Plant adenylate cyclases have come full circle

In bacteria, fungi and animals, 3 & PRIME;-5 & PRIME;-cyclic adenosine monophosphate (cAMP) and adenylate cyclases (ACs), enzymes that catalyse the formation of 3 & PRIME;,5 & PRIME;-cAMP from ATP, are recognized as key signalling components. In contrast, the presence of cAMP and its biological roles in higher plants have long been a matter of controversy due to the generally lower amounts in plant tissues compared with that in animal and bacterial cells, and a lack of clarity on the molecular nature of the generating and degrading enzymes, as well as downstream effectors. While treatment with 3 & PRIME;,5 & PRIME;-cAMP elicited many plant responses, ACs were, however, somewhat elusive. This changed when systematic searches with amino acid motifs deduced from the conserved catalytic centres of annotated ACs from animals and bacteria identified candidate proteins in higher plants that were subsequently shown to have AC activities in vitro and in vivo. The identification of active ACs moonlighting within complex multifunctional proteins is consistent with their roles as molecular tuners and regulators of cellular and physiological functions. Furthermore, the increasing number of ACs identified as part of proteins with different domain architectures suggests that there are many more hidden ACs in plant proteomes and they may affect a multitude of mechanisms and processes at the molecular and systems levels. This Perspective presents an historical overview and recent advances on adenylate cyclases (ACs) and cAMP signalling in plants, including an exploration of the active AC functions moonlighting within multifunctional protein complexes.

Automated summary

This article provides a historical overview and recent advances in adenylate cyclases (ACs) and cAMP signaling in plants, including the exploration of the active AC functions within multifunctional protein complexes.