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In vivo Interrogation of Central Nervous System Translatome by Polyribosome Fractionation
Published on: April 30, 2014
Interplay between protein synthesis and degradation in the CNS: physiological and pathological implications
Qunxing Ding1, Valentina Cecarini, Jeffrey N Keller
1Department of Anatomy and Neurobiology, and Sanders-Brown Center on Aging, University of Kentucky, Lexington, KY 40536-0230, USA.
Trends in Neurosciences
|November 28, 2006
Summary
Compromised ubiquitin-proteasome system (UPS) function in the CNS may impact protein synthesis, not just protein accumulation. This review explores the interplay between UPS and protein synthesis, crucial for CNS health and disease.
Area of Science:
- Neuroscience
- Molecular Biology
- Cellular Biology
Background:
- The ubiquitin-proteasome system (UPS) is vital for protein homeostasis.
- Compromised UPS function is linked to CNS abnormalities and pathologies.
- Previous assumptions linked UPS dysfunction to protein accumulation.
Purpose of the Study:
- To review evidence for crosstalk between the UPS and protein synthesis pathways.
- To explore the implications of this interplay for CNS physiology and pathology.
Main Methods:
- Literature review of studies investigating UPS function and protein synthesis.
- Analysis of data on the effects of UPS inhibition on protein synthesis.
Main Results:
- Impaired UPS function can directly inhibit protein synthesis.
- The toxicity of UPS inhibition may not solely rely on protein buildup.
- Evidence suggests significant crosstalk between UPS and protein synthesis machinery.
Conclusions:
- Crosstalk between UPS and protein synthesis is a key factor in CNS function.
- Understanding this interplay is crucial for addressing CNS disorders.
- UPS-protein synthesis interactions offer potential therapeutic targets for neurological diseases.
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