Plants constantly face changing conditions in their environment. Unravelling the transduction mechanisms from signal perception at the plasma membrane level down to gene expression in the nucleus is a fascinating challenge. Protein phosphorylation, catalysed by protein kinases, is one of the major posttranslational modifications involved in the specificity, kinetic(s) and intensity of a signal transduction pathway. Although commonly assumed, the involvement of nuclear protein kinases in signal transduction is often poorly characterized. In particular, both their regulation and mode of action remain to be elucidated and may lead to the unveiling of new original mechanisms. For example, unlike animal cells, plant cells contain only a few strictly nucleus-localized protein kinases, which calls into question the role of this cellular distribution between the cytosol and the nucleus in their activation and functions. The control of their nucleocytoplasmic trafficking appears to play a major role in their regulation, probably through promoting interactions with their substrates under specific cellular conditions. However, recent findings showing that the nucleus can generate complex networks of second messengers (e.g. Ca(2+)or diacyglycerol) suggest that nuclear protein kinases could play an active role in the decoding of such signals.