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Related Concept Videos

The Unfolded Protein Response01:37

The Unfolded Protein Response

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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The Proteasome01:13

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Protein Networks02:26

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
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How does the neuronal proteostasis network react to cellular cues?

Ki Hong Nam1, Alban Ordureau1

  • 1Cell Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY 10065, U.S.A.

Biochemical Society Transactions
|March 15, 2024
PubMed
Summary
This summary is machine-generated.

Neurons maintain cellular balance through protein synthesis and degradation. This review examines how neurons adapt their proteome to stress, a process impaired in neurodegenerative diseases like Parkinson's.

Keywords:
ISRUPRautophagyneuronsnutrient stressproteome

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Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons
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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Neurons, despite being post-mitotic, require continuous protein synthesis for organelle maintenance and energy-intensive functions like neurotransmitter production and redox homeostasis.
  • Cellular homeostasis in neurons depends on the balance between mRNA transcription-translation and protein degradation pathways (autophagy, proteasome).
  • Neuronal stress response mechanisms are crucial for survival, involving proteome adaptation.

Purpose of the Study:

  • To review neuronal proteome adaptation in response to cellular stress.
  • To focus on proteins involved in autophagy, stress response pathways, and neurotransmitters.
  • To highlight the impairment of these adaptive processes in neurodegenerative disorders such as Parkinson's disease.

Main Methods:

  • Literature review of studies on neuronal stress response.
  • Analysis of proteins involved in proteostasis, autophagy, and neurotransmitter metabolism.
  • Examination of impaired stress coping mechanisms in neurodegenerative conditions.

Main Results:

  • Neurons adapt their proteome under stress, primarily through regulating protein synthesis and degradation.
  • Autophagy and stress response pathways are key to neuronal survival during nutrient stress.
  • Impairment of these adaptive mechanisms contributes to neurodegeneration.

Conclusions:

  • Neuronal proteome adaptation is vital for maintaining cellular homeostasis under stress.
  • Dysfunctional stress response pathways are implicated in neurodegenerative diseases.
  • Understanding these adaptations offers potential therapeutic targets for neuroprotection.