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TRIM25 targets p300 for degradation

S. Elabd,Eleonora Pauletto,Valeria Solozobova,Nils Eickhoff,Nuno Padrão,W. Zwart,Christine Blattner

Published 2023 in Life Science Alliance

ABSTRACT

Here, it is shown that the E3 protein TRIM25 targets the transcriptional co-activator p300 in an ubiquitin-independent manner for proteasomal degradation involving the motor protein dynein. p300 is an important transcriptional co-factor. By stimulating the transfer of acetyl residues onto histones and several key transcription factors, p300 enhances transcriptional initiation and impacts cellular processes including cell proliferation and cell division. Despite its importance for cellular homeostasis, its regulation is poorly understood. We show that TRIM25, a member of the TRIM protein family, targets p300 for proteasomal degradation. However, despite TRIM25’s RING domain and E3 activity, degradation of p300 by TRIM25 is independent of TRIM25-mediated p300 ubiquitination. Instead, TRIM25 promotes the interaction of p300 with dynein, which ensures a microtubule-dependent transport of p300 to cellular proteasomes. Through mediating p300 degradation, TRIM25 affects p300-dependent gene expression.

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