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.

Reconstitution of the endosomal Rab cascade reveals that Rab5 binds and activates the Mon1-Ccz1 guanine nucleotide exchange factor, which in turn recruits Rab7 to membranes to drive fusion.

Parkin ubiquitination of damaged mitochondria recruits the Rab GEF, RABGEF1, to regulate downstream Rab cycles and ATG9A recruitment to growing phagophores that are participating in mitophagy.

The USP-50/USP8 protease removes the Rab5 GEF Rabex5 from endosomes while facilitating recruitment of the Rab7 GEF SAND-1/Mon1, promoting endosome maturation.

The axial organization and dynamics of the HOPS complex at membrane surface are resolved by graphene-induced energy transfer with subnanometer resolution.

A novel, inexpensive, easy-to-use method to analyse traffic along the endosomal pathway in mammalian cells shows that there is coordination between Rab conversion and acidification, but almost none between Rab conversion and recycling.

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.

Plant-unique RAB5 effector 2 (PUF2) is an effector of plant-unique ARA6, which plays a key role in plant endosomal transport, integrating functions of the two plant RAB5 groups by an unprecedented mechanism.

The structure of the yeast HOPS tethering complex suggests how this large complex may catalyze fusion by tethering Rab-decorated membranes and promoting the assembly of SNAREs.