Quantitative 3D lattice light sheet microscopy of unperturbed cells combined with electron tomography and acute loss of function experiments reveals how dynamic ESCRT-III/Vps4 assemblies succeed in reverse membrane budding on endosomes.

Cryo-EM structure and biochemical characterization of the human nuclear exosome reveals its specific properties with respect to the yeast complex, underscoring the evolutionary conservation of the RNA-channeling mechanisms and hMTR4 helicase recruitment.

The HCMV virion envelope is derived from the host exosome membrane, and exosome machinery and export pathways facilitate virion egress.

The nuclear exosome cofactors Mpp6 and Rrp47 can stimulate exoribonuclease activities of the nuclear RNA exosome and recruit the Mtr4 helicase to promote helicase dependent RNA decay.

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.

Phosphorylation of the Eps15-like protein Pan1p regulates how endocytic compartments interact with each other and with the actin cytoskeleton.

An endosomal component employs a novel PAM2-like motif to recruit a key RNA-binding protein, which explains how mRNAs and associated ribosomes are attached to endosomes during coupled transport.

BLOS1 is a new regulator of LDLR endosomal recycling through coordinating kinesins during long-range transport, and depletion of BLOS1 in mouse liver leads to aberrant lipid metabolism.

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.

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.