ER-phagy requires the assembly of actin at sites of contact between the cortical ER and endocytic pits | Zendy

Dongmei Liu | Zendy; Muriel Mari | Zendy; Xia Li | Zendy; Fulvio Reggiori | Zendy; Susan FerroNovick | Zendy; Peter Novick | Zendy

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ER-phagy requires the assembly of actin at sites of contact between the cortical ER and endocytic pits

Author(s) -

Dongmei Liu,

Muriel Mari,

Xia Li,

Fulvio Reggiori,

Susan FerroNovick,

Peter Novick

Publication year - 2022

Publication title -

proceedings of the national academy of sciences

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.

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