CAMSAP3 forms dimers via its α-helix domain that directly stabilize non-centrosomal microtubule minus ends

Microtubules are vital components of the cytoskeleton. Their plus ends are dynamic and respond to changes in cell morphology, whereas the minus ends are stable and serve a crucial role in microtubule seeding and maintaining spatial organization. In mammalian cells, the calmodulin-regulated spectrin-associated proteins (CAMSAPs), play a key role in directly regulating the dynamics of non-centrosomal microtubules minus ends. However, the molecular mechanisms are not yet fully understood. Our study reveals that CAMSAP3 forms dimers through its C-terminal α-helix; this dimerization not only enhances the microtubule-binding affinity of the CKK domain but also enables the CKK domain to regulate the dynamics of microtubules. Furthermore, CAMSAP3 also specializes in decorating at the minus end of microtubules through the combined action of the microtubule-binding domain (MBD) and the C-terminal α-helix, thereby achieving dynamic regulation of the minus ends of microtubules. These findings are crucial for advancing our understanding and treatment of diseases associated with non-centrosomal microtubules.

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Publication Details

Journal
Journal of Cell Science
Published
2024-10-31
DOI
https://doi.org/10.1242/jcs.263609
Citations
2
Primary Topic
Microtubule and mitosis dynamics
Type
article
Field-Weighted Citation Impact
0.65

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article

CAMSAP3 forms dimers via its α-helix domain that directly stabilize non-centrosomal microtubule minus ends

Wenxiang Meng, Haisu Cheng, Zhengrong Zhou, Wei Chen et al.
2 citations
Journal of Cell Science
Microtubule and mitosis dynamics
0.65
article

CAMSAP3 forms dimers via its α-helix domain that directly stabilize non-centrosomal microtubule minus ends

Wenxiang Meng, Haisu Cheng, Zhengrong Zhou, Wei Chen, Wei Feng, Jinqi Ren, Dong Li, Rui Zhang, Qi Xie, Honglin Xu, Yuejia Li, Wei Ji
article en
2 citations

Abstract

Microtubules are vital components of the cytoskeleton. Their plus ends are dynamic and respond to changes in cell morphology, whereas the minus ends are stable and serve a crucial role in microtubule seeding and maintaining spatial organization. In mammalian cells, the calmodulin-regulated spectrin-associated proteins (CAMSAPs), play a key role in directly regulating the dynamics of non-centrosomal microtubules minus ends. However, the molecular mechanisms are not yet fully understood. Our study reveals that CAMSAP3 forms dimers through its C-terminal α-helix; this dimerization not only enhances the microtubule-binding affinity of the CKK domain but also enables the CKK domain to regulate the dynamics of microtubules. Furthermore, CAMSAP3 also specializes in decorating at the minus end of microtubules through the combined action of the microtubule-binding domain (MBD) and the C-terminal α-helix, thereby achieving dynamic regulation of the minus ends of microtubules. These findings are crucial for advancing our understanding and treatment of diseases associated with non-centrosomal microtubules.

Journal of Cell ScienceVol. 137(23)
McGovern Institute for Brain Research (US), Chinese Academy of Sciences (CN), Chinese Academy of Medical Sciences & Peking Union Medical College (CN), Shantou University (CN), Guangzhou Regenerative Medicine and Health Guangdong Laboratory (CN), Shantou University Medical College (CN), Institute of Genetics and Developmental Biology (CN), Wangjing Hospital of China Academy of Chinese Medical Sciences (CN), University of Chinese Academy of Sciences (CN), State Key Laboratory of Molecular Developmental Biology, Tsinghua University (CN)
National Natural Science Foundation of China
Openalex Percentile: Top 31%
Microtubule and mitosis dynamics
0.65
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