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TRIM25 targets p300 for degradation

Elabd, Seham; Pauletto, Eleonora; Solozobova, Valeria ; Eickhoff, Nils; Padrao, Nuno; Zwart, Wilbert; Blattner, Christine ORCID iD icon 1
1 Institut für Biologische und Chemische Systeme (IBCS), Karlsruher Institut für Technologie (KIT)

Abstract:

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.


Verlagsausgabe §
DOI: 10.5445/IR/1000164320
Veröffentlicht am 14.11.2023
Cover der Publikation
Zugehörige Institution(en) am KIT Institut für Biologische und Chemische Systeme (IBCS)
Publikationstyp Zeitschriftenaufsatz
Publikationsmonat/-jahr 12.2023
Sprache Englisch
Identifikator ISSN: 2575-1077
KITopen-ID: 1000164320
HGF-Programm 47.14.02 (POF IV, LK 01) Information Storage and Processing in the Cell Nucleus
Erschienen in Life Science Alliance
Verlag Life Science Alliance
Band 6
Heft 12
Seiten e202301980
Bemerkung zur Veröffentlichung Gefördert durch den KIT-Publikationsfonds
Vorab online veröffentlicht am 28.09.2023
Nachgewiesen in Scopus
Web of Science
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