Membrane fusion articles from across Nature Portfolio

The Chloride Intracellular Channel (CLIC) protein family is highly conserved, yet their function remains a matter of ongoing research. Here, authors reveal their ability to facilitate membrane fusion, shedding light on their physiological role.

In intracellular trafficking, transport vesicles deliver cargo via membrane fusion. The fusion machinery includes both tethering factors and SNAREs. The cryo-electron microscopy structure of a tether–SNARE complex reveals the basis for their collaboration.

Life-crucial membrane fusion and budding were traditionally viewed with electron microscopy. With recent breakthroughs that visualize membrane transformation in real time, Wu and Chan synthesize a new model with mechanistic principles and functions.

Eukaryotic membrane fusion is hindered by energy barriers and often requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) to facilitate formation of a fusion pore. Recent studies describe SNARE activity along the fusion pathway and shed light on the regulation of SNARE complex assembly.

The HOPS complex mediates membrane tethering and autophagosome-lysosome fusion. Here, the authors biochemically reconstitute the mammalian HOPS in protoliposomes and propose a model of complex assembly that depends on Rab2 and Rab39A.

This Comment article proposes that the transfer of surface molecules between interacting cells by trogocytosis might affect the cellular specificity of monoclonal antibodies, as well as the functionality of receiving cells.

Receptor-mediated endocytosis delivers low-density lipoproteins (LDLs) to late endosomes, from where cholesterol is trafficked to mitochondria. Zhou et al. report that LDL-containing endosomes fuse with mitochondria, supplying cholesterol for steroid biosynthesis and enabling mitochondrial degradation of the LDL receptor.

Mitochondrial dynamics regulates stem cell expansion and differentiation.

Fusion between the inner membranes of two mitochondria requires the GTPase optic atrophy 1 (OPA1), but the molecular mechanism is poorly understood. A study now shows that fusion of two liposomes can be performed by OPA1 tethered to just one liposome, through an interaction with the phospholipid cardiolipin on the opposing liposome.

α-Synuclein is present at high levels in all neurons and their synapses. We now learn that this protein helps dilate the fusion pore, which forms transiently during vesicle exocytosis, promoting release of certain neurotransmitters.