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

Liza Cubeddu; Soumya Joseph; Derek J. Richard; Jacqueline M. Matthews

doi:10.1371/journal.pone.0039218

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

Liza Cubeddu, Soumya Joseph, Derek J. Richard, Jacqueline M. Matthews

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

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.

Original language	English
Article number	e39218
Number of pages	8
Journal	PLoS One
Volume	7
Issue number	6
DOIs	https://doi.org/10.1371/journal.pone.0039218
Publication status	Published - 2012

Open Access - Access Right Statement

Copyright: 2012 Cubeddu et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Keywords

breast
cancer
breast cancer
protein binding
protein-protein interactions

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1371/journal.pone.0039218

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abstract = "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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AU - Cubeddu, Liza

AU - Joseph, Soumya

AU - Richard, Derek J.

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AB - 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.

KW - breast

KW - cancer

KW - breast cancer

KW - protein binding

KW - protein-protein interactions

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ER -

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

Abstract

Open Access - Access Right Statement

Keywords

UN SDGs

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