The dynamic phosphorylation of autophagy component WIPI2B is critical to maintain autophagosome biogenesis in neurons, and ectopic expression of WIPI2B can restore rates of autophagosome biogenesis in aged neurons.

A cell-free biochemical assay for protein lipidation identifies the ER–Golgi intermediate compartment as a key early station in the formation of an autophagosome.

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.

Building on previous work (Ge et al., 2013), it is shown that the ER-Golgi intermediate compartment is a platform for the production of COPII vesicles as precursor membranes for the lipidation of LC3, which is an essential step in autophagosome biogenesis.

A pathogen effector mimics starvation-induced autophagy by subverting host endomembrane trafficking to stimulate biogenesis of autophagosomes around pathogen feeding sites, revealing how pathogens interlock distinct host compartments to facilitate infection.

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.

Phosphorylation of a core trafficking component, the COPII coat subunit Sec24, regulates cross-talk between the secretory and autophagy machinery during starvation.

cis-membrane insertion of human ATG8 N-terminus facilitates autophagosome membrane expansion independent of autophagic cargo.

The crosstalk between autophagy and the phagocytosis of apoptotic cells, two cellular clearance pathways, promotes the fusion of the double-membrane autophagosomes to the phagosomes and plays an important role in the degradation of engulfed apoptotic cells.

The control of SEC23B degradation by SCF^FBXW5 and ULK1 regulates the autophagy.