ArticleNucleic acids research2000
The mechanism of complex formation between Fli-1 and SRF transcription factors.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Inositol polyphosphate multikinase is a coactivator for serum response factor-dependent induction of immediate early genes.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Regulation of endothelial cell development by ETS transcription factors.Seminars in cell & developmental biology · 2011Review
- Thrombocytopenia in mice lacking the carboxy-terminal regulatory domain of the Ets transcription factor Fli1.Molecular and cellular biology · 2010Article
- Biology of EWS/ETS fusions in Ewing's family tumors.Oncogene · 2001Review
- The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex.The EMBO journal · 2001Article
- Temporal recruitment of the mSin3A-histone deacetylase corepressor complex to the ETS domain transcription factor Elk-1.Molecular and cellular biology · 2001Article
- The Ets-transcription factor family in embryonic development: lessons from the amphibian and bird.Oncogene · 2000Review
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- Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors.The EMBO journal · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The mechanisms of multicomponent transcription factor complex assembly are currently poorly defined. A paradigm for this type of complex is the ETS-domain transcription factor Elk-1 and the MADS-box transcription factor SRF which form a ternary complex with the c- fos serum response element (SRE). In this study we have analysed how a different ETS-domain transcription factor Fli-1 interacts with SRF to form ternary complexes with this element. Two regions of Fli-1 that are required for ternary complex formation have been identified. These SRF binding motifs are located on either side of the ETS DNA-binding domain. Hydrophobic amino acids within these motifs have been identified that play important roles in binding to SRF and ternary complex formation. By using Fli-1 derivatives with mutations in the N-terminal SRF binding motif, the significance of Fli-1-SRF interactions in recruitment of Fli-1 to the c- fos SRE in vivo has been demonstrated. Collectively our data provide a model of how Fli-1 interacts with SRF that differs significantly from the mechanism used by a different ETS-domain protein, Elk-1.
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Registered trials
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.