Protein kinase C control of gene expression.

Gene expression is fashioned at multiple interconnected levels and is controlled by a complex interplay between nucleosomal assembly, the establishment of multifaceted transcriptional motifs, and the temporal and spatial organization of chromatin in loops and domains. Protein phosphorylation is one of the most versatile posttranslational modifications used in eukaryotic cells and plays a crucial role in the continuous remodeling of different transcriptional regulators. The protein kinase C (PKC) family of serine-threonine kinases encompasses 12 different isozymes that have been shown to transduce a myriad of signals mediated by phospholipid hydrolysis as a consequence of the activation of G protein-coupled receptors, tyrosine kinase receptors, and nonreceptor tyrosine kinases. Although the analysis of PKC activity in many systems has provided crucial insights to its biological function, unraveling the molecular mechanisms that underlie isozyme-specific modulation of gene expression within the complexity of genome structure and function remains a challenging issue. This review focuses on recent advances in PKC-dependent regulation of gene expression within the context of the dynamic linkages involving nuclear architecture and transcription. Implications of isozyme-specific phosphorylation of selected members of transcription factors are also discussed. Future perspectives disclosed by recently available methods for large-scale transcriptional profiling are also outlined.