6QJA

Organizational principles of the NuMA-Dynein interaction interface and implications for mitotic spindle functions

6QJA の概要

• エントリーDOI: 10.2210/pdb6qja/pdb
• 分子名称: Nuclear mitotic apparatus protein 1, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: hook domain, motor protein-associated, structural protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 71337.09

構造登録者

Renna, C.,Rizzelli, F.,Carminati, M.,Gaddoni, C.,Pirovano, L.,Cecatiello, V.,Pasqualato, S.,Mapelli, M. (登録日: 2019-01-23, 公開日: 2020-02-05, 最終更新日: 2024-05-15)

主引用文献

Renna, C.,Rizzelli, F.,Carminati, M.,Gaddoni, C.,Pirovano, L.,Cecatiello, V.,Pasqualato, S.,Mapelli, M.
Organizational Principles of the NuMA-Dynein Interaction Interface and Implications for Mitotic Spindle Functions.
Structure, 28:820-829.e6, 2020

PubMed Abstract: Mitotic progression is orchestrated by the microtubule-based motor dynein, which sustains all mitotic spindle functions. During cell division, cytoplasmic dynein acts with the high-molecular-weight complex dynactin and nuclear mitotic apparatus (NuMA) to organize and position the spindle. Here, we analyze the interaction interface between NuMA and the light intermediate chain (LIC) of eukaryotic dynein. Structural studies show that NuMA contains a hook domain contacting directly LIC1 and LIC2 chains through a conserved hydrophobic patch shared among other Hook adaptors. In addition, we identify a LIC-binding motif within the coiled-coil region of NuMA that is homologous to CC1-boxes. Analysis of mitotic cells revealed that both LIC-binding sites of NuMA are essential for correct spindle placement and cell division. Collectively, our evidence depicts NuMA as the dynein-activating adaptor acting in the mitotic processes of spindle organization and positioning.

PubMed: 32413290
DOI: 10.1016/j.str.2020.04.017

実験手法

X-RAY DIFFRACTION (1.54 Å)