The family of ANTH domain proteins serve as adaptors to endocytose ubiquitinated proteins from the cell surface.

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.

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.

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.

Neurodegeneration driven by pathogenic aggregating proteins reorganizes the actin cytoskeleton, causing cellular stiffening and abolishing force generation required for endocytic events.

The postsynaptic endocytic zone is a highly organized structure composed of a diversity of endocytic proteins.

Histone, PCNA, and DNA binding are essential for CAF-1 functions in preventing DNA damage during DNA replication in Schizosaccharomyces pombe, while its C-terminal domain specifies distinct cellular processes.

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.

Coupling between subcellular localization and protein turnover of a neuronal stress kinase, DLK, and its role in neuronal stress responses in Drosophila.

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