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.

The first three-dimensional structure of the PI3KC3 complex I, which is involved in autophagy, provides a framework for understanding the allosteric regulation of lipid kinase activity.

Rab26 selectively directs synaptic and secretory vesicles into preautophagosomal structures, suggesting the presence of a novel pathway (vesiculophagy) for degradation of synaptic vesicles.

The AAA-ATPase VCP sustains sarcoplasmic proteostasis, in part, by controlling autophagosome-lysosome fusion and the integrity of a dynamic tubular lysosomal network.

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

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

Reconstitution of interleukin-1β secretion in non-macrophage cells implicates how this pro-inflammatory cytokine enters into the unconventional pathway of secretion through autophagy.

Sphingosine acts as a lipid messenger molecule in intracellular signaling networks that are relevant to lysosomal function and Niemann-Pick disease.