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Correction : Ets-1 interacts through a similar binding interface with Ku70 and Poly (ADP-Ribose) Polymerase-1

Abstract : Correction : The Ets-1 transcription factor plays an important role in various physiological and pathological processes. These diverse roles of Ets-1 are likely to depend on its interaction proteins. We have previously showed that Ets-1 interacted with DNA-dependent protein kinase (DNA-PK) complex including its regulatory subunits, Ku70 and Ku86 and with poly (ADP-ribose) polymerase-1 (PARP-1). In this study, the binding domains for the interaction between Ets-1 and these proteins were reported. We demonstrated that the interaction of Ets-1 with DNA-PK was mediated through the Ku70 subunit and was mapped to the C-terminal region of Ets-1 and the C-terminal part of Ku70 including SAP domain. The interactive domains between Ets-1 and PARP-1 have been mapped to the C-terminal region of Ets-1 and the BRCA1 carboxy-terminal (BRCT) domain of PARP-1. The results presented in this study may advance our understanding of the functional link between Ets-1 and its interaction partners, DNA-PK and PARP-1.
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https://hal.inrae.fr/hal-03179839
Contributor : Christopher Lallemant <>
Submitted on : Wednesday, March 24, 2021 - 3:10:42 PM
Last modification on : Thursday, March 25, 2021 - 3:32:16 AM

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Souhaila Choul-Li, Arnaud J Legrand, Baptiste Bidon, Dorothee Vicogne, Vincent Villeret, et al.. Correction : Ets-1 interacts through a similar binding interface with Ku70 and Poly (ADP-Ribose) Polymerase-1. Bioscience, Biotechnology and Biochemistry, Taylor & Francis, 2019, 83 (11), pp.2175-2175. ⟨10.1080/09168451.2019.1590678⟩. ⟨hal-03179839⟩

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