8PR1

Cytoplasmic dynein-B heavy chain bound to IC-LC tower

これはPDB形式変換不可エントリーです。

8PR1 の概要

• エントリーDOI: 10.2210/pdb8pr1/pdb
• EMDBエントリー: 17831
• 分子名称: Dynein light chain 1, cytoplasmic, Cytoplasmic dynein 1 intermediate chain 2, Dynein light chain Tctex-type 1, ... (6 entities in total)
• 機能のキーワード: dynein, aaa-atpase, lc8, tctex1, motor protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 1378897.79

構造登録者

Singh, K.,Lau, C.K.,Manigrasso, G.,Gassmann, R.,Carter, A.P. (登録日: 2023-07-12, 公開日: 2024-03-27, 最終更新日: 2024-04-10)

主引用文献

Singh, K.,Lau, C.K.,Manigrasso, G.,Gama, J.B.,Gassmann, R.,Carter, A.P.
Molecular mechanism of dynein-dynactin complex assembly by LIS1.
Science, 383:eadk8544-eadk8544, 2024

PubMed Abstract: Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil adaptor. However, how dynein and dynactin recognize diverse adaptors, how they interact with each other during complex formation, and the role of critical regulators such as lissencephaly-1 (LIS1) protein (LIS1) remain unclear. In this study, we determined the cryo-electron microscopy structure of dynein-dynactin on microtubules with LIS1 and the lysosomal adaptor JIP3. This structure reveals the molecular basis of interactions occurring during dynein activation. We show how JIP3 activates dynein despite its atypical architecture. Unexpectedly, LIS1 binds dynactin's p150 subunit, tethering it along the length of dynein. Our data suggest that LIS1 and p150 constrain dynein-dynactin to ensure efficient complex formation.

PubMed: 38547289
DOI: 10.1126/science.adk8544

実験手法

ELECTRON MICROSCOPY (8.2 Å)