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Article: Identification of COMMD1 as a novel lamin A binding partner

TitleIdentification of COMMD1 as a novel lamin A binding partner
Authors
KeywordsInfluenza vaccines
Live attenuated vaccine
NS1
Issue Date2019
PublisherSpandidos Publications. The Journal's web site is located at http://www.spandidos-publications.com/mmr/
Citation
Molecular Medicine Reports, 2019, v. 20 n. 2, p. 1790-1796 How to Cite?
AbstractLamin 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.
Descriptioneid_2-s2.0-85068690245
Persistent Identifierhttp://hdl.handle.net/10722/277179
ISSN
2017 Impact Factor: 1.922
2015 SCImago Journal Rankings: 0.637
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorJiang, Z-
dc.contributor.authorChen, W-
dc.contributor.authorZhou, J-
dc.contributor.authorPeng, Q-
dc.contributor.authorZheng, H-
dc.contributor.authorYuan, Y-
dc.contributor.authorCui, H-
dc.contributor.authorZhao, W-
dc.contributor.authorSun, X-
dc.contributor.authorZhou, Z-
dc.contributor.authorLiu, X-
dc.date.accessioned2019-09-20T08:46:07Z-
dc.date.available2019-09-20T08:46:07Z-
dc.date.issued2019-
dc.identifier.citationMolecular Medicine Reports, 2019, v. 20 n. 2, p. 1790-1796-
dc.identifier.issn1791-2997-
dc.identifier.urihttp://hdl.handle.net/10722/277179-
dc.descriptioneid_2-s2.0-85068690245-
dc.description.abstractLamin 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.-
dc.languageeng-
dc.publisherSpandidos Publications. The Journal's web site is located at http://www.spandidos-publications.com/mmr/-
dc.relation.ispartofMolecular Medicine Reports-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectInfluenza vaccines-
dc.subjectLive attenuated vaccine-
dc.subjectNS1-
dc.titleIdentification of COMMD1 as a novel lamin A binding partner-
dc.typeArticle-
dc.identifier.emailZhou, Z: zhongjun@hku.hk-
dc.identifier.authorityZhou, Z=rp00503-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.3892/mmr.2019.10419-
dc.identifier.pmid31257505-
dc.identifier.pmcidPMC6625409-
dc.identifier.hkuros305491-
dc.identifier.volume20-
dc.identifier.issue2-
dc.identifier.spage1790-
dc.identifier.epage1796-
dc.publisher.placeGreece-

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