2A20

Solution structure of Rim2 Zinc Finger Domain

2A20 の概要

• エントリーDOI: 10.2210/pdb2a20/pdb
• 分子名称: Regulating synaptic membrane exocytosis protein 2, ZINC ION (2 entities in total)
• 機能のキーワード: zinc-finger domain, metal binding protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell membrane; Peripheral membrane protein (By similarity): Q9JIS1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7001.75

構造登録者

Dulubova, I.,Lou, X.,Lu, J.,Huryeva, I.,Alam, A.,Schneggenburger, R.,Sudhof, T.C.,Rizo, J. (登録日: 2005-06-21, 公開日: 2005-08-16, 最終更新日: 2024-05-22)

主引用文献

Dulubova, I.,Lou, X.,Lu, J.,Huryeva, I.,Alam, A.,Schneggenburger, R.,Sudhof, T.C.,Rizo, J.
A Munc13/RIM/Rab3 tripartite complex: from priming to plasticity?
Embo J., 24:2839-2850, 2005

PubMed Abstract: alpha-RIMs and Munc13s are active zone proteins that control priming of synaptic vesicles to a readily releasable state, and interact with each other via their N-terminal sequences. The alpha-RIM N-terminal sequence also binds to Rab3s (small synaptic vesicle GTPases), an interaction that regulates presynaptic plasticity. We now demonstrate that alpha-RIMs contain adjacent but separate Munc13- and Rab3-binding sites, allowing formation of a tripartite Rab3/RIM/Munc13 complex. Munc13 binding is mediated by the alpha-RIM zinc-finger domain. Elucidation of the three-dimensional structure of this domain by NMR spectroscopy facilitated the design of a mutation that abolishes alpha-RIM/Munc13 binding. Selective disruption of this interaction in the calyx of Held synapse decreased the size of the readily releasable vesicle pool. Our data suggest that the ternary Rab3/RIM/Munc13 interaction approximates synaptic vesicles to the priming machinery, providing a substrate for presynaptic plasticity. The modular architecture of alpha-RIMs, with nested binding sites for Rab3 and other targets, may be a general feature of Rab effectors that share homology with the alpha-RIM N-terminal sequence.

PubMed: 16052212
DOI: 10.1038/sj.emboj.7600753

実験手法

SOLUTION NMR