Membrane atg8ylation but not canonical autophagy control retromer-dependent endosomal sorting of cargo, including glucose transporter GLUT1, of general import and of significance for control of tuberculosis.

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 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.

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.

CapZ controls actin filament density around immature early endosomes via its C-terminal domain to facilitate the homotypic fusion of the endocytic vesicles, and it functions as a scaffold protein via its N-terminal domain to recruit RAB5 effectors to early endosomes.

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

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.

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.