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	TOM20-driven E3 ligase recruitment regulates mitochondrial dynamics through PLD6.
ジャーナル・号・ページ	Nat Chem Biol, Vol. 22, Issue 1, Page 37-47, Year 2026
掲載日	2025年4月22日
著者	Anat Raiff / Shidong Zhao / Aizat Bekturova / Colin Zenge / Shir Mazor / Xinyan Chen / Wenwen Ru / Yaara Makaros / Tslil Ast / Alban Ordureau / Chao Xu / Itay Koren /
PubMed 要旨	Mitochondrial homeostasis is maintained through complex regulatory mechanisms, including the balance of mitochondrial dynamics involving fusion and fission processes. A central player in this ...Mitochondrial homeostasis is maintained through complex regulatory mechanisms, including the balance of mitochondrial dynamics involving fusion and fission processes. A central player in this regulation is the ubiquitin-proteasome system (UPS), which controls the degradation of pivotal mitochondrial proteins. In this study, we identified cullin-RING E3 ligase 2 (CRL2) and its substrate receptor, FEM1B, as critical regulators of mitochondrial dynamics. Through proteomic analysis, we demonstrate here that FEM1B controls the turnover of PLD6, a key regulator of mitochondrial dynamics. Using structural and biochemical approaches, we show that FEM1B physically interacts with PLD6 and that this interaction is facilitated by the direct association of FEM1B with the mitochondrial import receptor TOM20. Ablation of FEM1B or disruption of the FEM1B-TOM20 interaction impairs PLD6 degradation and induces mitochondrial defects, phenocopying PLD6 overexpression. These findings underscore the importance of FEM1B in maintaining mitochondrial morphology and provide further mechanistic insights into how the UPS regulates mitochondrial homeostasis.
リンク	Nat Chem Biol / PubMed:40263465 / PubMed Central
手法	EM (単粒子)
解像度	3.56 - 4.13 Å
構造データ	61196 9j77 EMDB-61196, PDB-9j77: Cryo-EM structure of CRL2-FEM1B (dimer 1) 手法: EM (単粒子) / 解像度: 3.56 Å 61197 9j78 EMDB-61197, PDB-9j78: Cryo-EM structure of CRL2-FEM1B (dimer 2) 手法: EM (単粒子) / 解像度: 3.88 Å 61198 9j79 EMDB-61198, PDB-9j79: Cryo-EM structure of CRL2-FEM1B bound with TOM20(tetramer) 手法: EM (単粒子) / 解像度: 4.08 Å 61199 9j7a EMDB-61199, PDB-9j7a: local refinement of FEM1B bound with TOM20 (dimer) 手法: EM (単粒子) / 解像度: 4.13 Å 61200 9j7b EMDB-61200, PDB-9j7b: local refinement of FEM1B bound with TOM20(tetramer) 手法: EM (単粒子) / 解像度: 4.12 Å 61362 9jce EMDB-61362, PDB-9jce: local refinement of FEM1B bound with TOM20 手法: EM (単粒子) / 解像度: 3.59 Å 63187 9lkx EMDB-63187, PDB-9lkx: local refinement of FEM1B bound with PLD6 手法: EM (単粒子) / 解像度: 3.76 Å 63188 9lky EMDB-63188, PDB-9lky: Dimer of CRL2-FEM1B bound with PLD6 手法: EM (単粒子) / 解像度: 3.93 Å
化合物	ChemComp-ZN: Unknown entry
由来	homo sapiens (ヒト)
キーワード	PROTEIN BINDING / ubiquitination E3 ligase / Cryo-EM