Evolving nature of the AP2 alpha-appendage hub during clathrin-coated vesicle endocytosis.

ABSTRACT: Clathrin-mediated endocytosis involves the assembly of a network of proteins that select cargo, modify membrane shape and drive invagination, vesicle scission and uncoating. This network is initially assembled around adaptor protein (AP) appendage domains, which are protein interaction hubs. Using crystallography, we show that FxDxF and WVxF peptide motifs from synaptojanin bind to distinct subdomains on alpha-appendages, called 'top' and 'side' sites. Appendages use both these sites to interact with their binding partners in vitro and in vivo. Occupation of both sites simultaneously results in high-affinity reversible interactions with lone appendages (e.g. eps15 and epsin1). Proteins with multiple copies of only one type of motif bind multiple appendages and so will aid adaptor clusterin

SUBMITTER: Praefcke GJ 

PROVIDER: S-EPMC526462 | biostudies-literature | 2004 Nov

REPOSITORIES: biostudies-literature