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.

Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: Nature Publishing Group 2019-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-08231-5
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spelling 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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