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Identification of ubiquitination targets of UHRF1

ABSTRACT: The reversible attachment of ubiquitin governs the interaction, activity and degradation of proteins whereby the type and target of this conjugation determine the biological response. The investigation of this complex and multi-faceted protein ubiquitination mostly relies on painstaking biochemical analyses. Here, we employ recombinant binding domains to identify the UHRF1 dependent ubiquitinated proteins by liquid chromatography tandem mass spectrometry (LC-MS/MS).

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Ignasi Forne

LAB HEAD: Prof. Dr. Heinrich Leonhardt

PROVIDER: PXD034335 | Pride | 2023-01-30

REPOSITORIES: Pride

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Probing protein ubiquitination in live cells.

Qin Weihua W Steinek Clemens C Kolobynina Ksenia K Forné Ignasi I Imhof Axel A Cardoso M Cristina MC Leonhardt Heinrich H

Nucleic acids research 20221101 21

The reversible attachment of ubiquitin governs the interaction, activity and degradation of proteins whereby the type and target of this conjugation determine the biological response. The investigation of this complex and multi-faceted protein ubiquitination mostly relies on painstaking biochemical analyses. Here, we employ recombinant binding domains to probe the ubiquitination of proteins in living cells. We immobilize GFP-fused proteins of interest at a distinct cellular structure and detect ...[more]

PMID: 36189882

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