Elucidating the transactivation domain of the pleiotropic transcription factor Myrf

Scientific Reports
Jin-Ok ChoiYungki Park

Abstract

Myrf is a newly discovered membrane-bound transcription factor that plays an essential role in as diverse organisms as human, worm, and slime mold. Myrf is generated as a type-II membrane protein in the endoplasmic reticulum (ER). It forms homo-oligomers to undergo auto-cleavage that releases Myrf N-terminal fragment from the ER membrane as a homo-trimer. The homo-trimer of Myrf N-terminal fragments enters the nucleus and binds the Myrf motif to activate transcription. Despite its prominent role as a transcriptional activator, little is known about the transactivation domain of Myrf. Here, we report that the N-terminal-most (NTM) domain of Myrf is required for transcriptional activity and, when fused to a Gal4 fragment, enables it to activate transcription. The transactivation function of the NTM domain did not require homo-trimerization. We also discovered that the NTM domain can be sumoylated at three lysine residues (K123, K208, and K276), with K276 serving as the main acceptor. K276 sumoylation repressed the transactivation function of the NTM domain without affecting the stability or nuclear localization of Myrf N-terminal fragment. In sum, this study identifies the NTM domain as the transactivation domain of Myrf and the ...Continue Reading

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Citations

Sep 12, 2019·Human Molecular Genetics·Dongkyeong Kim, Yungki Park
Aug 1, 2019·Scientific Reports·Dongkyeong KimYungki Park
Apr 3, 2021·The Journal of Biological Chemistry·Chuandong FanYungki Park
Jul 8, 2021·Human Molecular Genetics·Dongkyeong KimYungki Park

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Methods Mentioned

BETA
pulldown
sumoylation
immunoprecipitation
transfection
ChIP-seq

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