MARK4 interaction modulates the dynamic subcellular localization of USP21 deubiquitinase

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Published 18-11-2021
DOI https://doi.org/10.1387/ekaia.22644
Iraia García-Santisteban
Genetika, Antropologia Fisikoa eta Animalien Fisiologia Saila (UPV/EHU), Leioa Biocruces-Bizkaia Osasun Ikerketa Institutua, Barakaldo
https://orcid.org/0000-0002-7912-385X

Anne Olazabal-Herrero
Department of Oncology, Georgetown University, Washington, DC Department of Internal Medicine, Yale University School of Medicine, New Haven, CT
Jose Antonio Rodríguez
Genetika, Antropologia Fisikoa eta Animalien Fisiologia Saila (UPV/EHU), Leioa
https://orcid.org/0000-0002-2823-3733

Abstract

The deubiquitinase USP21 shuttles between the nucleus and the cytoplasm and can also localize to the centrosome, but how this complex subcellular localization is modulated remains unknown. A proteomics analysis has identified the centrosomal kinase MARK4 as a potential USP21-interacting partner. In this work, we validate the USP21/MARK4 interaction, identifying the MARK4-binding region of USP21. Our results indicate that MARK4 interaction may regulate USP21 nucleocytoplasmic shuttling dynamics, increasing its retention in the cytoplasm. On the other hand, our data show that the centrosomal localization of both proteins is highly dynamic, and suggest that USP21 centrosomal dynamics might be modulated by MARK4.

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Issue
No. 42 (2022): EKAIA 42
Section
Ale Arrunta
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