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Maurizio Molinari, PhD - "Endoplasmic Reticulum-to-Lysosome-Associated Degradation of Proteasome-Resistant Protein Polymers"

Istituto di Ricerca in Biomedicina, Bellinzona, Svizzera
When Nov 28, 2017
from 12:00 PM to 01:30 PM
Where Tigem Auditorium "Vesuvius"
Contact Name
Contact Phone 081-19230659
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Abstract
Efficient degradation of by-products of protein synthesis is required to maintain cellular proteostasis, i.e., the capacity to produce the proteome in appropriate quality and quantity. For misfolded proteins generated in the endoplasmic reticulum (ER), this mainly occurs via ER-associated degradation (ERAD), which requires dislocation across the ER membrane and degradation by cytosolic proteasomes. The mode of degradation from the ER of proteasome-resistant misfolded proteins, for example α1-antitrypsin Z (ATZ) polymers, is unknown. Here we report that luminal accumulation of polymeric ATZ activates ER-to-lysosomes-associated degradation (ERLAD). This course does not require autophagosome biogenesis, nor the intervention of ER-phagy pathways. Rather, it relies on vesicular delivery of luminal ER content to LAMP1-positive degradative organelles for clearance.

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