Final answer:
If misfolded proteins are not caught in the ER, the only other place they can be degraded is in the lysosomes. Lysosomes play an important role in the degradation of unwanted or misfolded proteins by utilizing proteases called cathepsins. These proteases break down the proteins into smaller peptides and amino acids for recycling or disposal.
Step-by-step explanation:
If misfolded proteins are not caught in the ER, the only other place where they can be degraded is at the proteasome. The process includes a protein called ubiquitin that tags the misfolded proteins, marking it for delivery to the proteasome, a large polypeptide complex responsible for degrading unwanted proteins. Moreover, lysosomes play a crucial role in the degradation of intracellular and extracellular proteins, utilizing proteases such as cathepsins to break down protein components.