Analysis of the phosphorylation of serine 280 in activation of Arabidopsis thaliana phospholipase C2 (AtPLC2).

ORIANA MARIANI, FERNANDO VILLARREAL, ANA M. LAXALT

Santa Fe

Congreso; RAFV; 2021

Plants have developed different strategies to respond to external stimuli. Recognition of these stimuli leads to intracellular signaling events via second messengers. Phospholipase C (PLC) are enzymes present in animals and plants that hydrolyze phosphoinositides producing two second messengers: diacylglycerol (DAG) and inositol phosphates (IPs). The structure and function of these enzymes has been extensively studied in animals, but little information is available in plants. The Arabidopsis thaliana genome encodes for 9 PLC, which are involved in the response to diverse stimuli both, biotic, abiotic and developing. In particular, our laboratory has proven that AtPLC2 plays a role in the immune response to biotic stress. In addition, phosphoproteomics studies report phosphorylation of S280 in response to the same stimulus. The objective is to determine the role of S280 phosphorylation on AtPLC2 biological activity through computational biology approaches and in vitro activity. The putative orthologues of AtPLC2 were identified by phylogeny, and we found that S280 is not strictly conserved. However, computational studies identified sites located in regulatory regions of the protein that could be involved in membrane location and binding, as well as regulatory processes. This work establishes a basis for designing and carrying out future experiments that would clarify notions not yet studied in plant PLCs enzymes.