BIOL 2520 Lecture Notes - Lecture 13: Translocon, Transmembrane Protein, Glycolipid
9 Dec 2017
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Document Summary
With newly folded protein, chaperones can make sure that protein is folded correctly: chaperones facilitate the proper folding of the polypeptide by suppressing or unfolding "incorrect" structures. Two common types of chaperone proteins are hsp70 and chaperonin. If the mis-folded proteins cannot be corrected, they are exported out of the er and destroyed by the proteasome. Sometimes too many unfolded proteins are produced at once. Er has sensors that monitor levels of unfolded proteins. Sensors are kept inactive by a chaperone called bip. If too many unfolded proteins arise, bip releases sensors, helps fold proteins, and the now active sensors alert the cell to make more chaperones. Sensors can also inactivate an initiation factor to prevent more protein synthesis. If more misfolded proteins are in the er, bip detaches from the sensor and helps protein (bip attached to sensor is inactive bip: 2 strategies cell can make to deal with unfolded protein response.
