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Indiana University Bloomington

Department of Biology

Faculty & Research

Faculty Profile

Roger Innes

Photo of Roger Innes
Research Images
Research photo by Roger Innes

Extracellular vesicles located between the plasma membrane and cell wall of an Arabidopsis mesophyll cell.

Professor of Biology

IU Affiliations
IUB Electron Microscopy Center

Contact Information
By telephone: 812-855-2219/5-2852(lab)
MY 316B / MY 302 (lab)

Innes Lab website

Genome, Cell & Developmental Biology
Research Areas
  • Eukaryotic Cell Biology, Cytoskeleton and Signaling
  • Microbial Interactions and Pathogenesis
  • Plant Molecular Biology

Ph.D., University of Colorado, 1988 Postdoctoral Fellow, University of California, Berkeley, 1988-91


American Association for the Advancement of Science Fellow

American Academy of Microbiology Fellow

Research Description

Our primary interest is in understanding the molecular and cellular basis of disease resistance in plants. Plants are able to specifically recognize pathogens and actively respond. We are investigating how this specific recognition is accomplished and how recognition is translated into a resistant response. To address these questions we take a molecular genetic approach. We use the small mustard Arabidopsis thaliana as our standard host plant, and both fungal (powdery mildew) and bacterial pathogens (Pseudomonas syringae) as our standard pathogens. Recognition of specific P. syringae strains by Arabidopsis is mediated by specific disease resistance (R) genes of Arabidopsis. These R genes encode intracellular receptors that detect a signal produced directly or indirectly by bacterial proteins that are injected into the plant cell. Our laboratory has made significant contributions to our understanding of HOW R proteins mediate pathogen recognition. These insights are now leading to new approaches for engineering disease resistance in plants. For example, we have shown that the R protein RPS5 is activated by proteolytic cleavage of a second host protein PBS1 by proteases secreted by P. syringae. Armed with this knowledge, we are now engineering this system to recognize new pathogens by modifying the protease cleavage site within PBS1 so that it becomes cleavable by proteases from other pathogens, such as viruses.  In this manner, we believe we can engineer resistance to a diverse array of pathogens, once we know the proteases employed by these pathogens to cause disease. We are currently applying this discovery to engineer novel disease resistance traits in soybean.

In a second project, we have been examining endomembrane trafficking in plant cells in the context of active defense responses.  When a plant leaf is colonized by a pathogen, it dramatically increases secretion of antimicrobial compounds.  This secretion process is complex and appears to involve non-canonical secretory pathways. Based on electron microscopy analyses, this process includes secretion of vesicles known as exosomes, which are lipid-bilayer spheres ranging in size between 50 and 200 nm.  The contents of these vesicles and their function in immunity has not been reported. We have recently determined that they are enriched in defense proteins and carry microRNAs. This latter finding is quite exciting as it suggests plants may employ exosomes for intercellular signaling, and perhaps interkingdom signaling.  We hypothesize that exosomes may mediate transfer of silencing RNAs between plants and pathogens, and are now actively testing this hypothesis.

Select Publications
Rutter, B.D. and R.W. Innes. 2017. Extracellular vesicles isolated from the leaf apoplast carry stress-response proteins. Plant Physiol. 173: 728-741.  [article]
Kim, S.H., D. Qi, T. Ashfield, M. Helm, and R.W. Innes. 2016. Using decoys to expand the recognition specificity of a plant disease resistance protein. Science, 351:684-687.  [article]

Russell, A., T. Ashfield, and R. W. Innes. 2015. Pseudomonas syringae effector AvrPphB suppresses AvrB-induced activation of RPM1, but not AvrRpm1-induced activation. Mol Plant-Microbe Interact. 28:727-735.  [article]

Serrano, I., Y. Gu, D. Qi, U. Dubiella, and R. W. Innes. 2014. The Arabidopsis EDR1 protein kinase negatively regulates the ATL1 E3 ubiquitin ligase to suppress cell death. Plant Cell. 26:4532-46      [article]
Karasov, T.L., J.M. Kniskern, L. Gao, B.J. DeYoung, J. Ding, U. Dubiella, R. Lastra, S. Nallu, F. Roux, R.W. Innes, L.G. Barrett, R.R. Hudson, J. Bergelson. 2014. The long-term maintenance of a resistance polymorphism through diffuse interactions. Nature 512:436-440.      [article]
Ashfield,T.,  T. Redditt, L. Galloway, Q. Kang, N. Rodibaugh, R. Podicheti, and R. W. Innes. 2014. Evolutionary relationship of disease resistance genes in soybean and Arabidopsis specific for the Pseudomonas syringae effectors AvrB and AvrRpm1. Plant Physiol. 166:235-251  [article]
Qi, D., U. Dubiella, S. H. Kim, D. I. Sloss, R. H. Dowen, J. E. Dixon and R. W. Innes. 2014. Recognition of the protein kinase PBS1 by the disease resistance protein RPS5 is dependent on S-acylation and an exposed loop in PBS1. Plant Physiol. 164: 340-351.  [article]
Gu, Y. and R. W. Innes. 2012.  The KEEP ON GOING (KEG) protein of Arabidopsis regulates intracellular protein trafficking and is degraded during fungal infection. Plant Cell, 24: 4717-4730  [article]

Qi, D., B.J. DeYoung, and R. W. Innes. 2012.  Structure-function analysis of the coiled-coil and leucine-rich repeat domains of the RPS5 disease resistance protein. Plant Physiol. 158: 1819-1832.  [article]

Wawrzynska, A., K. M. Christiansen, Y. Lan, N. L. Rodibaugh and R. W. Innes 2008. Powdery Mildew Resistance Conferred by Loss of the EDR1 Protein Kinase is Suppressed by a Missense Mutation in KEG, a Regulator of ABA Signaling. Plant Phys. 148: 1510-1522  [article]
Innes, R. W., C. Ameline-Torregrosa, T. Ashfield, E. Cannon, S. B. Cannon, B. Chacko, N. W. G. Chen, A. Couloux, A. Dalwani, R. Denny, S. Deshpande, A. Egan, N. Glover, C. S. Hans, S. Howell, D. Ilut, S. Jackson, H. Lai, J. Mammadov, S. M. d. Campo, M. Metcalf, A. Nguyen, M. O’Bleness, B. Pfeil, R. Podicheti, M. B. Ratnaparkhe, S. Samain, I. Sanders, B. Ségurens, M. Sévignac, S. Sherman-Broyles, V. Thareau, D. M. Tucker, J. Walling, A. Wawrzynski, J. Yi, J. J. Doyle, V. Geffroy, B. A. Roe, M. A. S. Maroof and N. D. Young 2008. Differential accumulation of retroelements and diversification of NB-LRR disease resistance genes in duplicated regions following polyploidy in the ancestor of soybean. Plant Phys. 148: 1740-1759.  [article]
Ade, J., B. J. DeYoung, C. Golstein and R. W. Innes. 2007. Indirect activation of a plant NBS-LRR protein by a bacterial protease. Proc. Natl. Acad. Sci. USA. 104: 2531-2536.  [article]
Tang, D., K. Christiansen and R. W. Innes. 2005. Regulation of plant disease resistance, stress responses, cell death and ethylene signaling in Arabidopsis by the EDR1 protein kinase. Plant Phys. 138: 1018-1026.  [article]
Ashfield, T., L. Ong, C. M. Scheider and R. W. Innes. 2004. Convergent evolution of disease resistance gene specificity in two flowering plant families. Plant Cell, 16:309-318.  [article]
Shao, F., C. Golstein, J. Ade, M. Stoutemyer, J. Dixon and R. Innes 2003. Cleavage of Arabidopsis PBS1 by a bacterial type III effector. Science, 301:1230-1233.  [article]
Shao, F., P.M.Merritt, Z. Bao, R.W. Innes and J.E. Dixon. 2002. A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell, 109: 575-588.  [article]

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