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Queen's University


      Wayne Snedden - Associate Professor

      Snedden.gif Research: My laboratory investigates the cellular mechanisms that plants use to cope with abiotic (cold, drought, etc.) and biotic (pathogen attack) stress. We are particularly interested in understanding the role of calcium ions as second messengers in stress-induced signal transduction pathways. Our research focuses on how calcium-binding proteins (often termed 'calcium sensors'), such as calmodulin and calmodulin-related proteins (CMLs), participate in the complex responses of plant cells to environmental stress. This work helps provide a base of knowledge in stress physiology and informs the technology for engineering improved stress-tolerance in important crop species.

      »» Lab Website »« email: »« telephone: 613-533-6154 ««

      Some Recent Publications:

      • Bender K, Dobney S, Ogunrinde A, Chiasson D, Mullen RT, Teresinsi HJ, Singh P, Munro K, Smith SP, Snedden WA (2013) The calmodulin--‐like protein, CML43, functions as a salicylic acid--‐inducible, root--‐specific Ca2+ sensor in Arabidopsis, Biochemical J, in press
      • Bender K, Rosenbaum D, Vanderbeld B, Ubaid M, Snedden WA (2013) The Arabidopsis calmodulin--‐like protein, CML39, functions during early seedling establishment.  Plant J, 76: 634--‐47
      • Bender K and Snedden WA (2013) Calmodulin--‐related proteins step out from the shadow of their namesake.  Plant Physiology 163:  486--‐95
      • Allan WL, Breitkreuz KE, Waller J, Simpson JP, Hoover GJ, Rochon A, Wolyn DJ, Rentsch D, Snedden WA, Shelp BJ (2012) Detoxification of succinate semialdehyde in Arabidopsis Glyoxylate reductase and NAD kinase mutants subjected to submergence stress, Botany, 90:51--‐61
      • DeFalco T, Chiasson D, Kaiser B, Snedden WA (2010) Characterization of GmCaMK1, a novel calmodulin--‐binding receptor--‐like kinase from soybean (Glycine max), FEBS Letters 584:4717--‐24
      • Waller J, Dhanoa P, Schumann U, Mullen R and Snedden WA (2010) Subcellular and Tissue Localization of NAD Kinases from Arabidopsis:  Compartmentalization of de novo NADP Biosynthesis, Planta, 231:305--‐17
      • DeFalco T*, Bender K*, Snedden WA (2009) Breaking the code:  Calcium sensors in plant signalling.  Biochemical Journal, 425:27--‐40 (*co--‐1st authors)
      • Dobney S, Chiasson D, Lam P, Smith SP, Snedden WA (2009).  The calmodulin--‐related Calcium sensor CML42 plays a role in trichome branching.  J Biol Chem, 284:31647--‐57  (features cover photo of cml42 knockout trichome phenotype)
      • Vanderbeld B and Snedden WA.  (2007) Developmental and stimulus--‐induced expression patterns of Arabidopsis calmodulin--‐like genes CML37, CML38 and CML39. Plant Mol Biol. 64:683--‐697
      • Veljanovski V, Vanderbeld B, Knowles VL, Snedden WA, Plaxton WC.  (2006) Biochemical and molecular characterization of AtPAP26, a vacuolar purple acid phosphatase up--‐regulated in phosphate--‐deprived Arabidopsis suspension cells and seedlings. Plant Physiol.  142:1282--‐93
      • Chiasson D, Ekengren SK, Martin GB, Dobney SL, Snedden WA (2005) Calmodulin--‐ like Proteins from Arabidopsis and tomato are involved in host defense against Pseudomonas Syringae pv. tomato.  Plant Mol. Biol. 58:887--‐97.
      • Nicolas Bouche, Ayelet Yellin, Wayne A. Snedden, Hillel Fromm (2005)  Plant--‐Specific Calmodulin--‐Binding Proteins.  Annual Review of Plant Biology 56: 435--‐66
      • Turner WL, Waller JC, and Snedden WA (2005) Identification, molecular cloning and functional characterization of a novel NADH kinase from Arabidopsis thaliana.  Biochemical  J 385:  217--‐223
      • Turner WL, Waller JC, Vanderbeld B, and Snedden WA (2004)  Cloning and Characterization of Two NAD Kinases from Arabidopsis.  Identification of a Calmodulin Binding Isoform.  Plant Physiology 135:  1243--‐1255
      • Bouché N, Scharlat A, Snedden WA, Bouchez D, and Fromm H (2002)  A novel family of calmodulin--‐binding transcription activators in multicellular organisms.  J. Biol. Chem. 277:  21851--‐21861

      Kingston, Ontario, Canada. K7L 3N6. 613.533.2000