Man-Ho Oh
  • Ph. D.
  • Man-Ho Oh
  • Plant Development Genetics
  • N11-307
  • Laboratory of Plant Developmental Genetics & Functional Proteomics (N11-308)
  • +82-42-821-5497

Academic Career

  • Ph.D., 1993, Seoul National University Seoul, Korea


  • Post-Doc., 1995-1999, North Carolina State University (Raleigh) NC, USA
  • Principal Investigator., 2001- 2004, TS Corporation R & D Center (Incheon), Korea
  • Senior Research Scientist., 2004-2013 USDA-ARS, University of Illinois (Urbana-Champaign) IL, USA
  • Professor, 2013- Current, Chungnam National University

Research Interests

  • Receptor kinases signaling in plants

    Plants respond to developmental and environmental signals in part through membrane-localized receptor kinases that interact with other proteins to initiate a cascade of biochemical events resulting in altered cellular function. The genome of the model plant Arabidopsis thaliana encodes 223 Leucine-Rich Repeat Receptor-Like Kinases (LRR RLKs) with a structural organization similar to that of animal receptor kinases. Several of these plant LRR RLKs have been characterized in some detail and are known to play critical roles in regulating growth, morphogenesis, disease resistance, and responses to stress signals. Key to understanding LRR RLK action in specific signaling pathways is the identification of both membrane-bound and soluble protein partners.
    However, the functions and interacting protein networks of the vast majority of this large family of signal transduction molecules remain unknown. Besides a broad study of protein interactions, a selected group of LRR RLKs will be functionally characterized at a detailed biochemical level, including those LRR RLKs interacting with other proteins. The large number of Arabidopsis LRR RLKs suggests extensive possibilities for protein-protein interaction and thus, the diversification and amplification of signaling pathways. Using interdisciplinary approaches from plant genetics, biochemistry, mass spectrometry and proteomics, an extensive network of LRR RLK interacting proteins and signal transduction including brassinosteroid hormone and small peptides will be generated.

Selected Publication

  • Lee JH, Kim H, Chae WB, Oh MH. (2019). Pattern recognition receptors and their interactions with bacterial type III effectors in plants. Genes Genomics doi: 10.1007/s13258-019-00801-1
  • Ji Hyea Lee, Jeongyeo Lee, HyeRan Kim, Won Byoung Chae, Yong Pyo Lim, and Man-Ho Oh* (2018). Brassinosteroids regulate glucosinolate biosynthesis in Arabidopsis thaliana. Physiol. Plant. doi: 10.1111/ppl.12691
  • Oh ES, Lee Y, Chae WB, Rameneni JJ, Park YS, Lim YP, Oh MH* (2018). Biochemical Analysis of the Role of Leucine-Rich Repeat Receptor-Like Kinases and the Carboxy-Terminus of Receptor Kinases in Regulating Kinase Activity in Arabidopsis thaliana and Brassica oleracea. Molecules doi: 10.3390/molecules23010236.
  • Daniel F. Caddell, Sweta Sharma, Man-Ho Oh, Tong Wei, Chang-Jin Park, Patrick Canlas, Steven C. Huber and Pamela C. Ronald (2018). Four tyrosine residues on the rice immune receptor XA21 are required for interaction with the co-receptor OsSERK2 and resistance to Xoo. Peer J. doi: 10.7717/peerj.6074.
  • Vijayata Singh, Artemis Perraki, Sang Yeol Kim, Stuti Shrivastava, Jae Hoon Lee, Youfu Zhao, Benjamin Schwessinger, Man-Ho Oh, Amy Marshall-Colon1, Cyril Zipfel, and Steven C. Huber (2017). Tyrosine 610 in the receptor kinase BAK1 does not play a major role in brassinosteroid signaling or innate immunity. Frontiers Plant Science doi: 10.3389/fpls.2017.01273.
  • Won Byoung Chae, Youn-Je Park, Kyung Sun Lee, Ill-Sup Nou and Man-Ho Oh* (2016). Plant receptor kinases bind and phosphorylate 14-3-3 proteins. Genes & Genomics 11: 1111-1119
  • Rameneni JJ, Lee Y, Dhandapani V, Yu X, Choi SR, Oh MH*, Lim YP*. 2015. Genomic and Post-Translational Modification Analysis of Leucine-Rich-Repeat Receptor-Like Kinases in Brassica rapa. PLoS One 2015 No20;10(11):e0142255. doi: 10.1371/journal.pone.0142255. eCollection 2015.
  • Oh MH*, Bender KW, Kim SY, Wu X, Lee S, Nou IS, Zielinski RE, Clouse SD, Huber SC. 2015. Functional analysis of the BRI1 receptor kinase by Thr-for-Ser substitution in a regulatory autophosphorylation site. Frontiers in Plant Science 10.3389/fpls.2015.00562.