**Why is folding in the ER slow and inefficient and how are the misfolded ones degraded?**In the endoplasmic reticulum (ER), protein folding is a critical but complex process that can be slow and inefficient due to the intricate nature of protein structure. Various factors contribute to these challenges, including the need for specific conditions and molecular chaperones to facilitate proper folding. Additionally, the ER environment is crowded with nascent polypeptide chains, which can interfere with efficient folding.Misfolded proteins are typically targeted for degradation to prevent accumulation and potential cellular damage. The degradation process often involves the ER-associated degradation (ERAD) pathway, where misfolded proteins are recognized, ubiquitinated, and then directed to the proteasome for degradation. This process ensures cellular health by maintaining protein quality control in the ER.

Name: **Why is folding in the ER slow and inefficient and how are the misfo
Uploaded: 2024-03-20T06:42:41.000Z
Channel: Bartleby
Description: **Why is folding in the ER slow and inefficient and how are the misfolded ones degraded?**In the endoplasmic reticulum (ER), protein folding is a critical but complex process that can be slow and inefficient due to the intricate nature of protein st

Endoplasmic reticulum-associated degradation (ERAD) is the QC check point of the ER which helps to maintain the protein homeostasis and removes the misfolded proteins via exocytosis or proteolysis mechanisms. Protein synthesis in ER is slow and often hydrophobic collapse occurs which disturbs the process of protein folding. the collapse of N-terminal protein will affect the folding of C terminal proteins. This makes the protein folding in the ER is slow and inefficient and also protein folding in the ER takes place rather randomly so it becomes error-prone. So there is a Protein quality control (PQC) system that checks the errors in the protein folding. the misfolded proteins are eliminated via the protein degradation method or autophagy. Misfolded proteins are recognized by the PQC or checkpoints and are destroyed in the ER by autophagy and ERAD. Some of them escape from ER and these are degraded bi vacuolar lysosomal proteases enzymes.