Scott C. Peck

Associate Professor of Biochemistry

Email:	pecks@missouri.edu
Phone:	(573) 882-8102
Lab:	(573) 882-7431
Fax:	(573) 884-9676
Office:	271H Bond Life Sciences Center
Mailing Address:	Biochemistry 271H Bond Life Sciences Center University of Missouri-Columbia Columbia, MO 65211
Research Areas:	Proteomics of protein phosphorylation and protein kinases; signaling and secretion during host-pathogen interactions.

Educational Background

PhD		Michigan State University	East Lansing, Mich.	Botany and Plant Pathology
BA		Lawrence University	Appleton, Wisc.	Biology

Notable Honors and Service

BMC Plant Techniques, Co-Editor
The Plant Cell, Co-Editor

Research Description

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

Nühse TS, Bottrill AR, Jones AME, Peck SC (2007) Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses. Plant J 51: 931-940. [Free Access]

Heese A, Hann DR, Gimenez-Ibenaz S, Jones AME, He K, Li J, Schroeder JI, Peck SC, Rathjen JP (2007) The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants. Proc Natl Acad Sci USA 104: 12217-12222. [MEDLINE]

Kalde M, Nühse TS, Findley K, Peck SC (2007) The syntaxin SYP132 contributes to plant resistance against bacteria and secretion of pathogenesis-related protein 1 (PR1). Proc Natl Acad Sci USA 104: 11850-11855. [MEDLINE]

Peck SC (2006) Analysis of Protein Phosphorylation: Methods and Strategies for Studying Kinases and Substrates. Plant J 45: 512-522. [Free Access]

Peck SC (2006) Phosphoproteomics in Arabidopsis: Moving from Empirical to Predictive Science. J Exp Botany 57: 1523-1527 . [Free Access]

Thomas S. Nühse, Allan Stensballe, Ole N. Jensen, and Scott C. Peck. (2004) Phosphoproteomics of the Arabidopsis Plasma Membrane and a New Phosphorylation Site Database. Plant Cell 16: 2394-2405. [Free Access]

Rentel MC, Lecourieux D, Ouaked F, Usher SL, Petersen L, Okamoto H, Knight H, Peck SC, Grierson CS, Hirt H, Knight MR (2004) OXI1 kinase is necessary for oxidative burst-mediated signalling in Arabidopsis. Nature 427: 858-861. [MEDLINE]

Nühse TS, Stansballe A, Jensen ON, Peck SC (2003) Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry. Mol Cell Proteomics 2: 1234-1243. [Free Access]

Complete Publication List

Employment Opportunities

Post-Doctoral Opportunities

Electronic submission is encouraged, e-mail to biochemsearch@missouri.edu

Applicants should send CV and names of two references to:
Dr. Scott Peck
Postdoctoral Application
Biochemistry
271H Bond Life Sciences Center
University of Missouri-Columbia
Columbia, MO 65211

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