Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.

The proteins LMO4 and DEAF1 contribute to the proliferation of mammary epithelial cells. During breast cancer LMO4 is upregulated, affecting its interaction with other protein partners. This may set cells on a path to tumour formation. LMO4 and DEAF1 interact, but it is unknown how they cooperate to...

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Main Authors: Liza Cubeddu, Soumya Joseph, Derek J Richard, Jacqueline M Matthews
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2012-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3378519?pdf=render
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author Liza Cubeddu
Soumya Joseph
Derek J Richard
Jacqueline M Matthews
author_facet Liza Cubeddu
Soumya Joseph
Derek J Richard
Jacqueline M Matthews
author_sort Liza Cubeddu
collection DOAJ
description The proteins LMO4 and DEAF1 contribute to the proliferation of mammary epithelial cells. During breast cancer LMO4 is upregulated, affecting its interaction with other protein partners. This may set cells on a path to tumour formation. LMO4 and DEAF1 interact, but it is unknown how they cooperate to regulate cell proliferation. In this study, we identify a specific LMO4-binding domain in DEAF1. This domain contains an unstructured region that directly contacts LMO4, and a coiled coil that contains the DEAF1 nuclear export signal (NES). The coiled coil region can form tetramers and has the typical properties of a coiled coil domain. Using a simple cell-based assay, we show that LMO4 modulates the activity of the DEAF NES, causing nuclear accumulation of a construct containing the LMO4-interaction region of DEAF1.
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spelling doaj.art-811f90489a804e098a98e159490a72dd2022-12-22T00:16:33ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0176e3921810.1371/journal.pone.0039218Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.Liza CubedduSoumya JosephDerek J RichardJacqueline M MatthewsThe proteins LMO4 and DEAF1 contribute to the proliferation of mammary epithelial cells. During breast cancer LMO4 is upregulated, affecting its interaction with other protein partners. This may set cells on a path to tumour formation. LMO4 and DEAF1 interact, but it is unknown how they cooperate to regulate cell proliferation. In this study, we identify a specific LMO4-binding domain in DEAF1. This domain contains an unstructured region that directly contacts LMO4, and a coiled coil that contains the DEAF1 nuclear export signal (NES). The coiled coil region can form tetramers and has the typical properties of a coiled coil domain. Using a simple cell-based assay, we show that LMO4 modulates the activity of the DEAF NES, causing nuclear accumulation of a construct containing the LMO4-interaction region of DEAF1.http://europepmc.org/articles/PMC3378519?pdf=render
spellingShingle Liza Cubeddu
Soumya Joseph
Derek J Richard
Jacqueline M Matthews
Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.
PLoS ONE
title Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.
title_full Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.
title_fullStr Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.
title_full_unstemmed Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.
title_short Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.
title_sort contribution of deaf1 structural domains to the interaction with the breast cancer oncogene lmo4
url http://europepmc.org/articles/PMC3378519?pdf=render
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AT derekjrichard contributionofdeaf1structuraldomainstotheinteractionwiththebreastcanceroncogenelmo4
AT jacquelinemmatthews contributionofdeaf1structuraldomainstotheinteractionwiththebreastcanceroncogenelmo4