Legionella effector RavZ evades host autophagy by extracting LC3-PE from the membrane before deconjugation.

The endosomal GEF Mon1-Ccz1 binds to Atg8 on autophagosomes, and recruits its substrate, the Rab7-like Ypt7, which then mediates fusion of the autophagosomes with the lysosome.

Oligomerization of p62/SQSTM1 generates high avidity binding regions that enable it to spatially select for concentrated ubiquitin and ATG8-family proteins.

WASp is an immunometabolic regulator of human myeloid cells and regulates autophagy and mitochondrial homeostasis.

C53 bridges selective autophagy with ribosome-associated quality control at the endoplasmic reticulum.

Full length RTN3 homodimerization mediates ER tubules fragmentation and their subsequent delivery to lysosome.

Mitophagy regulates mitochondrial quality and mediates extensive mitochondrial degradation in (patho-)physiological settings and is one of the key components of hypoxic preconditioning which protects the heart from ischemia/reperfusion injury.

Two GAP proteins bound to mitochondria regulate the enyzme Rab7, and thereby the expansion of the isolation membrane during mitophagy, downstream of PINK1 and Parkin, two proteins that are mutated in familial Parkinson's disease.

The core autophagy protein Atg8 plays non-autophagy roles through binding to an integral membrane protein Hfl1, which harbors an unusual Atg8-interacting motif.

An ensemble of the ubiquitin-activating enzyme UBA6 and ubiquitin-conjugating enzyme/ubiquitin-ligase BIRC6 mediates ubiquitination of LC3, targeting the latter for proteasomal degradation and thus attenuating autophagic degradation of cellular substrates.