Differential directing of c-Fos and c-Jun proteins to the proteasome in serum-stimulated mouse embryo fibroblasts
| Autor: | Claire Acquaviva, Marc Piechaczyk, Isabelle Jariel-Encontre, Catherine Salvat, Satoshi Omura |
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| Přispěvatelé: | Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Maladies Héréditaires du Métabolisme, Centre de Biologie et pathologie Est |
| Rok vydání: | 1998 |
| Předmět: |
Cancer Research
Proteasome Endopeptidase Complex Proto-Oncogene Proteins c-jun Proteolysis Ubiquitin-Protein Ligases Cultured Culture Media Cysteine Endopeptidases/*metabolism Embryo c-Fos Resting Phase Cell Cycle S Phase Ligases 03 medical and health sciences Mice 0302 clinical medicine Ubiquitin Multienzyme Complexes Gene expression Genetics medicine Animals [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Fluorescent Antibody Technique Indirect Molecular Biology Transcription factor Cells Cultured 030304 developmental biology 0303 health sciences biology medicine.diagnostic_test Indirect G0 Phase Ligases/biosynthesis/*metabolism Mice Multienzyme Complexes/*metabolism Proteasome Endopeptidase Complex Proto-Oncogene Proteins c-fos/*metabolism Proto-Oncogene Proteins c-jun/*metabolism S Phase Temperature Ubiquitin-Protein Ligases Cell Cycle Temperature 3T3 Cells Animals Blood Calcium-Calmodulin-Dependent Protein Kinases/metabolism Cattle *Cell Cycle Cells Mammalian Fluorescent Antibody Technique 3T3 Cells Cell cycle Embryo Mammalian Molecular biology Culture Media Cysteine Endopeptidases Blood Proteasome 030220 oncology & carcinogenesis Transcription preinitiation complex Calcium-Calmodulin-Dependent Protein Kinases biology.protein Cattle Proto-Oncogene Proteins c-fos |
| Zdroj: | Oncogene Oncogene, Nature Publishing Group, 1998, 17 (3), pp.327--37. ⟨10.1038/sj.onc.1201922⟩ |
| ISSN: | 0950-9232 1476-5594 |
| DOI: | 10.1038/sj.onc.1201922⟩ |
| Popis: | c-Fos and c-Jun proteins are highly unstable transcription factors that heterodimerize within the AP-1 transcription complex. Their accumulation is transiently induced at the beginning of the G0-to-S phase transition in quiescent cells stimulated for growth. To address the mechanisms responsible for rapid clearance of c-Fos and c-Jun proteins under these experimental conditions, we have used the ts20 mouse embryo fibroblasts which express a thermosensitive mutant of the E1 enzyme of the ubiquitin pathway. The use of cell-permeant protease inhibitors indicates that both proteins are degraded by the proteasome and excludes any major contribution for calpains and lysosomes during the G0-to-S phase transition. Synchronisation of ts20 cells at the non permissive temperature blocks the degradation of c-Jun, indicating that this process is E1-dependent. In contrast, c-Fos is broken down according to an apparently E1-independent pathway in ts20 cells, although a role for ubiquitinylation in this process cannot be formally ruled out. Interestingly, c-Jun is highly unstable in c-Fos-null mouse embryo fibroblasts stimulated for growth. Taken together, these observations show that in vivo during a G0-to-S phase transition (i) the precise mechanisms triggering c-Fos and c-Jun directing to the proteasome are not identical, (ii) the presence of c-Fos is not an absolute prerequisite for the degradation of c-Jun and (iii) the degradation of c-Jun is not required for that of c-Fos. |
| Databáze: | OpenAIRE |
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