Open AccessER-phagy requires the assembly of actin at sites of contact between the cortical ER and endocytic pits
Author(s) -
Dongmei Li,
Muriel Mari,
Xia Li,
Fulvio Reggiori,
Susan FerroNovick,
Peter Novick
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2117554119
Subject(s) - endocytic cycle , endoplasmic reticulum , microbiology and biotechnology , vacuole , lysosome , autophagy , saccharomyces cerevisiae , chemistry , actin , biology , receptor , yeast , endocytosis , biochemistry , apoptosis , cytoplasm , enzyme
Significance Portions of the endoplasmic reticulum (ER) are degraded by autophagy (ER-phagy) in response to starvation or the accumulation of misfolded proteins. We show that ER-phagy requires assembly of actin at sites of contact between the edges of ER sheets and endocytic pits on the plasma membrane. Actin assembly may help to bring an element of the ER carrying the selective autophagy receptor Atg40 into the cell interior, where it associates with Atg11, a scaffold needed to recruit components for autophagosome assembly. Understanding the mechanism by which regions of the ER are selected for degradation and sequestered within autophagosomes may help in the development of novel approaches to treat diseases that result from the accumulation of misfolded proteins within the ER.