15. What happens to proteins that misfold in the ER? 16. You are at a cocktail p

Question

15. What happens to proteins that misfold in the ER?

16. You are at a cocktail party and overhead an obnoxious academic trying to impress a group of students by saying: “The interior space, or lumen, of each membrane-enclosed compartment along the biosynthetic–secretory and endocytic pathways is topologically equivalent to the lumen of most other membrane-enclosed compartments and to the cell exterior.” Your friend whispers in your ear—“what is that guy talking about?” Rephrase, in plain language, the statement above:

17. Aside from the cell surface, where else can a secretory protein end up?

Explanation / Answer

15: The misfolded proteins are removed from the ER by the quality control mechanism as accumulation of these misfolded proteins in ER disturbs the protein trafficking. The binding proteins (chaperons) serve to recognize the misfolded proteins through the aberrant AA sites. These misfolded proteins are retained in the ER and are not allowed to pass into the golgi apparatus. The GT monitoring enzyme serves to add the single glucose resude to the terminal end of the misfolded proteins which then bind to calnexin again to ensure the proper folding this time. The process continues till the proper folding of the protein is done.

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