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.

HIV-1 viral protein u (Vpu) can stimulate novel versions of canonical interactions with the clathrin adaptor AP1 to counteract the host antiviral protein BST2.

Endocytosis is regulated by a protein family that recycles the AP2 clathrin adaptor by restoring the inactive form of complex.

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

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

The structure of the Nef:AP-2 complex has been determined and used as the basis of a model that explains how HIV-1 Nef downregulates the CD4 receptor from the surface of the infected cells.

A protein complex that enables cells to transport substances across their membranes, and that typically consists of four subunits, can also function as two hemicomplexes, each with two subunits.

A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.

Kazrin, a protein widely expressed in vertebrates whose depletion causes defects in cell adhesion and migration, is recruited to early endosomes and promotes dynein/dynactin-dependent traffic of endocytosed cargo to the recycling endosomes.

In filamentous fungi the AP-2 complex, which in mammals is an adaptor of clathrin-mediated endocytosis, is recruited to specific clathrin-independent apical endocytosis necessary for proper lipid maintenance and polar growth.