Abstract

The abundance of cellular proteins is determined largely by the rate of transcription and translation coupled with the stability of individual proteins. Although we know a great deal about global transcript abundance, little is known about global protein stability. We present a highly parallel multiplexing strategy to monitor protein turnover on a global scale by coupling flow cytometry with microarray technology to track the stability of individual proteins within a complex mixture. We demonstrated the feasibility of this approach by measuring the stability of ∼8000 human proteins and identifying proteasome substrates. The technology provides a general platform for proteome-scale analysis of protein turnover under various physiological and disease conditions.

Keywords

ProteomeProteasomeProtein stabilityProtein turnoverComputational biologyUbiquitinProteomicsFlow cytometryBiologyTranscription (linguistics)Cell biologyProtein degradationProtein–protein interactionProtein biosynthesisBioinformaticsMolecular biologyBiochemistryGene

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Year
2008
Type
article
Volume
322
Issue
5903
Pages
918-923
Citations
478
Access
Closed

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Hsueh-Chi S. Yen, Qikai Xu, Danny M. Chou et al. (2008). Global Protein Stability Profiling in Mammalian Cells. Science , 322 (5903) , 918-923. https://doi.org/10.1126/science.1160489

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DOI
10.1126/science.1160489