دورية أكاديمية
Maximum entropy determination of mammalian proteome dynamics.
| العنوان: | Maximum entropy determination of mammalian proteome dynamics. |
|---|---|
| المؤلفون: | Dear AJ; Department of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.; Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom., Garcia GA; Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom., Meisl G; Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom., Collins GA; Department of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.; Department of Biochemistry, Molecular Biology, Entomology & Plant Pathology, Mississippi State University, Starkville, MS 39762., Knowles TPJ; Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.; Cavendish Laboratory, Department of Physics, University of Cambridge, Cambridge CB3 0HE, United Kingdom., Goldberg AL; Department of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115. |
| المصدر: | Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Apr 30; Vol. 121 (18), pp. e2313107121. Date of Electronic Publication: 2024 Apr 23. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, DC : National Academy of Sciences |
| مواضيع طبية MeSH: | Entropy* , Proteome*/metabolism , Proteolysis*, Humans ; Animals ; Bayes Theorem ; Proteostasis ; Kinetics ; Cyclic AMP/metabolism ; TOR Serine-Threonine Kinases/metabolism ; Cyclic GMP/metabolism |
| مستخلص: | Full understanding of proteostasis and energy utilization in cells will require knowledge of the fraction of cell proteins being degraded with different half-lives and their rates of synthesis. We therefore developed a method to determine such information that combines mathematical analysis of protein degradation kinetics obtained in pulse-chase experiments with Bayesian data fitting using the maximum entropy principle. This approach will enable rapid analyses of whole-cell protein dynamics in different cell types, physiological states, and neurodegenerative disease. Using it, we obtained surprising insights about protein stabilities in cultured cells normally and upon activation of proteolysis by mTOR inhibition and increasing cAMP or cGMP. It revealed that >90% of protein content in dividing mammalian cell lines is long-lived, with half-lives of 24 to 200 h, and therefore comprises much of the proteins in daughter cells. The well-studied short-lived proteins (half-lives < 10 h) together comprise <2% of cell protein mass, but surprisingly account for 10 to 20% of measurable newly synthesized protein mass. Evolution thus appears to have minimized intracellular proteolysis except to rapidly eliminate misfolded and regulatory proteins. Competing Interests: Competing interests statement:The authors declare no competing interest. |
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| معلومات مُعتمدة: | R01 GM051923 United States GM NIGMS NIH HHS |
| فهرسة مساهمة: | Keywords: maximum entropy; protein degradation; protein half-lives; proteome; proteostasis |
| المشرفين على المادة: | 0 (Proteome) E0399OZS9N (Cyclic AMP) EC 2.7.11.1 (TOR Serine-Threonine Kinases) H2D2X058MU (Cyclic GMP) |
| تواريخ الأحداث: | Date Created: 20240423 Date Completed: 20240423 Latest Revision: 20240505 |
| رمز التحديث: | 20240505 |
| مُعرف محوري في PubMed: | PMC11067036 |
| DOI: | 10.1073/pnas.2313107121 |
| PMID: | 38652742 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1091-6490 |
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| DOI: | 10.1073/pnas.2313107121 |