Endocytosis is switched off in dividing cells because actin is not available to assist the clathrin machinery at a time when membrane tension is increased.

The examination of the ultra-structure and in vivo dynamics of endocytosis in plants reveal plants unique actin-independent, clathrin-mediated endocytosis mechanisms to overcome their unique physiological properties.

The main proteins of clathrin-mediated endocytosis bind and unbind rapidly, continuously turning over about five times during the formation of an endocytic vesicle in yeast.

An experimentally constrained multiscale mathematical model predicts that branched actin networks self-organize at endocytic sites and bend to produce force, which was verified with cryo-electron tomography of intact cells.

Analysis of neurons that lack the two neuronal dynamins, dynamin 1 and 3, demonstrates a pathway of synaptic vesicle reformation that does not require these two dynamins or clathrin-dependent budding.

Quantitative comparison of clathrin-mediated endocytosis in budding and fission yeast identified conserved mechanisms and species-specific adaptations with broad implications that extend from yeast to humans.

Capacitance measurements and pH imaging reveal distinct modes of uptake for endocytotic presynaptic membrane and proteins.

At mammalian synapses the clathrin adaptor AP-2 plays a crucial role in the endocytic retrieval of a subset of synaptic vesicle proteins from the presynaptic cell surface, while clathrin is dispensable.

Studies of Lowe syndrome patient cells, which lack the inositol 5-phosphatase OCRL, suggest that a defect in endocytosis plays a role in the pathological manifestations of the disease.

Epsin has a key role in the coupling of actin to endocytic clathrin coated pits that is required for their maturation and helps capture SNAREs at endocytic clathrin coated pits.