Scott Peck

Scott C. Peck

Associate Professor
Department of Biochemistry

Office address: 271H Bond Life Sciences Center, University of Missouri
Office phone: (573) 882-8102
Fax: (573) 884-9676

Research Interest

Proteomics of protein phosphorylation and protein kinases; signaling and secretion during host-pathogen interactions.


The perception of and response to microbial signal molecules is a vital strategy evolved by plants to survive attacks by potential pathogens. Substantial evidence exists for the requirement of phosphorylation to initiate a range of defense-related responses. The identity of the phosphorylated proteins and their role in defense, however, remains largely unknown. To uncover new subsets of signaling candidates, my laboratory has developed complementary proteomic approaches to identify proteins undergoing phosphorylation in Arabidopsis cells within minutes after the application of microbial elicitors. This program has revealed more than 40 novel components associated with defense responses. We have also used reverse genetics to demonstrate that at least some of these phosphoproteins play important roles in resistance to microbes. Our next goal is to complete the pathways linking elicitor perception to the phosphorylation of these signaling components.

These initial studies on protein phosphorylation lead us to investigate the role of protein secretion in defense. We discovered a syntaxin, AtSYP132, that is essential for multiple forms of resistance to bacteria; and this syntaxin appears to be required for the secretion of antimicrobial proteins and/or compounds. A more in-depth proteomic analysis of proteins secreted during interactions between Arabidopsis and different genotypes of bacterial pathogens has revealed a complex, extracellular interaction. We are now investigating the molecular basis of these changes in protein secretion.

Selected Publications