PRAM-1 potentiates arsenic trioxide-induced JNK activation
| Autor: | Arndt Benecke, Pierre G. Lutz, Ivo P. Touw, Frédéric M. Denis, Yolande Di Gioia, Yvon E. Cayre |
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| Přispěvatelé: | Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Hematology |
| Rok vydání: | 2005 |
| Předmět: |
Acute promyelocytic leukemia
[SDV]Life Sciences [q-bio] Retinoic acid Tretinoin Cysteine Proteinase Inhibitors Biochemistry SH3 domain Arsenicals src Homology Domains 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Arsenic Trioxide Leukemia Promyelocytic Acute Cell Line Tumor medicine Humans Arsenic trioxide Molecular Biology Caspase 030304 developmental biology Adaptor Proteins Signal Transducing 0303 health sciences biology Kinase Caspase 3 Microfilament Proteins JNK Mitogen-Activated Protein Kinases Proteins Oxides Cell Biology medicine.disease Molecular biology Enzyme Activation Kinetics chemistry 030220 oncology & carcinogenesis Caspases biology.protein Signal transduction Oligopeptides Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280 (10), pp.9043-9048. ⟨10.1074/jbc.M413564200⟩ Journal of Biological Chemistry, 280(10), 9043-9048. American Society for Biochemistry and Molecular Biology Inc. |
| ISSN: | 1083-351X 0021-9258 |
| DOI: | 10.1074/jbc.M413564200 |
| Popis: | International audience; The promyelocytic leukemia RARalpha target gene encoding an adaptor molecule-1 (PRAM-1) is involved in a signaling pathway induced by retinoic acid in acute promyelocytic leukemia (APL) cells. To better understand the function of PRAM-1, we have undertaken the identification of its partners through a yeast two-hybrid screen. Here, we show that the proline-rich domain of PRAM-1 interacted with the Src homology 3 (SH3) domain of hematopoietic progenitor kinase 1 (HPK-1)-interacting protein of 55 kDa (HIP-55, also called SH3P7 and Abp1) known to stimulate the activity of HPK-1 and c-Jun N-terminal kinase (JNK). Overexpression of PRAM-1 in the NB4 APL cell line increased arsenic trioxide-induced JNK activation through a caspase 3-like-dependent activity. Dissociation of the SH3 domain from the rest of the HIP-55 protein was observed in the NB4 APL cell line treated with arsenic trioxide due to specific cleavage by caspase 3-like enzymes. The cleavage of HIP-55 correlated with the induction of PRAM-1 mRNA and protein expression. Taken together, our results suggest that the caspase 3-cleaved SH3 domain of HIP-55 is likely involved in PRAM-1-mediated JNK activation upon arsenic trioxide-induced differentiation of NB4 cells. |
| Databáze: | OpenAIRE |
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