Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome.

ABSTRACT: Recognition of specific substrates for degradation by the ubiquitin-proteasome pathway is ensured by a cascade of ubiquitin transferases E1, E2 and E3. The mechanism by which the target proteins are transported to the proteasome is not clear, but two yeast E3s and one mammalian E3 ligase seem to be involved in the delivery of targets to the proteasome, by escorting them and by binding to the 19 S regulatory particle of the proteasome. In the present study, we show that SNEV (senescence evasion factor), a protein with in vitro E3 ligase activity, which is also involved in DNA repair and splicing, associates with the proteasome by directly binding to the beta7 subunit of the 20 S proteasome. Upon inhibition of proteasome activity, SNEV does not accumulate within the cells although its co-loc

SUBMITTER: Loscher M 

PROVIDER: S-EPMC1138967 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature