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JCS ePress online publication date 28 Jun 2005
doi: 10.1242/jcs.02451

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Research Article

Non-canonical YXXG{Phi} endocytic motifs: recognition by AP2 and preferential utilization in P2X4 receptors


Stephen J. Royle, Omar S. Qureshi, Laura K. Bobanovic, Philip R. Evans, David J. Owen, and Ruth D. Murrell-Lagnado*
* Author for correspondence (e-mail: rdm1003{at}cam.ac.uk)

During clathrin-mediated endocytosis, proteins on the cell surface are selected for inclusion in clathrin-coated vesicles by clathrin adaptors, mainly the adaptor complex AP2. The P2X4 subtype of ATP-gated ion channel has in its C-terminus two putative endocytic motifs: a canonical YXX{Phi} motif and a non-canonical YXXG{Phi} motif (YEQGL). We demonstrate that endocytosis of P2X4 receptors is mediated preferentially by the YXXG{Phi} motif because the YXX{Phi} motif is inaccessible to AP2 owing to the structure of the channel. The crystal structure of a complex between residues 160-435 of the µ2 subunit of AP2 and a P2X4 C-terminal peptide showed that the YEQGL motif binds to µ2 at the same site as YXX{Phi} motifs. Y and {Phi} residues are accommodated in the same hydrophobic pockets in µ2 with the extra residue between them being accommodated by changes in the peptide's backbone configuration, when compared to YXX{Phi} motifs. These data demonstrate that the family of potential tyrosine-based endocytic signals must be expanded to include motifs with an additional glycine at Y+3 (YXXG{Phi}).
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