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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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			Action	DRS
	SID1638_WQ_UbaE14_B1.RAW	Raw
	SID1638_WQ_UbaE14_B2.RAW	Raw
	SID1638_WQ_UbaE14_B3.RAW	Raw
	SID1638_WQ_UbaE14_B4.RAW	Raw
	SID1638_WQ_UbaE14_B5.RAW	Raw

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Publications

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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