ArticlePloS one2012
Contribution of DEAF1 structural domains to the interaction with the breast cancer oncogene LMO4.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 1 citations in OpenAlex.
- Genome-wide association study in East Asians identifies two novel breast cancer susceptibility loci.Human molecular genetics · 2016Trial
- A new method for network bioinformatics identifies novel drug targets for mucinous ovarian carcinoma.NAR genomics and bioinformatics · 2024Article
- Transcriptional Regulation of the Human 5-HT1A Receptor Gene by Lithium: Role of Deaf1 and GSK3β.International journal of molecular sciences · 2023Article
- Zinc finger myeloid Nervy DEAF-1 type (ZMYND) domain containing proteins exert molecular interactions to implicate in carcinogenesis.Discover oncology · 2022Review
- LMO4 mediates trastuzumab resistance in HER2 positive breast cancer cells.American journal of cancer research · 2018Article
- A data-driven structural model of hSSB1 (NABP2/OBFC2B) self-oligomerization.Nucleic acids research · 2017Article
- A structural analysis of DNA binding by hSSB1 (NABP2/OBFC2B) in solution.Nucleic acids research · 2016Article
- BS69/ZMYND11 C-Terminal Domains Bind and Inhibit EBNA2.PLoS pathogens · 2016Article
- Mutations affecting the SAND domain of DEAF1 cause intellectual disability with severe speech impairment and behavioral problems.American journal of human genetics · 2014Article
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- DEAF1 is a Pellino1-interacting protein required for interferon production by Sendai virus and double-stranded RNA.The Journal of biological chemistry · 2013Article
- LIM-domain-only proteins in cancer.Nature reviews. Cancer · 2013Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.