Polyamine-modulated factor 1 represses glucocorticoid receptor activity.
Polyamine-modulated factor 1 (PMF-1) has been reported to interact with NF-E2 related factor 2 (Nrf-2) and activate the polyamine-induced transcription of spermidine/spermine N(1)-acetyltransferase (SSAT) gene. Polyamines are important regulators of cell growth and cell death and have been implicated in glucocorticoid-induced apoptosis. In the present study, we have identified and characterized new functional binding partners for PMF-1. Our results demonstrate that PMF-1 binds to the glucocorticoid receptor (GR). PMF-1 also represses glucocorticoid-induced transcription. Furthermore, we show that PMF-1 has an intrinsic repression activity, which could contribute to the repressive effect on GR. PMF-1 can also interact with the GR corepressor, receptor-interacting protein 140 (RIP140), but does not further enhance the repressive effect of RIP140. Our results suggest that PMF-1 has a broader function in regulation of genes and can contribute to glucocorticoid signaling.
Shoji
Yutaka
Y
Department of Biosciences and Nutrition, Karolinska Institutet, Novum, SE-141 86 Huddinge, Sweden.
Osman
Waffa
W
Zilliacus
Johanna
J
D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D051379:Mice; D009687:Nuclear Proteins / Q000378:metabolism; D000078723:Nuclear Receptor Interacting Protein 1; D011965:Receptors, Glucocorticoid / Q000037:antagonists & inhibitors*; D012097:Repressor Proteins / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism*; D015533:Transcriptional Activation
D048868:Adaptor Proteins, Signal Transducing; D009687:Nuclear Proteins; D000078723:Nuclear Receptor Interacting Protein 1; C486540:Pmf1 protein, mouse; D011965:Receptors, Glucocorticoid; D012097:Repressor Proteins; D014157:Transcription Factors