SUMOylation can regulate the activity of ETS-like transcription factor 4

Biochimica Et Biophysica Acta
Sanna KaikkonenJorma J Palvimo

Abstract

ETS-like transcription factor 4 (ELK4) (a.k.a. serum response factor accessory protein 1) belongs to the ternary complex factor (TCF) subfamily of E twenty-six (ETS) domain transcription factors. Compared to the other TCF subfamily members, ELK1 and ELK3 (NET), there is limited information of the mechanisms regulating the ELK4 activity. Here, we show that the ELK4 can be covalently modified (SUMOylated) by small ubiquitin-related modifier (SUMO) 1 protein, an important regulator of signaling and transcription. SUMOylation of ELK4 was reversed by SUMO-specific proteases (SENP) 1 and 2 and stimulated by SUMO E3 ligase PIAS3. Conserved lysine residue 167 that is located in the NET inhibitory domain of ELK4 was identified as the main site of SUMO-1 conjugation. Interestingly, mutation of the K167 disrupting the SUMOylation markedly enhanced the transcriptional activity of the ELK4, but weakened its repressive function on c-fos promoter. In conclusion, our results suggest that covalent modification by SUMO-1 can regulate the activity of ELK4, contributing to the transcriptional repression by the ELK4.

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Jun 23, 2012·Nature·Matthew F BarberKatrin F Chua
Nov 24, 2012·Nature Reviews. Molecular Cell Biology·Christopher M HickeyMark Hochstrasser
Nov 2, 2015·Advances in Medical Sciences·Mateusz Wątroba, Dariusz Szukiewicz
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Aug 27, 2015·DNA and Cell Biology·Chun-Jie HuangLi-Jun Huo
Aug 9, 2016·Journal of Pathology and Translational Medicine·Hye Seung LeeBaek-Hui Kim
Mar 21, 2017·The Journal of Immunology : Official Journal of the American Association of Immunologists·Aibo WangChen Dong
Mar 10, 2017·The Biochemical Journal·Erika HookerSerge Lemay

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