Atomic force microscopy reveals a floppy, dimeric, coiled coil Golgin structure that captures transport vesicles via splayed, N-terminal ends at the Golgi complex.

The first quantitative live-cell microscopy this work shows depicting the order of events preceding secretion in budding yeast.

Rigorous assays of membrane fusion show that a distinct tethering step is required for lumenal compartment mixing in a manner that extends beyond simply increasing the amount of total trans-SNARE complex.

Synaptic vesicles undergo reversible tethering at the plasma membrane which is activity- and myosin V- dependent.

Blocking acidification causes endosomes to fuse with the plasma membrane, releasing exosomes that remain attached to the cell surface via the anti-viral protein tetherin.

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.

Uso1 critically regulating traffic in the ER/Golgi interface is a coiled-coil protein traditionally regarded as a tether, but a forward genetic screen revealed that its essential role appears to involve its ability to interact with SNAREs.

Lumen extension in intracellular tubes relies on a molecular pathway involving Rho GTPase signaling, cell polarity, and vesicle-tethering proteins.

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

The golgin GMAP-210 captures vesicles at the cis Golgi by merely recognizing the high curvature and lipid unsaturation level of transport vesicles.