6QJA

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

Summary for 6QJA

• Entry DOI: 10.2210/pdb6qja/pdb
• Descriptor: Nuclear mitotic apparatus protein 1, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: hook domain, motor protein-associated, structural protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 71337.09

Authors

Renna, C.,Rizzelli, F.,Carminati, M.,Gaddoni, C.,Pirovano, L.,Cecatiello, V.,Pasqualato, S.,Mapelli, M. (deposition date: 2019-01-23, release date: 2020-02-05, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.54 Å)