New Protein Interaction Partners for the α- and β-Appendage Domains of AP2 Adaptors

<div><p>(A) Plot of the network of protein interactions in clathrin-mediated endocytosis. AP2 adaptors and clathrin have disproportionately large numbers of interactors and so are the hubs of this network. Dynamin is a “party” hub as it is shared between different networks but we have not included all its interactors.</p> <p>(B) Scheme of AP2 showing the overall domain architecture and the appendages where most of the protein interactors bind are located on flexible linkers called “hinges.”</p> <p>(C) Protein interactors of α- and β2 appendages from HeLa cells as determined by LC-MS/MS of Coomassie stained bands. Bolded proteins were not detected previously. The interaction of CVAK104 and CVAK90 were tested and confirmed by yeast-2-hybrid analysis. The numbers of peptides sequenced from each protein are given in brackets. Further mass spectrometry data from brain and liver samples, accession numbers, domain structures and details are given in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040262#pbio-0040262-sg001" target="_blank">Figures S1</a> and <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.0040262#pbio-0040262-sg002" target="_blank">S2</a>.</p>