Cell signaling meets gene transcription.

Cells rely on the selective transcription of genes to maintain their identity and adapt to changing conditions (1, 2). Proteins called transcription factors regulate selective gene transcription in the nucleus by binding to DNA regulatory elements and recruiting RNA polymerase II (Pol II), which then transcribes the genes. Cells can respond to changes in their extracellular environment by using plasma membrane receptors that bind various ligands, which then send signals to the nucleus. For decades, these receptors were thought to use signaling intermediates that act on transcription factors, which then bind gene regulatory elements and regulate Pol II activity. On page 594 of this issue, Dabas et al. (3) report a change to this canonical view, revealing that signaling molecules of the receptor tyrosine kinase (RTK) family can also act directly on a key regulatory domain of Pol II within the nucleus. [ABSTRACT FROM AUTHOR]