title: Regulation of plasmodesmatal permeability and stomatal patterning by the glycosyltransferase-like protein KOBITO1.
abstract: The differentiation of stomata provides a convenient model for studying pattern formation in plant tissues. Stomata formation is induced by a set of basic helix-loop-helix transcription factors and inhibited by a signal transduction pathway initiated by TOO MANY MOUTHS (TMM) and ERECTA family (ERf) receptors. The formation of a proper stomata pattern is also dependent upon the restriction of symplastic movement of basic helix-loop-helix transcription factors into neighboring cells, especially in the backgrounds where the function of the TMM/ERf signaling pathway is compromised. Here, we describe a novel mutant of KOBITO1 in Arabidopsis (Arabidopsis thaliana). The kob1-3 mutation leads to the formation of stomata clusters in the erl1 erl2 background but not in the wild type. Cell-to-cell mobility assays demonstrated an increase in intercellular protein trafficking in kob1-3, including increased diffusion of SPEECHLESS, suggesting that the formation of stomata clusters is due to an escape of cell fate-specifying factors from stomatal lineage cells. While plasmodesmatal permeability is increased in kob1-3, we did not detect drastic changes in callose accumulation at the neck regions of the plasmodesmata. Previously, KOBITO1 has been proposed to function in cellulose biosynthesis. Our data demonstrate that disruption of cellulose biosynthesis in the erl1 erl2 background does not lead to the formation of stomata clusters, indicating that cellulose biosynthesis is not a major determining factor for regulating plasmodesmatal permeability. Analysis of KOBITO1 structure suggests that it is a glycosyltransferase-like protein. KOBITO1 might be involved in a carbohydrate metabolic pathway that is essential for both cellulose biosynthesis and the regulation of plasmodesmatal permeability.
authors.affiliation: Department of Biochemistry, Cellular, and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996, USA.
authors.forename: Danyu
authors.initials: D
authors.lastname: Kong
authors.forename: Rucha
authors.initials: R
authors.lastname: Karve
authors.forename: Alaina
authors.initials: A
authors.lastname: Willet
authors.forename: Ming-Kun
authors.initials: MK
authors.lastname: Chen
authors.forename: Jennifer
authors.initials: J
authors.lastname: Oden
authors.forename: Elena D
authors.initials: ED
authors.lastname: Shpak
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000254:growth & development / Q000378:metabolism / Q000502:physiology; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D050260:Carbohydrate Metabolism; D002463:Cell Membrane Permeability; D002482:Cellulose / Q000096:biosynthesis / Q000235:genetics; D002874:Chromosome Mapping; D032461:Chromosomes, Plant / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D003433:Crosses, Genetic; D005936:Glucans / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D054046:Plant Stomata / Q000254:growth & development / Q000502:physiology*; D031425:Plasmodesmata / Q000378:metabolism* / Q000502:physiology; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D002482:Cellulose; D005936:Glucans; D008565:Membrane Proteins; D017346:Protein Serine-Threonine Kinases; C469256:KOB1 protein, Arabidopsis; C048306:callose; C502168:ERL1 protein, Arabidopsis; C502169:ERL2 protein, Arabidopsis