells/cytology ; Hematopoietic Stem Cells/drug effects ; Hematopoietic Stem Cells/metabolism ; Humans ; I-kappa B Kinase/genetics ; I-kappa B Kinase/metabolism ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/complications ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/genetics ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/metabolism ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/pathology ; NF-kappa B/genetics ; NF-kappa B/metabolism ; Oncogene Proteins, Fusion/genetics ; Oncogene Proteins, Fusion/metabolism ; Protein Kinase Inhibitors/pharmacology ; Receptor, Platelet-Derived Growth Factor alpha/genetics ; Receptor, Platelet-Derived Growth Factor alpha/metabolism ; STAT Transcription Factors/genetics ; STAT Transcription Factors/metabolism ; Signal Transduction/drug effects ; Transduction, Genetic ; Transgenes ; mRNA Cleavage and Polyadenylation Factors/genetics ; mRNA Cleavage and Polyadenylation Factors/metabolism
Chemical Substances	Antigens, CD34 ; ETV6-PDGFRB fusion protein, human ; NF-kappa B ; Oncogene Proteins, Fusion ; Protein Kinase Inhibitors ; STAT Transcription Factors ; mRNA Cleavage and Polyadenylation Factors ; FIP1L1-PDGFRA fusion protein, human (EC 2.7.10.1) ; Receptor, Platelet-Derived Growth Factor alpha (EC 2.7.10.1) ; I-kappa B Kinase (EC 2.7.11.10)
Language	English
Publishing date	2012-01-22
Publishing country	Italy
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2333-4
ISSN	1592-8721 ; 0017-6567 ; 0390-6078
ISSN (online)	1592-8721
ISSN	0017-6567 ; 0390-6078
DOI	10.3324/haematol.2011.047530
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Article ; Online: FOXO1 forkhead domain mutants in B-cell lymphoma lack transcriptional activity.

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Article ; Online: Idiopathic basal ganglia calcification-associated PDGFRB mutations impair the receptor signalling.

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Article: PDGF‐induced fibroblast growth requires monounsaturated fatty acid production by stearoyl‐CoA desaturase

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Article ; Online: Atomistic mechanism of the constitutive activation of PDGFRA via its transmembrane domain.

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Article: PDGF-induced fibroblast growth requires monounsaturated fatty acid production by stearoyl-CoA desaturase.

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Article ; Online: PDGFRB gain-of-function mutations in sporadic infantile myofibromatosis.

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Article ; Online: ETV6-PDGFRB and FIP1L1-PDGFRA stimulate human hematopoietic progenitor cell proliferation and differentiation into eosinophils: the role of nuclear factor-κB.

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