1. Centromere/kinetochore is assembled through CENP-C oligomerization
- Author
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1000030565099, 0000-0001-8433-1111, Hara, Masatoshi, 1000080437243, 0000-0002-1361-2642, Ariyoshi, Mariko, Sano, Tomoki, 1000070868710, Nozawa, Ryu-Suke, 1000060547058, Shinkai, Soya, 1000050348843, Onami, Shuichi, Jansen, Isabelle, 1000050421368, Hirota, Toru, 1000060321600, Fukagawa, Tatsuo, 1000030565099, 0000-0001-8433-1111, Hara, Masatoshi, 1000080437243, 0000-0002-1361-2642, Ariyoshi, Mariko, Sano, Tomoki, 1000070868710, Nozawa, Ryu-Suke, 1000060547058, Shinkai, Soya, 1000050348843, Onami, Shuichi, Jansen, Isabelle, 1000050421368, Hirota, Toru, 1000060321600, and Fukagawa, Tatsuo
- Abstract
Hara M., Ariyoshi M., Sano T., et al. Centromere/kinetochore is assembled through CENP-C oligomerization. Molecular Cell 83, 2188 (2023); https://doi.org/10.1016/j.molcel.2023.05.023., Kinetochore is an essential protein complex required for accurate chromosome segregation. The constitutive centromere-associated network (CCAN), a subcomplex of the kinetochore, associates with centromeric chromatin and provides a platform for the kinetochore assembly. The CCAN protein CENP-C is thought to be a central hub for the centromere/kinetochore organization. However, the role of CENP-C in CCAN assembly needs to be elucidated. Here, we demonstrate that both the CCAN-binding domain and the C-terminal region that includes the Cupin domain of CENP-C are necessary and sufficient for chicken CENP-C function. Structural and biochemical analyses reveal self-oligomerization of the Cupin domains of chicken and human CENP-C. We find that the CENP-C Cupin domain oligomerization is vital for CENP-C function, centromeric localization of CCAN, and centromeric chromatin organization. These results suggest that CENP-C facilitates the centromere/kinetochore assembly through its oligomerization.
- Published
- 2023