2BP5

MU2 ADAPTIN SUBUNIT (AP50) OF AP2 ADAPTOR (SECOND DOMAIN), COMPLEXED WITH NON-CANONICAL INTERNALIZATION PEPTIDE VEDYEQGLSG

Summary for 2BP5

• Entry DOI: 10.2210/pdb2bp5/pdb
• Related: 1BW8 1BXX 1GW5 1HES 1I31
• Descriptor: CLATHRIN COAT ASSEMBLY PROTEIN AP50, P2X PURINOCEPTOR 4 (3 entities in total)
• Functional Keywords: adaptor, coated pits, endocytosis, endocytosis-exocytosis, endocytosis/exocytosis, peptide complex
• Biological source: RATTUS NORVEGICUS (RAT); More
• Total number of polymer chains: 2
• Total formula weight: 50822.74

Authors

Royle, S.J.,Evans, P.R.,Owen, D.J.,Murrell-Lagnado, R.D. (deposition date: 2005-04-18, release date: 2005-07-06, Last modification date: 2023-12-13)

Primary citation

Royle, S.J.,Qureshi, O.S.,Bobanovic, L.K.,Evans, P.R.,Owen, D.J.,Murrell-Lagnado, R.D.
Non-Canonical Yxxg-Phi Endocytic Motifs: Recognition by Ap2 and Preferential Utilization in P2X4 Receptors.
J.Cell.Sci, 118:3073-, 2005

PubMed Abstract: 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 YXXPhi motif and a non-canonical YXXGPhi motif (YEQGL). We demonstrate that endocytosis of P2X4 receptors is mediated preferentially by the YXXGPhi motif because the YXXPhi motif is inaccessible to AP2 owing to the structure of the channel. The crystal structure of a complex between residues 160-435 of the mu2 subunit of AP2 and a P2X4 C-terminal peptide showed that the YEQGL motif binds to mu2 at the same site as YXXPhi motifs. Y and Phi residues are accommodated in the same hydrophobic pockets in mu2 with the extra residue between them being accommodated by changes in the peptide's backbone configuration, when compared to YXXPhi 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 (YXXGPhi).

PubMed: 15985462
DOI: 10.1242/JCS.02451

Experimental method

X-RAY DIFFRACTION (2.8 Å)