USP45 and Spindly are part of the same complex implicated in cell migration
Abstract Ubiquitylation is a protein modification implicated in several cellular processes. This process is reversible by the action of deubiquinating enzymes (DUBs). USP45 is a ubiquitin specific protease about which little is known, aside from roles in DNA damage repair and differentiation of the...
Guardado en:
Autores principales: | , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/009b0e446c014860a8da9ab01d93189f |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:009b0e446c014860a8da9ab01d93189f |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:009b0e446c014860a8da9ab01d93189f2021-12-02T15:08:54ZUSP45 and Spindly are part of the same complex implicated in cell migration10.1038/s41598-018-32685-82045-2322https://doaj.org/article/009b0e446c014860a8da9ab01d93189f2018-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-32685-8https://doaj.org/toc/2045-2322Abstract Ubiquitylation is a protein modification implicated in several cellular processes. This process is reversible by the action of deubiquinating enzymes (DUBs). USP45 is a ubiquitin specific protease about which little is known, aside from roles in DNA damage repair and differentiation of the vertebrate retina. Here, by using mass spectrometry we have identified Spindly as a new target of USP45. Our data show that Spindly and USP45 are part of the same complex and that their interaction specifically 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 specifically removed by USP45 in its active form but not by the catalytic inactive form. Lastly, we identified a new role for USP45 in cell migration, similar to that which was recently described for Spindly.Claudia ConteEric R. GriffisIan HicksonAna B. Perez-OlivaNature PortfolioarticleUbiquitin ChainsType UbiquitinProtein UbiquitylationUSP14 ActivityDako Mounting MediumMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-13 (2018) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Ubiquitin Chains Type Ubiquitin Protein Ubiquitylation USP14 Activity Dako Mounting Medium Medicine R Science Q |
spellingShingle |
Ubiquitin Chains Type Ubiquitin Protein Ubiquitylation USP14 Activity Dako Mounting Medium Medicine R Science Q Claudia Conte Eric R. Griffis Ian Hickson Ana B. Perez-Oliva USP45 and Spindly are part of the same complex implicated in cell migration |
description |
Abstract Ubiquitylation is a protein modification implicated in several cellular processes. This process is reversible by the action of deubiquinating enzymes (DUBs). USP45 is a ubiquitin specific protease about which little is known, aside from roles in DNA damage repair and differentiation of the vertebrate retina. Here, by using mass spectrometry we have identified Spindly as a new target of USP45. Our data show that Spindly and USP45 are part of the same complex and that their interaction specifically 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 specifically removed by USP45 in its active form but not by the catalytic inactive form. Lastly, we identified a new role for USP45 in cell migration, similar to that which was recently described for Spindly. |
format |
article |
author |
Claudia Conte Eric R. Griffis Ian Hickson Ana B. Perez-Oliva |
author_facet |
Claudia Conte Eric R. Griffis Ian Hickson Ana B. Perez-Oliva |
author_sort |
Claudia Conte |
title |
USP45 and Spindly are part of the same complex implicated in cell migration |
title_short |
USP45 and Spindly are part of the same complex implicated in cell migration |
title_full |
USP45 and Spindly are part of the same complex implicated in cell migration |
title_fullStr |
USP45 and Spindly are part of the same complex implicated in cell migration |
title_full_unstemmed |
USP45 and Spindly are part of the same complex implicated in cell migration |
title_sort |
usp45 and spindly are part of the same complex implicated in cell migration |
publisher |
Nature Portfolio |
publishDate |
2018 |
url |
https://doaj.org/article/009b0e446c014860a8da9ab01d93189f |
work_keys_str_mv |
AT claudiaconte usp45andspindlyarepartofthesamecompleximplicatedincellmigration AT ericrgriffis usp45andspindlyarepartofthesamecompleximplicatedincellmigration AT ianhickson usp45andspindlyarepartofthesamecompleximplicatedincellmigration AT anabperezoliva usp45andspindlyarepartofthesamecompleximplicatedincellmigration |
_version_ |
1718387978844241920 |