pSILAC mass spectrometry reveals ZFP91 as IMiD-dependent substrate of the CRL4CRBN ubiquitin ligase

Jian An; Charles M. Ponthier; Ragna Sack; Jan Seebacher; Michael B. Stadler; Katherine A. Donovan; Eric S. Fischer

doi:10.1038/ncomms15398

Nature Communications (May 2017)

pSILAC mass spectrometry reveals ZFP91 as IMiD-dependent substrate of the CRL4CRBN ubiquitin ligase

Jian An,
Charles M. Ponthier,
Ragna Sack,
Jan Seebacher,
Michael B. Stadler,
Katherine A. Donovan,
Eric S. Fischer

Affiliations

Jian An: Department of Cancer Biology, Dana-Farber Cancer Institute
Charles M. Ponthier: Department of Cancer Biology, Dana-Farber Cancer Institute
Ragna Sack: Friedrich Miescher Institute for Biomedical Research
Jan Seebacher: Friedrich Miescher Institute for Biomedical Research
Michael B. Stadler: Friedrich Miescher Institute for Biomedical Research
Katherine A. Donovan: Department of Cancer Biology, Dana-Farber Cancer Institute
Eric S. Fischer: Department of Cancer Biology, Dana-Farber Cancer Institute

DOI: https://doi.org/10.1038/ncomms15398
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 11

Abstract

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Targeting therapeutically-relevant proteins for degradation is an emerging paradigm in drug discovery. Here the authors describe a sensitive pulse SILAC mass spectrometry-based proteomics approach that reports global changes in protein stability following drug treatment in a single time point experiment.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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