EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Nde1 promotes Lis1 binding to full-length autoinhibited human dynein 1.
ジャーナル・号・ページ	Nat Chem Biol, Year 2025
掲載日	2025年8月1日
著者	Jun Yang / Yuanchang Zhao / Pengxin Chai / Ahmet Yildiz / Kai Zhang /
PubMed 要旨	Cytoplasmic dynein 1 (dynein) is the primary motor responsible for the retrograde transport of intracellular cargoes along microtubules. Activation of dynein requires the opening its autoinhibited ...Cytoplasmic dynein 1 (dynein) is the primary motor responsible for the retrograde transport of intracellular cargoes along microtubules. Activation of dynein requires the opening its autoinhibited Phi conformation, a process driven by Lis1 and Nde1/Ndel1. Using biochemical reconstitution and cryo-electron microscopy, we demonstrate that Nde1 enhances Lis1 binding to autoinhibited dynein and facilitates Phi opening. We identify a key intermediate in this activation pathway where a single Lis1 dimer binds between Phi-like (Phi) motor rings. In this 'Phi-Lis1' complex, Lis1 interacts with one motor domain through canonical sites at the AAA+ (adenosine triphosphatases associated with diverse cellular activities) ring and stalk, and with AAA5, AAA6 and linker regions of the other motor domain. Mutagenesis and motility assays confirm the critical role of the Phi-Lis1 interface in dynein activation. This intermediate forms rapidly in the presence of Nde1, although Nde1 is not part of Phi-Lis1. These findings provide key insights into how Nde1 promotes Lis1-mediated Phi opening.
リンク	Nat Chem Biol / PubMed:40751002
手法	EM (単粒子)
解像度	2.71 - 6.22 Å
構造データ	EMDB-47374: Tail domain from phi dynein-1 under Lis1 condition 手法: EM (単粒子) / 解像度: 4.21 Å EMDB-47375: Tail domain from phi-like dynein-1 under Lis1 condition 手法: EM (単粒子) / 解像度: 4.05 Å EMDB-47376: Tail domain from phi-like dynein-1 under Nde1-Lis1 condition 手法: EM (単粒子) / 解像度: 6.22 Å 47378 9e0z EMDB-47378, PDB-9e0z: Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dimer under Nde1-Lis1 condition 手法: EM (単粒子) / 解像度: 2.86 Å 47379 9e10 EMDB-47379, PDB-9e10: Dimeric motor domains from phi dynein-1 under Lis1 condition 手法: EM (単粒子) / 解像度: 2.71 Å 47380 9e11 EMDB-47380, PDB-9e11: Dimeric motor domains from phi-like dynein-1 bound to a Lis1 dimer under Lis1 condition 手法: EM (単粒子) / 解像度: 2.86 Å 47381 9e12 EMDB-47381, PDB-9e12: Full-length human dynein-1 in phi comformation under Lis1 condition 手法: EM (単粒子) / 解像度: 4.5 Å 47382 9e13 EMDB-47382, PDB-9e13: Full-length human dynein-1 in phi-like comformation bound to a Lis1 dimer under Lis1 condition 手法: EM (単粒子) / 解像度: 4.5 Å 47383 9e14 EMDB-47383, PDB-9e14: Full-length human dynein-1 in phi-like comformation bound to a Lis1 dimer under Nde1-Lis1 condition 手法: EM (単粒子) / 解像度: 5.0 Å EMDB-48089: Consensus map of full-length human dynein-1 in phi conformation under Lis1 condition 手法: EM (単粒子) / 解像度: 4.5 Å EMDB-48091: Consensus map of full-length human dynein-1 in phi-like conformation bound to a Lis1 dimer under Lis1 condition 手法: EM (単粒子) / 解像度: 4.5 Å EMDB-48092: Consensus map of full-length human dynein-1 in phi-like conformation bound to a Lis1 dimer under Nde1-Lis1 condition 手法: EM (単粒子) / 解像度: 4.5 Å
化合物	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM ChemComp-MG: Unknown entry / マグネシウムジカチオン
由来	homo sapiens (ヒト)
キーワード	MOTOR PROTEIN / dynein-1 / phi-like conformation / Lis1 / phi / phi conformation