Functional proteomics of Arabidopsis thaliana guard cells uncovers new stomatal signaling pathways

Zhixin Zhao, Wei Zhang, Bruce A. Stanley, Sarah M. Assmann

Research output: Contribution to journalArticlepeer-review

216 Scopus citations


We isolated a total of 3 x 108 guard cell protoplasts from 22,000 Arabidopsis thaliana plants and identified 1734 unique proteins using three complementary proteomic methods: protein spot identification from broad and narrow pH range two-dimensional (2D) gels, and 2D liquid chromatography-matrix assisted laser desorption/ionization multidimensional protein identification technology. This extensive single-cell-type proteome includes 336 proteins not previously represented in transcriptome analyses of guard cells and 52 proteins classified as signaling proteins by Gene Ontology analysis, of which only two have been previously assessed in the context of guard cell function. THIOGLUCOSIDE GLUCOHYDROLASE1 (TGG1), a myrosinase that catalyzes the production of toxic isothiocyanates from glucosinolates, showed striking abundance in the guard cell proteome. tgg1 mutants were hyposensitive to abscisic acid (ABA) inhibition of guard cell inward K+ channels and stomatal opening, revealing that the glucosinolate-myrosinase system, previously identified as a defense against biotic invaders, is required for key ABA responses of guard cells. Our results also suggest a mechanism whereby exposure to abiotic stresses may enhance plant defense against subsequent biotic stressors and exemplify how enhanced knowledge of the signaling networks of a specific cell type can be gained by proteomics approaches.

Original languageEnglish (US)
Pages (from-to)3210-3226
Number of pages17
JournalPlant Cell
Issue number12
StatePublished - Dec 2008

All Science Journal Classification (ASJC) codes

  • Plant Science
  • Cell Biology


Dive into the research topics of 'Functional proteomics of Arabidopsis thaliana guard cells uncovers new stomatal signaling pathways'. Together they form a unique fingerprint.

Cite this