What is it about?
Degradation of misfolded proteins from the ER requires their translocation across the ER membrane to allow clearance by cytosolic proteasomes. Degradation of proteins that cannot be transported across the membrane (as an example large aggregates) relies on their transport to degradative endolysosomes and has been poorly studied. Here we explain the mechanisms of proteasomal ER-associated degradation (ERAD) and lysosomal ER-to-lysosome-associated degradation (ERLAD).
Featured Image
Why is it important?
Clearance of misfolded proteins from the ER is crucial to maintain the function of this intracellular compartment dedicated to synthesis of proteins, lipids and sugar.
Perspectives
Understanding the mechanisms of misfolded proteins clearance may be instrumental to identify druggable pathways and therapeutically intervene in diseases caused by protein misfolding.
Maurizio Molinari
Institute for Research in Biomedicine, Bellinzona, Switzerland
Read the Original
This page is a summary of: Proteasomal and lysosomal clearance of faulty secretory proteins: ER-associated degradation (ERAD) and ER-to-lysosome-associated degradation (ERLAD) pathways, Critical Reviews in Biochemistry and Molecular Biology, March 2019, Taylor & Francis,
DOI: 10.1080/10409238.2019.1610351.
You can read the full text:
Contributors
The following have contributed to this page
