Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity
Deubiquitinating enzymes (DUBs) are critical regulators of cellular processes by removing ubiquitin from specific targets. Here global kinetic modelling reveals the mechanism by which the low intrinsic activity of USP7 is substantially enhanced on a specific physiological target.
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2019-01-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-018-08231-5 |
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doaj-822bd4cb8eb04f3199afc82488ed53d32021-05-11T11:42:20ZengNature Publishing GroupNature Communications2041-17232019-01-0110111610.1038/s41467-018-08231-5Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activityRobbert Q. Kim0Paul P. Geurink1Monique P. C. Mulder2Alexander Fish3Reggy Ekkebus4Farid El Oualid5Willem J. van Dijk6Duco van Dalen7Huib Ovaa8Hugo van Ingen9Titia K. Sixma10Division of Biochemistry and Oncode Institute, Netherlands Cancer InstituteDivision of Cell Biology II, Netherlands Cancer InstituteDivision of Cell Biology II, Netherlands Cancer InstituteDivision of Biochemistry and Oncode Institute, Netherlands Cancer InstituteDivision of Cell Biology II, Netherlands Cancer InstituteUbiQ Bio BV, Science Park 408Division of Biochemistry and Oncode Institute, Netherlands Cancer InstituteDivision of Cell Biology II, Netherlands Cancer InstituteDivision of Cell Biology II, Netherlands Cancer InstituteMacromolecular Biochemistry, Leiden Institute of Chemistry, Leiden UniversityDivision of Biochemistry and Oncode Institute, Netherlands Cancer InstituteDeubiquitinating enzymes (DUBs) are critical regulators of cellular processes by removing ubiquitin from specific targets. Here global kinetic modelling reveals the mechanism by which the low intrinsic activity of USP7 is substantially enhanced on a specific physiological target.https://doi.org/10.1038/s41467-018-08231-5 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Robbert Q. Kim Paul P. Geurink Monique P. C. Mulder Alexander Fish Reggy Ekkebus Farid El Oualid Willem J. van Dijk Duco van Dalen Huib Ovaa Hugo van Ingen Titia K. Sixma |
spellingShingle |
Robbert Q. Kim Paul P. Geurink Monique P. C. Mulder Alexander Fish Reggy Ekkebus Farid El Oualid Willem J. van Dijk Duco van Dalen Huib Ovaa Hugo van Ingen Titia K. Sixma Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity Nature Communications |
author_facet |
Robbert Q. Kim Paul P. Geurink Monique P. C. Mulder Alexander Fish Reggy Ekkebus Farid El Oualid Willem J. van Dijk Duco van Dalen Huib Ovaa Hugo van Ingen Titia K. Sixma |
author_sort |
Robbert Q. Kim |
title |
Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity |
title_short |
Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity |
title_full |
Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity |
title_fullStr |
Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity |
title_full_unstemmed |
Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity |
title_sort |
kinetic analysis of multistep usp7 mechanism shows critical role for target protein in activity |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2019-01-01 |
description |
Deubiquitinating enzymes (DUBs) are critical regulators of cellular processes by removing ubiquitin from specific targets. Here global kinetic modelling reveals the mechanism by which the low intrinsic activity of USP7 is substantially enhanced on a specific physiological target. |
url |
https://doi.org/10.1038/s41467-018-08231-5 |
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