Craig A. Schenck, PhD

Assistant Professor


Contact Information

Address 214 Schweitzer Hall
Websites Schenck Lab
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  • BS, Plant Biology, Ohio University, Athens, OH
  • MS, Molecular and Cellular Biology, Ohio University, Athens, OH
  • PhD, Botany, University of Wisconsin, Madison, WI

Research Area

Evolution of plant chemical diversity, plant natural product pathway discovery, connections between core and specialized metabolism

Research Description

To deal with relentless environmental pressures, plants produce an arsenal of structurally diverse defensive chemicals. These sometimes-complex compounds are derived from much simpler building blocks from primary metabolic pathways. Unlike well-documented diversification of plant specialized metabolic enzymes, core metabolic pathways are highly conserved and evolutionarily constrained because they serve essential metabolic functions, which makes manipulation of these pathways difficult.

The expansion and alteration of core metabolism has given rise to the evolution of structurally diverse plant specialized metabolites. However, the underlying mechanisms enabling metabolic diversity and the connections linking core to specialized metabolism are not well known. These knowledge gaps create bottlenecks in synthetic biology platforms for production of high-value plant metabolites and increasing plant resilience.

Our goal is to identify biochemical pathways of novel plant metabolites and core metabolic innovations that have potentiated chemical diversity. Then, harness these innovations for increased crop resilience using gene editing approaches and enhanced production of medicinal plant compounds through synthetic biology platforms.

Notable Honors and Service

  • Eric E. Conn Young Investigator Award, American Society of Plant Biologists, 2019

Selected Publications

CA Schenck, TM Anthony, MK Jacobs, AD Jones, RL Last (2022) Natural Variation Meets Synthetic Biology: Promiscuous Trichome-Expressed Acyltransferases from Nicotiana. Plant Physiol., DOI:10.1093/plphys/kiac192

CA Schenck, L Busta (2021) Using interdisciplinary, phylogeny-guided approaches to understand the evolution of plant metabolism. Plant Mol. Bio., 1-13 DOI:10.1007/s11103-021-01220-1

Fan P, Wang P, Lou Y-R, Leong BJ, Moore BM, Schenck CA, Combs R, Cao P, Brandizzi F, Shiu S-H, Last RL. (2020) Evolution of a plant gene cluster in Solanaceae and emergence of metabolic diversity. eLife, DOI:10.7554/eLIFE.56717

Schenck CA, Last RL. (2020) Location, location! Cellular relocalization primes specialized metabolic diversification. FEBS J., DOI:10.1111/febs.15097

Schenck CA, Westphal J, Jayaraman D, Garcia K, Wen J, Mysore KS, Ané J-M, Sumner LW, Maeda HA. (2020) Role of cytosolic, tyrosine-insensitive prephenate dehydrogenase in Medicago truncatula. Plant Direct, DOI:10.1002/pld3.218

Cao P, Kim S-J, Schenck CA, Xing A, Liu L, Jiang N, Wang J, Last RL, Brandizzi F. (2019) Homeostasis of branched-chain amino acids is critical for the activity of TOR signaling in Arabidopsis. eLife, DOI: 10.7554/eLife.50747

Moore BM, Wang P, Fan P, Leong B, Schenck CA, Lloyd JP, Lehti-Shiu MD, Last RL, Pichersky E, Shiu S-H, (2019) Robust predictions of specialized metabolism genes through machine learning. Proc. Natl. Acad. Sci. USA, 116 (6) 2344-2353. DOI:10.1073/pnas.1817074116

Schenck CA, Maeda HA. (2018) Tyrosine biosynthesis, metabolism, and catabolism in plants. Phytochemistry, 149, 82-102. DOI:10.1016/j.phytochem.2018.02.003

Schenck CA, Men Y, Maeda HA. (2017) Conserved molecular mechanism of TyrA dehydrogenase substrate specificity underlying alternative tyrosine biosynthetic pathways in plants and microbes. Front. Mol. Biosci., 4, 73. DOI:10.3389/fmolb.2017.00073

Schenck CA, Holland CK, Schneider M, Men Y, Lee SG, Jez JM, Maeda HA. (2017) Molecular basis of the evolution of alternative tyrosine biosynthetic pathways in plants. Nat. Chem. Biol., 13, 1029-1035. DOI:10.1038/nchembio.2414

Schenck CA, Chen S, Siehl DL, Maeda HA. (2015) Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes. Nat. Chem. Biol., 11, 52-57. DOI:10.1038/nchembio.1693