Knowledge of the functions of plant receptor-like-kinases (RLKs) is increasing rapidly, but how their cytoplasmic signalling activity is regulated and how signals are transduced to cytoplasmic or nuclear proteins remain important questions. Recent studies, particularly of the BRASSINOSTEROID INSENSITIVE1 RLK, have begun to shed light on the mechanistic details of RLK activation, including the possible role of ligand binding. Studies of this and other RLKs have also highlighted the potential importance of hetero-oligomerisation and receptor internalisation in RLK signalling. Finally, a range of potential regulatory proteins and putative downstream signalling substrates have been identified for various RLKs. Despite some similarities with animal receptor kinase signalling systems, mechanisms that affect the intracellular behaviour, regulation and interactions of RLKs appear to be very diverse, potentially explaining how signalling specificity is maintained at the cytoplasmic level.