Parallel measurements of pH gradient and membrane potential at the single vesicle level have revealed that the synaptic vesicle acidification is initiated by removal of its clathrin coat, which blocks vesicular ATPase activity.

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.

Clathrin-coated vesicles can be made to form on intracellular membranes using a minimal molecular system, which defines the core vesicle budding machinery.

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.

The muniscin protein FCHO1 interacts with, and activates, the adapter protein-2 complex (AP-2) to promote the assembly of clathrin-coated vesicles.

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.

A new user-intervention-free classification, using single-fluorescent markers, measures conventionally unmeasureable phenotypes in early stages during clathrin-mediated endocytosis.

Endocytosis is triggered by membrane-associated proteins that transform the clathrin adaptor into an active complex.

Chemical labelling of all primary endocytic vesicles allows the contribution of different endocytic mechanisms to the total endocytic uptake in cultured mammalian cells to be quantified.