ArticleMolecular and cellular biochemistry2011
Eukaryotic translation elongation factor 1 delta inhibits the ubiquitin ligase activity of SIAH-1.
Article in Molecular and cellular biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Interfering with the expression of EEF1D gene enhances the sensitivity of ovarian cancer cells to cisplatin.BMC cancer · 2022Article
- The role of EEF1D in disease pathogenesis: a narrative review.Annals of translational medicine · 2021Review
- Host cell factors stimulate HIV-1 transcription by antagonizing substrate-binding function of Siah1 ubiquitin ligase to stabilize transcription elongation factor ELL2.Nucleic acids research · 2020Article
- Non-translational Connections of eEF1B in the Cytoplasm and Nucleus of Cancer Cells.Frontiers in molecular biosciences · 2020Review
- EEF1D overexpression promotes osteosarcoma cell proliferation by facilitating Akt-mTOR and Akt-bad signaling.Journal of experimental & clinical cancer research : CR · 2018Article
- Independent overexpression of the subunits of translation elongation factor complex eEF1H in human lung cancer.BMC cancer · 2014Article
- Article
- Regulators and effectors of Siah ubiquitin ligases.Cell biochemistry and biophysics · 2013Review
- SIAH proteins: critical roles in leukemogenesis.Leukemia · 2013Review
- The many roles of the eukaryotic elongation factor 1 complex.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SIAH-1, an E3 ubiquitin ligase, plays an important role in regulating cell cycle, tumorigenesis and several neurodegenerative diseases. In this study, we found a novel SIAH-1-interacting protein, EEF1D (Eukaryotic translation elongation factor 1 delta). The interaction was confirmed in vitro and in vivo, and both proteins were co-localized in the cytoplasm. The Cys-rich domain of SIAH-1 was essential for its interaction with EEF1D. Overexpressing SIAH-1 had no effect on the protein level of EEF1D, implying that EFF1D is not the substrate of SIAH-1. In contrast, the protein level of SIAH-1 increased significantly in the cells overexpressing EEF1D. Increased amount of SIAH-1 was caused by the EEF1D-mediated inhibition of auto-ubiquitination and degradation of SIAH-1. Furthermore, EEF1D was able to inhibit the degradation of HPH2, a known substrate of SIAH-1. Taken together, our data suggest EFF1D functions as a novel negative regulator of SIAH-1.
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Registered trials
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