A 'liaison dangereuse' between AUF1/hnRNPD and the oncogenic tyrosine kinase NPM-ALK
Autor: | Bernard Monsarrat, Severine Ollier, Henri Dupont, Florence Armstrong, Mohamad Fawal, Dominique Morello, Georges Delsol, Christian Touriol, Bernard Payrastre |
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Přispěvatelé: | Groupe d'analyse et de théorie économique ( GATE ), Université Lumière - Lyon 2 ( UL2 ) -Ecole Normale Supérieure Lettres et Sciences Humaines-Centre National de la Recherche Scientifique ( CNRS ), Centre de REcherches sur les Stratégies Economiques - UFC ( CRESE ), Université Bourgogne Franche-Comté ( UBFC ) -Université de Franche-Comté ( UFC ), Institut de pharmacologie et de biologie structurale ( IPBS ), Université Paul Sabatier - Toulouse 3 ( UPS ) -Centre National de la Recherche Scientifique ( CNRS ), Centre de Physiopathologie Toulouse Purpan, Université Paul Sabatier - Toulouse 3 ( UPS ) -IFR30-IFR150-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Groupe d'analyse et de théorie économique (GATE), Université Lumière - Lyon 2 (UL2)-Ecole Normale Supérieure Lettres et Sciences Humaines (ENS LSH)-Centre National de la Recherche Scientifique (CNRS), Centre de REcherches sur les Stratégies Economiques (EA 3190) (CRESE), Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Institut de pharmacologie et de biologie structurale (IPBS), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Centre de Physiopathologie Toulouse Purpan (CPTP), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de REcherches sur les Stratégies Economiques (UR 3190) (CRESE), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) |
Jazyk: | angličtina |
Rok vydání: | 2006 |
Předmět: |
MESH: Cell Death
MESH : Molecular Sequence Data MESH : RNA Messenger Oncogene Proteins Fusion MESH : NIH 3T3 Cells Genes myc MESH: Amino Acid Sequence MESH : Models Biological MESH : Oncogene Proteins Fusion Biochemistry Mice MESH : Phosphorylation 0302 clinical medicine hemic and lymphatic diseases Anaplastic lymphoma kinase MESH: Animals MESH: Lymphoma Large-Cell RNA Neoplasm Heterogeneous-Nuclear Ribonucleoprotein D Phosphorylation Anaplastic large-cell lymphoma 0303 health sciences Cell Death integumentary system Kinase MESH : Amino Acid Sequence Hematology Protein-Tyrosine Kinases Cell biology MESH : Genes myc 030220 oncology & carcinogenesis Lymphoma Large B-Cell Diffuse Signal transduction MESH : Transfection Tyrosine kinase Immunology Molecular Sequence Data MESH : Cyclins Biology MESH : Heterogeneous-Nuclear Ribonucleoprotein D Transfection Models Biological MESH: Protein-Tyrosine Kinases 03 medical and health sciences Cyclins MESH : Mice medicine MESH : Protein-Tyrosine Kinases Animals Humans Heterogeneous Nuclear Ribonucleoprotein D0 [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence RNA Messenger MESH: Mice MESH : Lymphoma Large-Cell [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology MESH: Genes myc 030304 developmental biology MESH: RNA Messenger MESH: Heterogeneous-Nuclear Ribonucleoprotein D MESH: Molecular Sequence Data MESH: Humans MESH: Phosphorylation Cell growth MESH: Transfection MESH : Humans MESH: Models Biological Cell Biology medicine.disease MESH: RNA Neoplasm MESH: Cyclins Fusion protein MESH : RNA Neoplasm MESH : Cell Death NIH 3T3 Cells MESH : Animals MESH: NIH 3T3 Cells MESH: Oncogene Proteins Fusion |
Zdroj: | Blood Blood, American Society of Hematology, 2006, 108 (8), pp.2780-8. 〈10.1182/blood-2006-04-014902〉 Blood, American Society of Hematology, 2006, 108 (8), pp.2780-8. ⟨10.1182/blood-2006-04-014902⟩ Blood, 2006, 108 (8), pp.2780-8. ⟨10.1182/blood-2006-04-014902⟩ |
ISSN: | 0006-4971 1528-0020 |
DOI: | 10.1182/blood-2006-04-014902〉 |
Popis: | Nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) is a chimeric protein expressed in a subset of cases of anaplastic large cell lymphoma (ALCL) for which constitutive expression represents a key oncogenic event. The ALK signaling pathway is complex and probably involves functional redundancy between various signaling substrates of ALK. Despite numerous studies on signaling mediators, the molecular mechanisms contributing to the distinct oncogenic features of NPM-ALK remain incompletely understood. The search for additional interacting partners of NPM-ALK led to the discovery of AUF1/hnRNPD, a protein implicated in AU-rich element (ARE)-directed mRNA decay. AUF1 was immunoprecipitated with ALK both in ALCL-derived cells and in NIH3T3 cells stably expressing NPM-ALK or other X-ALK fusion proteins. AUF1 and NPM-ALK were found concentrated in the same cytoplasmic foci, whose formation required NPM-ALK tyrosine kinase activity. AUF1 was phosphorylated by ALK in vitro and was hyperphosphorylated in NPM-ALK-expressing cells. Its hyperphosphorylation was correlated with increased stability of several AUF1 target mRNAs encoding key regulators of cell proliferation and with increased cell survival after transcriptional arrest. Thus, AUF1 could function in a novel pathway mediating the oncogenic effects of NPM-ALK. Our data establish an important link between oncogenic kinases and mRNA turnover, which could constitute a critical aspect of tumorigenesis. |
Databáze: | OpenAIRE |
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