Protein Folding in Neurons

Introduction of Peroxisomes

The shape determines the function of the protein, and the amino acid sequence contains the essential information about protein folding. As a vital cellular process, the protein folding always occurs in the endoplasmic reticulum. In the complex cellular environment contain proteins, nucleotides, lipids, sugars, and organelles, proteins can easily misfold and aggregate. The unfolded protein response (UPR) is a sensitive system to prevent the cellular stress caused by the problems of protein folding. However, severe stress can also overwhelm the UPR and result in abnormal cellular function. For example, the prion is an abnormally folded protein that can change the other proteins’ shape in its path and finally damaging brains in this process. It has also been reported that other major degenerative neurological diseases, such as Parkinson’s, Alzheimer’s, Huntington’s, and amyotrophic lateral sclerosis, are associated with protein folding.

Levels of Protein Folding

For most proteins, there are only one or two correct shapes and almost countless different ways of misfolding. In fact, the protein must have very exact structures for specific molecules’ interaction and chemical reactions.

• Primary Structure- The sequence of amino acids derived from the DNA sequence.
• Secondary Structure- Partial folding of amino acids to form local substructures, including α Helix and β Sheets.
• Tertiary Structure- The completed three-dimensional structure.
• Quaternary Structure- Large proteins composed of multiple pieces with a larger structure.

Molecular Chaperones-Mediated Protein Folding

To avoid the inappropriate interactions between polypeptides, a class of proteins named molecular chaperones has evolved to promote the refolding of the misfolded protein and further enhance the efficiency of de novo protein folding. In fact, the molecular chaperones are almost heat shock proteins (HSPs) to degrade unfold proteins according to interaction with components of the ubiquitin-proteasome pathway and lysosome-mediated autophagy.

In neurons, the protein folding mediated by molecular chaperones plays a key role in brain functions and neurodegenerative diseases. The studies have shown that molecular chaperones are promising targets for the treatment of neurodegenerative diseases. However, upregulation of molecular chaperones might result in undesirable side effects, such as cancer.

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