Enhancement of CEP215 dynamics for spindle pole assembly during mitosis

The microtubule-organizing activity of centrosomes fluctuates during the cell cycle, reaching the highest levels at M phase. CEP215 (also known as CDK5RAP2) is a key pericentriolar material (PCM) protein for microtubule organization of the human centrosome. Here, we provide evidence that CEP215 exhibits a dynamically suppressed, solid-like state in interphase centrosomes, and becomes a more dynamic state in mitotic centrosomes. Specific interaction with PCNT, another centrosome protein, is crucial for diffusible molecular dynamicity of the CEP215 protein. We also found that the cluster formation activity of CEP215 is impaired in a light-inducible system when its coiled-coil domains (CCDs) are truncated. Defects in spindle pole assembly and spindle formation were accompanied in the cells whose CEP215 is replaced with the CCD-truncated mutants. Our results support the notion that the diffusible mobility of CEP215 is enhanced by both homotypic and heterotypic interactions among CCDs, especially at mitotic spindle poles. This work highlights that biophysical properties of the PCM proteins at the centrosomes fluctuate during the cell cycle.

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Publication Details

Journal
Journal of Cell Science
Published
2025-04-24
DOI
https://doi.org/10.1242/jcs.263542
Citations
3
Primary Topic
Microtubule and mitosis dynamics
Type
article
Field-Weighted Citation Impact
3.45

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article

Enhancement of CEP215 dynamics for spindle pole assembly during mitosis

Hyunjeong Yoo, Yongdae Shin, Jeesoo Kim, Donghee Ko et al.
3 citations
Journal of Cell Science
Microtubule and mitosis dynamics
3.45
article

Enhancement of CEP215 dynamics for spindle pole assembly during mitosis

Hyunjeong Yoo, Yongdae Shin, Jeesoo Kim, Donghee Ko, Hee‐Jung Choi, Tae Hyun Kim, Sungjin Ryu, Kunsoo Rhee
article en
3 citations

Abstract

The microtubule-organizing activity of centrosomes fluctuates during the cell cycle, reaching the highest levels at M phase. CEP215 (also known as CDK5RAP2) is a key pericentriolar material (PCM) protein for microtubule organization of the human centrosome. Here, we provide evidence that CEP215 exhibits a dynamically suppressed, solid-like state in interphase centrosomes, and becomes a more dynamic state in mitotic centrosomes. Specific interaction with PCNT, another centrosome protein, is crucial for diffusible molecular dynamicity of the CEP215 protein. We also found that the cluster formation activity of CEP215 is impaired in a light-inducible system when its coiled-coil domains (CCDs) are truncated. Defects in spindle pole assembly and spindle formation were accompanied in the cells whose CEP215 is replaced with the CCD-truncated mutants. Our results support the notion that the diffusible mobility of CEP215 is enhanced by both homotypic and heterotypic interactions among CCDs, especially at mitotic spindle poles. This work highlights that biophysical properties of the PCM proteins at the centrosomes fluctuate during the cell cycle.

Journal of Cell ScienceVol. 138(10)
Seoul National University (KR), Seoul National University of Education (KR), New Generation University College (ET)
National Research Foundation, National Research Foundation of Korea
Openalex Percentile: Top 9%
Microtubule and mitosis dynamics
3.45
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