Mechanisms of Selective Autophagy
By Gabriele Zaffagnini, S. Martens. Journal of Molecular Biology, 2016
623 citations recorded by the source corpus.
Selective autophagy contributes to intracellular homeostasis by mediating the degradation of cytoplasmic material such as aggregated proteins, damaged or over-abundant organelles, and invading pathogens. The molecular machinery for selective autophagy must ensure efficient recognition and sequestration of the cargo within autophagosomes. Cargo specificity can be mediated by autophagic cargo receptors that specifically bind the cargo material and the autophagosomal membrane. Here we review the recent insights into the mechanisms that enable cargo receptors to confer selectivity and exclusivity to the autophagic process. We also discuss their different roles during starvation-induced and selective autophagy. We propose to classify autophagic events into cargo-independent and cargo-induced autophagosome formation events.
Subfields: Cell Biology, Epidemiology, Parasitology
View Paper: https://www.semanticscholar.org/paper/5820c8bb405ee4f8ad7e97feebc1ad4867852427
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Citations in the corpus
- Molecular mechanisms and physiological functions of mitophagy (2021, neutral): “…selective autophagy-related processes including mitophagy, a series of autophagy adaptors (p62/SQSTM1, NBR1, NDP52/ CALCOCO2, TAX1BP1, and OPTN) play important roles in selective uptake of cargoes (Johansen & Lamark, 2011; Mizushima & Komatsu, 2011; Stolz et al , 2014; Zaffagnini & Martens, 2016).”
- Mechanisms of Autophagy Initiation (2017, background): “In selective autophagy, a variety of adaptor proteins link cargoes to the autophagy machinery, including p62, Optineurin (OPTN), and NDP52 (3, 4, 22).”
- Molecular definitions of autophagy and related processes (2017, neutral): “Indeed, both autophagy substrates and receptors are subjected to lysosomal degradation, but only the latter function as part of the autophagy apparatus (Boya et al , 2013; Noda & Inagaki, 2015; Zaffagnini & Martens, 2016).”
- A cross-kingdom conserved ER-phagy receptor maintains endoplasmic reticulum homeostasis during stress (2020, background): “4 ATG8 with nanomolar affinity (KD=~700 nM), in contrast to the AIM mutant peptide (AIM mut), which 71 does not show any binding (Figure S1c-f) or the low micromolar-range affinities measured for most cargo 72 receptors (Zaffagnini and Martens, 2016).”