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FLI-1 Functionally Interacts with PIASxα, a Member of the PIAS E3 SUMO Ligase Family

Abstract : FLI-1 is a transcription factor of the ETS family that is involved in several developmental processes and that becomes oncogenic when overexpressed or mutated. As the functional regulators of FLI-1 are largely unknown, we performed a yeast two-hybrid screen with FLI-1 and identified the SUMO E3 ligase PIASxalpha/ARIP3 as a novel in vitro and in vivo binding partner of FLI-1. This interaction involved the ETS domain of FLI-1 and required the integrity of the SAP domain of PIASxalpha/ARIP3. SUMO-1 and Ubc9, the ubiquitin carrier protein component in the sumoylation pathway, were also identified as interactors of FLI-1. Both PIASxalpha/ARIP3 and the closely related PIASxbeta isoform specifically enhanced sumoylation of FLI-1 at Lys(67), located in its N-terminal activation domain. PIASxalpha/ARIP3 relocalized the normally nuclear but diffusely distributed FLI-1 protein to PIASxalpha nuclear bodies and repressed FLI-1 transcriptional activation as assessed using different ETS-binding site-dependent promoters and different cell systems. PIASxalpha repressive activity was independent of sumoylation and did not result from inhibition of FLI-1 DNA-binding activity. Analysis of the properties of a series of ARIP3 mutants showed that the repressive properties of PIASxalpha/ARIP3 require its physical interaction with FLI-1, identifying PIASxalpha as a novel corepressor of FLI-1.
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Submitted on : Wednesday, May 26, 2021 - 2:53:51 PM
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Emile van den Akker, Sabine Ano, Hsiu-Ming Shih, Ling-Chi Wang, Martine Pironin, et al.. FLI-1 Functionally Interacts with PIASxα, a Member of the PIAS E3 SUMO Ligase Family. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280 (45), pp.38035-38046. ⟨10.1074/jbc.M502938200⟩. ⟨pasteur-03237002⟩



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