4CZ2
Complex of human VARP-ANKRD1 with Rab32-GppCp. Selenomet derivative.
4CZ2 の概要
| エントリーDOI | 10.2210/pdb4cz2/pdb |
| 関連するPDBエントリー | 4CYM |
| 分子名称 | RAS-RELATED PROTEIN RAB-32, ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 27, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, ... (5 entities in total) |
| 機能のキーワード | signaling protein, varp, rab-effector, rab, endosome, vesicle trafficking, melanosome biogenesis |
| 由来する生物種 | HOMO SAPIENS (HUMAN) 詳細 |
| 細胞内の位置 | Mitochondrion: Q13637 Cytoplasm: Q96NW4 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 145950.05 |
| 構造登録者 | Perez-Dorado, I.,Schaefer, I.B.,McCoy, A.J.,Owen, D.J.,Evans, P.R. (登録日: 2014-04-16, 公開日: 2014-06-04, 最終更新日: 2024-11-13) |
| 主引用文献 | Hesketh, G.G.,Perez-Dorado, I.,Jackson, L.P.,Wartosch, L.,Schefer, I.B.,Gray, S.R.,Mccoy, A.J.,Zeldin, O.B.,Garman, E.F.,Harbour, M.E.,Evans, P.R.,Seaman, M.N.,Luzio, J.P.,Owen, D.J. Varp is Recruited on to Endosomes by Direct Interaction with Retromer, Where Together They Function in Export to the Cell Surface. Dev.Cell, 29:591-, 2014 Cited by PubMed Abstract: VARP is a Rab32/38 effector that also binds to the endosomal/lysosomal R-SNARE VAMP7. VARP binding regulates VAMP7 participation in SNARE complex formation and can therefore influence VAMP7-mediated membrane fusion events. Mutant versions of VARP that cannot bind Rab32:GTP, designed on the basis of the VARP ankyrin repeat/Rab32:GTP complex structure described here, unexpectedly retain endosomal localization, showing that VARP recruitment is not dependent on Rab32 binding. We show that recruitment of VARP to the endosomal membrane is mediated by its direct interaction with VPS29, a subunit of the retromer complex, which is involved in trafficking from endosomes to the TGN and the cell surface. Transport of GLUT1 from endosomes to the cell surface requires VARP, VPS29, and VAMP7 and depends on the direct interaction between VPS29 and VARP. Finally, we propose that endocytic cycling of VAMP7 depends on its interaction with VARP and, consequently, also on retromer. PubMed: 24856514DOI: 10.1016/J.DEVCEL.2014.04.010 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.97 Å) |
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