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Article Dans Une Revue Journal of Biological Chemistry Année : 1995

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

Résumé

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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hal-02192665 , version 1 (27-05-2021)

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I. Jariel-Encontre, M. Pariat, F. Martin, S. Carillo, C. Salvat, et al.. Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome. Journal of Biological Chemistry, 1995, 270 (19), pp.11623-11627. ⟨10.1074/jbc.270.19.11623⟩. ⟨hal-02192665⟩
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