Abstract 2282 Novel micro-ER-phagy selectively clears aberrant membrane proteins during nutritional stress

Accumulation of aberrant membrane proteins is associated with human disease. Membrane proteins are inserted first into the endoplasmic reticulum (ER) where two quality-control (QC): ER-associated degradation (ERAD) and macro-ER-phagy, deliver misfolded and excess membrane proteins for degradation in the proteasome and lysosome, respectively. In mutant cells defective in ER-QC, aberrant proteins accumulate. We show that these aberrant proteins are cleared efficiently in the lysosome under nutritional stress through a novel selective micro-ER-phagy pathway, much before a small fraction of normal membrane proteins is degraded via macro-ER-phagy.