c-Fos proto-oncoprotein defines a family of closely related transcription factors (Fos proteins) also comprising Fra-1, Fra-2, FosB and ΔFosB, the latter two proteins being generated by alternative splicing. Through the regulation of many genes, most of them still unidentified, they regulate major functions from the cell level up to the whole organism. Thus they are involved in the control of proliferation, differentiation and apoptosis, as well as in the control of responses to stresses, and they play important roles in organogenesis, immune responses and control of cognitive functions, among others. Fos proteins are intrinsically unstable. We have studied how two of them, c-Fos and Fra-1, are degraded. Departing from the classical scenario where unstable key cell regulators are hydrolysed by the proteasome after polyubiquitination, we showed that the bulk of c-Fos and Fra-1 can be broken down independently of any prior ubiquitination. Certain conserved structural domains suggest that similar mechanisms may also apply to Fra-2 and FosB. Computer search indicates that certain motifs shared by the Fos proteins and putatively responsible for instability are found in no other protein, suggesting the existence of degradation mechanisms specific for this protein family. Under particular signalling conditions, others have shown that a part of cytoplasmic c-Fos requires ubiquitination for fast turnover. This poses the question of the multiplicity of degradation pathways that apply to proteins depending on their intracellular localization.
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October 2008
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Conference Article|
September 19 2008
Fos family protein degradation by the proteasome
Tiphanie Gomard;
Tiphanie Gomard
1Institut de Génétique Moléculaire de Montpellier, CNRS, Universités Montpellier I et II, UMR 5535, IFR 122, 1919 Route de Mende, Montpellier F-34293, France
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Isabelle Jariel-Encontre;
Isabelle Jariel-Encontre
1Institut de Génétique Moléculaire de Montpellier, CNRS, Universités Montpellier I et II, UMR 5535, IFR 122, 1919 Route de Mende, Montpellier F-34293, France
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Jihane Basbous;
Jihane Basbous
1Institut de Génétique Moléculaire de Montpellier, CNRS, Universités Montpellier I et II, UMR 5535, IFR 122, 1919 Route de Mende, Montpellier F-34293, France
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Guillaume Bossis;
Guillaume Bossis
1Institut de Génétique Moléculaire de Montpellier, CNRS, Universités Montpellier I et II, UMR 5535, IFR 122, 1919 Route de Mende, Montpellier F-34293, France
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Gabriel Mocquet-Torcy;
Gabriel Mocquet-Torcy
1Institut de Génétique Moléculaire de Montpellier, CNRS, Universités Montpellier I et II, UMR 5535, IFR 122, 1919 Route de Mende, Montpellier F-34293, France
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Marc Piechaczyk
Marc Piechaczyk
1
1Institut de Génétique Moléculaire de Montpellier, CNRS, Universités Montpellier I et II, UMR 5535, IFR 122, 1919 Route de Mende, Montpellier F-34293, France
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
March 03 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem Soc Trans (2008) 36 (5): 858–863.
Article history
Received:
March 03 2008
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A correction has been published:
Fos family protein degradation by the proteasome
Citation
Tiphanie Gomard, Isabelle Jariel-Encontre, Jihane Basbous, Guillaume Bossis, Gabriel Mocquet-Torcy, Marc Piechaczyk; Fos family protein degradation by the proteasome. Biochem Soc Trans 1 October 2008; 36 (5): 858–863. doi: https://doi.org/10.1042/BST0360858
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