TITLE

Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation

AUTHOR(S)
Ji, Z.; Degerny, C.; Vintonenko, N.; Deheuninck, J.; Foveau, B.; Leroy, C.; Coll, J.; Tulasne, D.; Baert, J.-L.; Fafeur, V.
PUB. DATE
January 2007
SOURCE
Oncogene;1/18/2007, Vol. 26 Issue 3, p395
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Sumoylation and ubiquitinylation reversibly regulate the activity of transcription factors through covalent attachment to lysine residues of target proteins. We examined whether the Ets-1 transcription factor is modified by sumoylation and/or ubiquitinylation. Among four potential SUMO motifs in Ets-1, we identified lysines 15 and 227 within the LK15YE and IK227QE motifs, as being the sumoylation acceptor sites. Using transfection of Ets-1 wildtype (WT) or its sumoylation deficient version (Ets-1 K15R/K227R), as well as WT or mutant proteins of the SUMO pathway, we further demonstrated that the E2 SUMO-conjugating enzyme Ubc9 and a E3 SUMO ligase, PIASy, can enhance Ets-1 sumoylation, while a SUMO protease, SENP1, can desumoylate Ets-1. We also found that Ets-1 is modified by K48-linked polyubiquitinylation independently of the sumoylation acceptor sites and is degraded through the 26S proteasome pathway, while sumoylation of Ets-1 does not affect its stability. Finally, sumoylation of Ets-1 leads to reduced transactivation and we demonstrated that previously identified critical lysine residues in Synergistic Control motifs are the sumoylation acceptor sites of Ets-1. These data show that Ets-1 can be modified by sumoylation and/or ubiquitinylation, with sumoylation repressing transcriptional activity of Ets-1 and having no clear antagonistic action on the ubiquitin-proteasome degradation pathway.Oncogene (2007) 26, 395–406. doi:10.1038/sj.onc.1209789; published online 24 July 2006
ACCESSION #
23717154

 

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