Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.
| Field | Value | Language |
| dc.contributor.author | Cubeddu, Liza | |
| dc.contributor.author | Joseph, Soumya | |
| dc.contributor.author | Richard, D.J. | |
| dc.contributor.author | Matthews, Jacqueline | |
| dc.date.accessioned | 2014-01-23 | |
| dc.date.available | 2014-01-23 | |
| dc.date.issued | 2012-06-19 | |
| dc.identifier.citation | Cubeddu, L., Joseph, S., Richard, D.J., and Matthews, J.M., (2012) Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4. PloS One, 7: p. e39218. | en |
| dc.identifier.uri | http://hdl.handle.net/2123/9919 | |
| dc.description.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 | en |
| dc.description.sponsorship | Australian Research Council and the Association for International Cancer Research | en |
| dc.language.iso | en | en |
| dc.publisher | Public Library of Science | en |
| dc.relation | ARC DP0985020 | en |
| dc.rights | Copyright All Rights Reserved | en |
| dc.subject | LMO4 | en |
| dc.subject | DEAF1 | en |
| dc.subject | Intrinsically disordered proteins | en |
| dc.subject | Protein-protein interactions | en |
| dc.title | Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4. | en |
| dc.type | Article | en |
| dc.subject.asrc | FoR::060109 - Proteomics and Intermolecular Interactions (excl. Medical Proteomics) | en |
| dc.identifier.doi | 10.1371/journal.pone.0039218 | |
| dc.type.pubtype | Publisher's version | en |
| dc.relation.arc | DP0985020 | |
| usyd.faculty | SeS faculties schools::Faculty of Science | en |
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