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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Neuronal and synaptic protein lifetimes.

Laurie D Cohen1, Noam E Ziv1

  • 1Technion Faculty of Medicine, Rappaport Institute and Network Biology Research Laboratories, Fishbach Building, Technion City, Haifa, 32000, Israel.

Current Opinion in Neurobiology
|January 25, 2019
PubMed
Summary
This summary is machine-generated.

Neurons maintain protein balance (proteostasis) with unusually long protein lifetimes, lasting days to months. These long-lived neuronal proteins are crucial for synaptic function and are longer-lived in vivo than in cell culture.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Neuronal proteostasis faces unique challenges due to complex neuron architecture and synaptic demands.
  • Understanding protein turnover is key to deciphering how neurons maintain function.

Purpose of the Study:

  • To estimate the lifetimes of neuronal and synaptic proteins.
  • To investigate factors influencing neuronal protein half-lives.

Main Methods:

  • Utilized advances in proteomics and mass spectrometry.
  • Enabled comprehensive lifetime estimations for thousands of proteins.

Main Results:

  • Neuronal and synaptic proteins exhibit unusually long half-lives (days to weeks, months).
  • In vivo half-lives are significantly longer than in cell culture.
  • Protein lifetimes correlate with developmental stage, molecular complexes, and potentially activity levels.

Conclusions:

  • Long protein half-lives are a critical strategy for neuronal proteostasis.
  • In vivo conditions profoundly influence neuronal protein stability.
  • Further research into environmental and activity-dependent regulation is warranted.