Protein Degradation

Question 1

• 2 major ways for small volume endocytosis? Def? Ex?
• Reasons for degradation? (4)
• 2 chaperones in ER? How do they work?
• Percent of newly synthesized proteins that are correctly folded? chaperone assisted? degraded?

Answer 1

1. ) Clatherin Coated Vessicles: Coat forms and is pinched of by dynamin 2.) Cavelae: surface of cell has many invaginations; 3 major proteins = caveolin 1,2,3; also pinched by dynamin; LDLR
   - misfolded, finite lifetime, damaged organelles, material (good or bad) is endocytosed
2. ) HSP70: Bind exposed hydrophobic patches (ATP) dependent 2.) HSP60: Iso chamber groes and groel
   - 40; 30; 30

Question 2

• Quality control methods for protein synthesis at the ER? (4) Example of each?
• Proteosome: Def? ATP? Located where? Purpose of a units? B units? Size? Composition? AA’s spiralled in at what rate? ATP used for? Mediated how? By what?
• Roles of lysosome? (2)

Answer 2

1. ) provide optimized oxidizing environment; oligometric assembly 2.) Folding enzymes ERB57 allows proper disulfide bonds 3.) Chaperones 4.) Folding sensors: UGGT
   - Protein that breaks down proteins; Yes; Nucleus and cytosol; regulate entry; proteolytic; 7-9 AA’s; unfold not cleave; poly ubiquitization; ubiquitin
2. ) degrade monoubiquiniated proteins 2.) degrade all cellular componenets