Proteomics

Dataset Information

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An interaction landscape of ubiquitin signaling


ABSTRACT: This project paper describes, for the first time, a global, proteome-wide interaction screening for ubiquitin signaling. Our data reveals both cell type dependent and independent diubiquitin interactions. In additon, we show that certain proteins more potently bind to K6 diubiquitin upon induction of DNA damage.

INSTRUMENT(S): LTQ FT, Q Exactive

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: Xiaofei Zhang  

LAB HEAD: Michiel Vermeulen

PROVIDER: PXD004185 | Pride | 2017-02-08

REPOSITORIES: Pride

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Publications


Intracellular signaling via the covalent attachment of different ubiquitin linkages to protein substrates is fundamental to many cellular processes. Although linkage-selective ubiquitin interactors have been studied on a case-by-case basis, proteome-wide analyses have not been conducted yet. Here, we present ubiquitin interactor affinity enrichment-mass spectrometry (UbIA-MS), a quantitative interaction proteomics method that makes use of chemically synthesized diubiquitin to enrich and identify  ...[more]

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