A plant pathogen effector evolved a short linear motif to subvert autophagic defenses by antagonising a host cargo receptor.

Under normal nutritional conditions, G-protein coupled receptors can control autophagy by regulating the degradation of key autophagic regulator Atg14L through ZBTB16-mediated ubiquitination and proteasome degradation.

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

Atg43 serves as a selective autophagy receptor by tethering isolation membranes to mitochondria to promote mitophagy and plays a mitophagy-independent role that facilitates normal cell growth in fission yeast.

Autophagic cargo receptors recruit the E3-like enzyme for Atg8 lipid conjugation to the cargo and thereby promote local formation of Atg8-positive autophagosomal membranes.

Defense-related selective autophagy mediated by the antimicrobial autophagy cargo receptor NBR1/Joka2 is diverted to pathogen penetration sites to restrict plant colonization by the oomycete pathogen Phytophthora infestans.

Measurement of post-translational modifications in primary macrophages infected with Mtb revealed phosphorylation of TAX1BP1, an autophagy receptor that enables full maturation of the Mtb autophagosome.

NCOA4, the ferritin autophagy receptor, is regulated by HERC2 in an iron-dependent manner and is critical for red blood cell development.

Autophagy is critical for the turnover of inflammatory signaling complexes containing RHIM-domain proteins.

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