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. 2024 Dec 20;117(1):e2400096. doi: 10.1111/boc.202400096

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© 2024 The Author(s). Biology of the Cell published by Wiley‐VCH GmbH on behalf of Société Française des Microscopies and Société de Biologie Cellulaire de France.

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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PPIns regulate the transcriptional activity of SF‐1. The steroidogenic factor 1(SF‐1) and the liver hormone receptor (LHR‐1) belong to the NR5A family of orphan nuclear receptors. PI(4,5)P2 binds to the ligand binding domain of SF‐1 (LBD) through its acyl chains. PI(4,5)P2 is converted to PI(3,4,5)P3 by the inositol polyphosphate multikinase (IPMK), resulting in SF‐1 transcriptional activation. The phosphatase and tensin homolog deleted on chromosome 10 (PTEN) acts antagonistically to IPMK to shut down SF‐1 transcriptional activity. The inositol headgroup of PI(3,4,5)P3 that faces the cytosol may recruit additional, yet unknown, nuclear transcription factors.