About

Gitta Coaker is a Professor and Fiddyment Endowed Chair in the Department of Plant Pathology at the University of California, Davis. She serves as the Graduate Program Chair within the department. Her research program focuses on the interaction between bacterial pathogens and plants, with particular emphasis on understanding kinase-mediated immune signaling and pathogen effector targets in both model and crop plants. Her recent work investigates vascular pathogens, including vector-borne diseases associated with Liberibacter species in citrus, tomato, and potato, as well as the interaction between the Gram-positive vascular pathogen Clavibacter and its plant hosts. Her expertise encompasses molecular biology, genetics, and proteomics of plant-microbe interactions, specifically in plant bacteriology.

Research topics

• Biology
• Cell biology
• Genetics
• Ecology
• Biochemistry
• Immunology
• Biotechnology
• Computational biology

Selected publications

• Stress-induced reactive oxygen species compartmentalization, perception and signalling

  Nature Plants · 2021 · 434 citations

  Senior authorCorresponding
  • Cell biology
  • Biology
  • Biochemistry
  DOI

• Bacterial Vector-Borne Plant Diseases: Unanswered Questions and Future Directions

  Molecular Plant · 2020 · 110 citations

  Senior authorCorresponding
  • Biology
  • Biotechnology
  • Ecology
  DOI

• Regulation of reactive oxygen species during plant immunity through phosphorylation and ubiquitination of RBOHD

  Nature Communications · 2020 · 307 citations

  Senior authorCorresponding
  • Cell biology
  • Biology
  • Biochemistry

  Production of reactive oxygen species (ROS) is critical for successful activation of immune responses against pathogen infection. The plant NADPH oxidase RBOHD is a primary player in ROS production during innate immunity. However, how RBOHD is negatively regulated remains elusive. Here we show that RBOHD is regulated by C-terminal phosphorylation and ubiquitination. Genetic and biochemical analyses reveal that the PBL13 receptor-like cytoplasmic kinase phosphorylates RBOHD's C-terminus and two phosphorylated residues (S862 and T912) affect RBOHD activity and stability, respectively. Using protein array technology, we identified an E3 ubiquitin ligase PIRE (PBL13 interacting RING domain E3 ligase) that interacts with both PBL13 and RBOHD. Mimicking phosphorylation of RBOHD (T912D) results in enhanced ubiquitination and decreased protein abundance. PIRE and PBL13 mutants display higher RBOHD protein accumulation, increased ROS production, and are more resistant to bacterial infection. Thus, our study reveals an intricate post-translational network that negatively regulates the abundance of a conserved NADPH oxidase.

  DOI

• Plant NLR-triggered immunity: from receptor activation to downstream signaling

  Current Opinion in Immunology · 2020 · 195 citations

  Senior authorCorresponding
  • Biology
  • Cell biology
  • Immunology
  DOI

Recent grants

• CAREER: Investigating Dynamic Changes in the Plasma Membrane Proteome during Plant Immune Signaling.

  NSF · $1.1M · 2011–2017

• Elucidating RIN4_Mediated Immune Signaling Cascades in Arabidopsis

  NIH · $2.8M · 2010–2020

• Immune perception of bacterial pathogens in plants

  NIH · $3.0M · 2020–2030

• NSF-BSF: Investigating the role of a tandem kinase-pseudokinase in plant defense

  NSF · $319k · 2020–2025

Frequent coauthors

• Shree Prasad Thapa

  University of California, Davis

  31 shared

• Danielle M. Stevens

  University of California, Berkeley

  27 shared

• Jun Liu

  China Agricultural University

  24 shared

• James R. Elmore

  22 shared

• Tania Y. Toruño

  University of California, Davis

  17 shared

• Zhiqian Pang

  Florida Department of Citrus

  16 shared

• Nian Wang

  University of Florida

  16 shared

• Clare L. Casteel

  Plant (United States)

  15 shared

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