Identification of COMMD1 as a novel lamin A binding partner

Jiang,Zhiwen; Chen,Weichun; Zhou,Jing; Peng,Qi; Zheng,Huiling; Yuan,Yuan; Cui,Hongjing; Zhao,Wei; Sun,Xuerong; Zhou,Zhongjun; Liu,Xinguang

doi:10.3892/mmr.2019.10419

Identification of COMMD1 as a novel lamin A binding partner

Authors:
- Zhiwen Jiang
- Weichun Chen
- Jing Zhou
- Qi Peng
- Huiling Zheng
- Yuan Yuan
- Hongjing Cui
- Wei Zhao
- Xuerong Sun
- Zhongjun Zhou
- Xinguang Liu
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Affiliations: Institute of Aging Research, Guangdong Provincial Key Laboratory of Medical Molecular Diagnostics, Guangdong Medical University, Dongguan, Guangdong 523808, P.R. China, Department of Biochemistry, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong, SAR, P.R. China
Published online on: June 24, 2019 https://doi.org/10.3892/mmr.2019.10419
Pages: 1790-1796
Copyright: © Jiang et al. This is an open access article distributed under the terms of Creative Commons Attribution License.

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Abstract

Lamin A, which is encoded by the LMNA gene, regulates gene expression and genome stability through interactions with a variety of proteins. Mutations in LMNA lead to a diverse set of inherited human diseases, collectively referred to as laminopathies. To gain insight into the protein interactions of lamin A, a yeast two‑hybrid screen was conducted using the carboxy‑terminus of lamin A. The screen identified copper metabolism MURR1 domain‑containing 1 (COMMD1) as a novel lamin A binding partner. Colocalization experiments using fluorescent confocal microscopy revealed that COMMD1 colocalized with lamin A in 293 cells. Furthermore, the COMMD1‑lamin A protein interaction was also demonstrated in co‑immunoprecipitation experiments. Collectively, the present study demonstrated a physical interaction between COMMD1 and lamin A, which may aid to elucidate the mechanisms of lamin A in the aging process.

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