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Post Translational Modifications by PAK6 and CARM1 Regulate p54nrb Function

In the human adrenal cortex, transcription of CYP17 is regulated by adrenocorticotropin (ACTH), which activates a cAMP/cAMP‐dependent protein kinase (PKA) signal transduction pathway. ACTH/cAMP triggers a series of events, including reciprocal presence of coactivator and corepressor complexes on the promoter of CYP17. One of the proteins that binds to the CYP17 gene is the splicing/transcription factor p54nrb, a ubiquitously expressed 54‐kDa, non‐POU domain‐containing protein that activates CYP17 transcription by forming a trimeric complex with steroidogenic factor 1 (SF‐1) and polypyrimidine‐tract‐binding protein‐associated splicing factor (PSF). p54nrb is known to couple transcription and splicing by interacting with both RNA Polymerase II (Pol II) and splicing factors. In this study, we show that phosphorylation and methylation by p‐21 activated kinase (PAK) 6 and coactivator associated arginine methyltransferase (CARM1), respectively, control the coactivator potential of p54nrb by modulating interactions with Pol II and SF‐1. We show that PAK6 and CARM1 are essential for transcription of CYP17 and identify them as key effectors in ACTH/cAMP‐stimulated CYP17 gene expression.