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Lookup NU author(s): Professor Ian HicksonORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Ubiquitylation is a protein modifcation implicated in several cellular processes. This process is reversible by the action of deubiquinating enzymes (DUBs). USP45 is a ubiquitin specifc protease about which little is known, aside from roles in DNA damage repair and diferentiation of the vertebrate retina. Here, by using mass spectrometry we have identifed Spindly as a new target of USP45. Our data show that Spindly and USP45 are part of the same complex and that their interaction specifcally depends on the catalytic activity of USP45. In addition, we describe the type of ubiquitin chains associated with the complex that can be cleaved by USP45, with a preferential activity on K48 ubiquitin chain type and potentially K6. Here, we also show that Spindly is mono-ubiquitylated and this can be specifcally removed by USP45 in its active form but not by the catalytic inactive form. Lastly, we identifed a new role for USP45 in cell migration, similar to that which was recently described for Spindly.
Author(s): Conte C, Griffis ER, Hickson I, Perez-Oliva AB
Publication type: Article
Publication status: Published
Journal: Scientific Reports
Year: 2018
Volume: 8
Pages: 14375
Print publication date: 26/09/2018
Online publication date: 26/09/2018
Acceptance date: 11/09/2018
Date deposited: 27/09/2018
ISSN (electronic): 2045-2322
Publisher: Nature Research
URL: https://doi.org/10.1038/s41598-018-32685-8
DOI: 10.1038/s41598-018-32685-8
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