Unfolded protein response
6 important questions on Unfolded protein response
Via which pathway are misfolded proteins degraded?
When is there stress in the ER? Two types and give examples.
Cellular aspects:
- Glucose deprivation
- amino acid depletion
- calcium deregulation
- ROS
- hypoxia
- viral infection
- protein mutations
Chemical inducers:
- the N-linked glycosylation inhibitor tunicamycin
- thapsigargin
- the calcium ionophore A23187
- DTT
What are tunicamycin and thapsigargin?
Thapsigargin: Non-competitive inhibitor of the sarco/endoplasmic reticulum Ca2+ ATPase. Depletes ER calcium leading to ER stress.
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Explain the ER associated degradation pathway. Which three pathway are there?
- coupled to PERK- AFT 4: reactivation of translation
- coupled to ATF6- AFT6: augment XBP1 arme, ready to stop => gene = XBP1 and DDIT3
- coupled to IRE1- sXBP1: proper protein folding, proteasomal degradation.
The HsPA5/PERK pathway. What does it activate (3)?
2. Amino acid transport SLC7A1, SLC7A11, SLC38A1
3. Aminoacyl-tRNA synthesis Aminoacyl-tRNA
Summarize the unfolded protein stress pathway.
Activation mechanism: HSPA5 (BiP) binding to unfolded proteins
Inhibition mechanism: Competition (less unfolded proteins)
Key outcomes and genes involved:
Prime for translation (tijdelijke translatie remming + aanrukken van amino acid synthese en transport) - ATF4 arm
Chaperone (verbetert het vouwen en helpt bij opruimen)– XBP1arm
Apoptosis (als de stress te groot is) – DDIT3 (CHOP)
Links to disease: Many genetic diseases, where the mutant protein is not folded correctly Diabetes, Cancer
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