Proteomics

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A family of unconventional deubiquitinases with modular chain specificity determinants

ABSTRACT: Interactors of human ZUFSP in HEK-293T cells. Flp-in T-REx 293 cells with stable 3xFLAG-ZUFSP integration were assayed for ZUFSP interactors under three different conditions: i) Cells expressing wild-type ZUFSP, ii) Cells expressing catalytically inactive ZUFSP, iii) Cells expressing wild-type ZUFSP with additional treatment by an unspecific nuclease (Benzonase) during purification.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

SUBMITTER: Kay Hofmann  

LAB HEAD: Kay Hofmann

PROVIDER: PXD008731 | Pride | 2018-04-06

REPOSITORIES: Pride

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20161124_UC_ColID_251_ThomasHermanns_Hofmann_ProjID_278_IP_TH_Z1.raw Raw
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20161124_UC_ColID_251_ThomasHermanns_Hofmann_ProjID_278_IP_TH_Z3.raw Raw
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A family of unconventional deubiquitinases with modular chain specificity determinants.

Hermanns Thomas T   Pichlo Christian C   Woiwode Ilka I   Klopffleisch Karsten K   Witting Katharina F KF   Ovaa Huib H   Baumann Ulrich U   Hofmann Kay K  

Nature communications 20180223 1

Deubiquitinating enzymes (DUBs) regulate ubiquitin signaling by trimming ubiquitin chains or removing ubiquitin from modified substrates. Similar activities exist for ubiquitin-related modifiers, although the enzymes involved are usually not related. Here, we report human ZUFSP (also known as ZUP1 and C6orf113) and fission yeast Mug105 as founding members of a DUB family different from the six known DUB classes. The crystal structure of human ZUFSP in covalent complex with propargylated ubiquiti  ...[more]

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