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
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