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 tethering complex HOPS employs affinity for each of the 4 SNAREs to catalyze assembly of 3-SNARE intermediates, supporting an immediate burst of membrane fusion triggered by the 4th SNARE.

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.

The coordinate activity of Sec17/SNAP and Sec18/NSF for membrane fusion is not limited to systems with homotypic fusion and vacuole protein sorting (HOPS), the lysosomal/vacuolar tethering, and SNARE assembly complex.

Knockout of the methyltransferase ICMT prevents progerin methylation and improves survival in mice with Hutchinson-Gilford progeria syndrome (HGPS) and an ICMT inhibitor delays senescence and stimulates proliferation of HGPS cells.

Selection by national-level antibiotic consumption and vaccination trends drives atypical recombinations, frequently resulting in interspecies sequence exchange at many sites across a bacterial species’ chromosome.

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

Age-stratified comparisons of gene expression in progeria patient fibroblasts reveals disruption of mesenchymal lineage pathways and points to a deficit in chondrogenic commitment in early development and a depletion of the mesenchymal lineage stem cell pool.

Direct reprogramming of smooth muscle cells from HGPS patients revealed that BMP4 is a key contributor of vascular degeneration and might represent a new therapeutic target.

Sec17 is shown to have divergent effects on pre-fusion SNARE complex activity, depending on the state of SNARE zippering and HOPS, an SM-tether complex, controls the outcome of Sec17-SNARE engagement.