TANGO1 creates a sub-compartment at the endoplasmic reticulum, to segregate and export fully assembled bulky cargoes.

The core of histone acetyltransferase complex, NuA4, flexibly tethers various histone recognition modules, including the HAT module which is capable of binding nucleosomes marked by H3K4me3 and H3 acetylation.

Recruitment of HOPS tethering complex to target membranes to promote vesicle fusions requires proper complex assembly and specific small GTPases, and HOPS is not transformed from the related miniCORVET complex.

TANGO1 creates a barrier to control lipid and protein flux across fused secretory compartments.

In vitro single-particle tracking reveals that ATP binding increases the one-dimensional diffusion of yeast chromatin remodeler SWR1 on DNA stretched between optical tweezers and diffusion is confined by protein roadblocks and nucleosomes.

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.

Chaperoning defects in axonemal dynein subunits trigger proteostatic clearance of dynein motors opening up the possibility of trialling proteostasis modulators to treat the motile ciliopathy primary ciliary dyskinesia (PCD).

Variability in bacterial transcription start site selection involves DNA “scrunching” and “anti-scrunching,” which may represent a general mechanism for start site selection in all organisms.