Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome

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Jariel-Encontre, I. | Pariat, M. | Martin, F. | Carillo, S. | Salvat, C. | Piechaczyk, Marc

Edité par CCSD ; American Society for Biochemistry and Molecular Biology -

International audience. Degradation of rapidly turned over cellular proteins is commonly thought to be energy dependent, to require tagging of protein substrates by multi-ubiquitin chains, and to involve the 26 S proteasome, which is the major neutral proteolytic activity in both the cytosol and the nucleus. The c-Jun oncoprotein is very unstable in vivo. Using cell-free degradation assays, we show that ubiquitinylation, along with other types of tagging, is not an absolute prerequisite for ATP-dependent degradation of c-Jun by the 26 S proteasome. This indicates that a protein may bear intrinsic structural determinants allowing its selective recognition and breakdown by the 26 S proteasome. Moreover, taken together with observations by different groups, our data point to the notion of the existence of multiple degradation pathways operating on c-Jun.

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