Ontology highlight
ABSTRACT:
SUBMITTER: Praefcke GJ
PROVIDER: S-EPMC526462 | biostudies-literature | 2004 Nov
REPOSITORIES: biostudies-literature
Praefcke Gerrit J K GJ Ford Marijn G J MG Schmid Eva M EM Olesen Lene E LE Gallop Jennifer L JL Peak-Chew Sew-Yeu SY Vallis Yvonne Y Babu M Madan MM Mills Ian G IG McMahon Harvey T HT
The EMBO journal 20041021 22
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 ...[more]