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Kinetic analysis of protein stability reveals age-dependent degradation

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Sin,  Celine
Angelo Valleriani, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Valleriani,  Angelo
Angelo Valleriani, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

McShane, E., Sin, C., Zauber, H., Wells, J., Donnelly, N., Wang, X., et al. (2016). Kinetic analysis of protein stability reveals age-dependent degradation. Cell, 167(3), 803-815.e21. doi:10.1016/j.cell.2016.09.015.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-B69D-C
Abstract
Do young and old protein molecules have the same probability to be degraded? We addressed this question using metabolic pulse-chase labeling and quantitative mass spectrometry to obtain degradation profiles for thousands of proteins. We find that gt;10 of proteins are degraded non-exponentially. Specifically, proteins are less stable in the first few hours of their life and stabilize with age. Degradation profiles are conserved and similar in two cell types. Many non-exponentially degraded (NED) proteins are subunits of complexes that are produced in super-stoichiometric amounts relative to their exponentially degraded (ED) counterparts. Within complexes, \NED\} proteins have larger interaction interfaces and assemble earlier than \{ED\} subunits. Amplifying genes encoding \{NED\ proteins increases their initial degradation. Consistently, decay profiles can predict protein level attenuation in aneuploid cells. Together, our data show that non-exponential degradation is common, conserved, and has important consequences for complex formation and regulation of protein abundance.