Lecture 8 Physiological Regulation of Protein Degradation

Lecture 8 Physiological Regulation of Protein Degradation -...

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IPHY 3060 Lecture 8: Physiological Regulation of Protein Degradation
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Key Points from Before: Proteins consist of chains of amino acids The amount of protein can be regulated to regulate cell size
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Key Point #1: Protein degradation can also be regulated to change cell size
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Protein Degradation:
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Protein Degradation: The process of breaking down old, damaged or unneeded proteins
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Main functions of protein degradation Eliminate old, worn out proteins Eliminate mutant, truncated, or misfolded proteins Regulate the total amount of protein
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Protein degradation is carried out by proteases: Proteins that break down other proteins
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Main protein degradation pathways in cells: Ubiquitin-mediated proteasomal degradation most quantitatively important Calpain mediated degradation Caspase mediated degradation Lysosomal degradation
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Ubiquitin-Mediated Proteasomal Degradation
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Ubiquitin-mediated proteasomal degradation requires 3 components Ubiquitin : A small peptide that when linked to a protein can allow proteases to recognize it and degrade it Ubiquitin activating enzymes —proteins that transfer ubiquitin onto the protein to be degraded Proteasome —large protein complex containing proteases that recognizes ubiquitinated proteins Proteasome
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The Ubiquitin-Mediated Protein Degradation Pathway Step 1: ubiquitin is added to E1 and E2 ubiquitin activating enzymes
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The Ubiquitin-Mediated Protein Degradation Pathway Step 1: ubiquitin is activated by binding to E1 and E2 ubiquitin activating enzymes Step 2: ubiquitin is added to lysine residues on protein by E3 ubiquitin ligase
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The Ubiquitin-Mediated Protein Degradation Pathway Step 1: ubiquitin is activated by binding to E1 and E2 ubiquitin activating enzymes Step 2: ubiquitin is added to lysine residues on protein by E3 ubiquitin ligase Step 3: ubiquitated protein is recognized and degraded by proteases in the proteasome complex
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Regulation of Protein Degradation
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