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  Kinetic Analysis of Protein Stability Reveals Age-Dependent Degradation

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-B69D-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-B69E-A
Genre: Journal Article

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 Creators:
McShane, Erik, Author
Sin, Celine1, Author              
Zauber, Henrik, Author
Wells, Jonathan N., Author
Donnelly, Neysan, Author
Wang, Xi, Author
Hou, Jingyi, Author
Chen, Wei, Author
Storchova, Zuzana, Author
Marsh, Joseph A., Author
Valleriani, Angelo1, Author              
Selbach, Matthias, Author
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1Angelo Valleriani, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863324              

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 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.

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 Dates: 2016-10-062016
 Publication Status: Published in print
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 Identifiers: DOI: 10.1016/j.cell.2016.09.015
BibTex Citekey: McShane2016
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Title: Cell
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 167 (3) Sequence Number: - Start / End Page: 803 - 815.e21 Identifier: ISSN: 0092-8674