7E34

Crystal structure of SUN1-Speedy A-CDK2

Summary for 7E34

• Entry DOI: 10.2210/pdb7e34/pdb
• Descriptor: Cyclin-dependent kinase 2, Speedy protein A, SUN domain-containing protein 1, ... (6 entities in total)
• Functional Keywords: telomere, meiosis, kinase, cell cycle
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 57726.71

Authors

Chen, Y.,Huang, C.,Wu, J.,Lei, M. (deposition date: 2021-02-08, release date: 2021-04-14, Last modification date: 2023-11-29)

Primary citation

Chen, Y.,Wang, Y.,Chen, J.,Zuo, W.,Fan, Y.,Huang, S.,Liu, Y.,Chen, G.,Li, Q.,Li, J.,Wu, J.,Bian, Q.,Huang, C.,Lei, M.
The SUN1-SPDYA interaction plays an essential role in meiosis prophase I.
Nat Commun, 12:3176-3176, 2021

PubMed Abstract: Chromosomes pair and synapse with their homologous partners to segregate correctly at the first meiotic division. Association of telomeres with the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex composed of SUN1 and KASH5 enables telomere-led chromosome movements and telomere bouquet formation, facilitating precise pairwise alignment of homologs. Here, we identify a direct interaction between SUN1 and Speedy A (SPDYA) and determine the crystal structure of human SUN1-SPDYA-CDK2 ternary complex. Analysis of meiosis prophase I process in SPDYA-binding-deficient SUN1 mutant mice reveals that the SUN1-SPDYA interaction is required for the telomere-LINC complex connection and the assembly of a ring-shaped telomere supramolecular architecture at the nuclear envelope, which is critical for efficient homologous pairing and synapsis. Overall, our results provide structural insights into meiotic telomere structure that is essential for meiotic prophase I progression.

PubMed: 34039995
DOI: 10.1038/s41467-021-23550-w

Experimental method

X-RAY DIFFRACTION (3.19 Å)