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Identification of COMMD1 as a novel lamin A binding partner.


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.

SUBMITTER: Jiang Z 

PROVIDER: S-EPMC6625409 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature

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Identification of COMMD1 as a novel lamin A binding partner.

Jiang Zhiwen Z   Chen Weichun W   Zhou Jing J   Peng Qi Q   Zheng Huiling H   Yuan Yuan Y   Cui Hongjing H   Zhao Wei W   Sun Xuerong X   Zhou Zhongjun Z   Liu Xinguang X  

Molecular medicine reports 20190624 2


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.  ...[more]

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