4Z88

SH3-II of Drosophila Rim-binding protein with Aplip1 peptide

4Z88 の概要

• エントリーDOI: 10.2210/pdb4z88/pdb
• 関連するPDBエントリー: 2CSQ
• 分子名称: RIM-binding protein, isoform F, JNK-interacting protein 1, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: synapse, active zone, rim-binding protein, sh3 domain, aplip1
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Cytoplasm : Q9W0K0
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 123798.16

構造登録者

Driller, J.H.,Holton, N.,Siebert, M.,Boehme, M.A.,Wahl, M.C.,Sigrist, S.J.,Loll, B. (登録日: 2015-04-08, 公開日: 2015-08-05, 最終更新日: 2024-11-13)

主引用文献

Siebert, M.,Bohme, M.A.,Driller, J.H.,Babikir, H.,Mampell, M.M.,Rey, U.,Ramesh, N.,Matkovic, T.,Holton, N.,Reddy-Alla, S.,Gottfert, F.,Kamin, D.,Quentin, C.,Klinedinst, S.,Andlauer, T.F.,Hell, S.W.,Collins, C.A.,Wahl, M.C.,Loll, B.,Sigrist, S.J.
A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones.
Elife, 4:-, 2015

PubMed Abstract: Synaptic vesicles (SVs) fuse at active zones (AZs) covered by a protein scaffold, at Drosophila synapses comprised of ELKS family member Bruchpilot (BRP) and RIM-binding protein (RBP). We here demonstrate axonal co-transport of BRP and RBP using intravital live imaging, with both proteins co-accumulating in axonal aggregates of several transport mutants. RBP, via its C-terminal Src-homology 3 (SH3) domains, binds Aplip1/JIP1, a transport adaptor involved in kinesin-dependent SV transport. We show in atomic detail that RBP C-terminal SH3 domains bind a proline-rich (PxxP) motif of Aplip1/JIP1 with submicromolar affinity. Pointmutating this PxxP motif provoked formation of ectopic AZ-like structures at axonal membranes. Direct interactions between AZ proteins and transport adaptors seem to provide complex avidity and shield synaptic interaction surfaces of pre-assembled scaffold protein transport complexes, thus, favouring physiological synaptic AZ assembly over premature assembly at axonal membranes.

PubMed: 26274777
DOI: 10.7554/eLife.06935

実験手法

X-RAY DIFFRACTION (2.09 Å)