title: Alterations in auxin homeostasis suppress defects in cell wall function.
abstract: The plant cell wall is a highly dynamic structure that changes in response to both environmental and developmental cues. It plays important roles throughout plant growth and development in determining the orientation and extent of cell expansion, providing structural support and acting as a barrier to pathogens. Despite the importance of the cell wall, the signaling pathways regulating its function are not well understood. Two partially redundant leucine-rich-repeat receptor-like kinases (LRR-RLKs), FEI1 and FEI2, regulate cell wall function in Arabidopsis thaliana roots; disruption of the FEIs results in short, swollen roots as a result of decreased cellulose synthesis. We screened for suppressors of this swollen root phenotype and identified two mutations in the putative mitochondrial pyruvate dehydrogenase E1α homolog, IAA-Alanine Resistant 4 (IAR4). Mutations in IAR4 were shown previously to disrupt auxin homeostasis and lead to reduced auxin function. We show that mutations in IAR4 suppress a subset of the fei1 fei2 phenotypes. Consistent with the hypothesis that the suppression of fei1 fei2 by iar4 is the result of reduced auxin function, disruption of the WEI8 and TAR2 genes, which decreases auxin biosynthesis, also suppresses fei1 fei2. In addition, iar4 suppresses the root swelling and accumulation of ectopic lignin phenotypes of other cell wall mutants, including procuste and cobra. Further, iar4 mutants display decreased sensitivity to the cellulose biosynthesis inhibitor isoxaben. These results establish a role for IAR4 in the regulation of cell wall function and provide evidence of crosstalk between the cell wall and auxin during cell expansion in the root.
authors.affiliation: Biology Department, University of North Carolina, Chapel Hill, North Carolina, United States of America.
authors.forename: Blaire J
authors.initials: BJ
authors.lastname: Steinwand
authors.affiliation: Biology Department, University of North Carolina, Chapel Hill, North Carolina, United States of America.
authors.forename: Shouling
authors.initials: S
authors.lastname: Xu
authors.affiliation: Biology Department, University of North Carolina, Chapel Hill, North Carolina, United States of America.
authors.forename: Joanna K
authors.initials: JK
authors.lastname: Polko
authors.affiliation: Biology Department, University of North Carolina, Chapel Hill, North Carolina, United States of America.
authors.forename: Stephanie M
authors.initials: SM
authors.lastname: Doctor
authors.affiliation: Biology Department, University of North Carolina, Chapel Hill, North Carolina, United States of America.
authors.forename: Mike
authors.initials: M
authors.lastname: Westafer
authors.affiliation: Biology Department, University of North Carolina, Chapel Hill, North Carolina, United States of America.
authors.forename: Joseph J
authors.initials: JJ
authors.lastname: Kieber
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D001549:Benzamides / Q000494:pharmacology; D049109:Cell Proliferation / Q000187:drug effects / Q000502:physiology*; D002473:Cell Wall / Q000235:genetics / Q000378:metabolism*; D002482:Cellulose / Q000096:biosynthesis / Q000235:genetics; D006706:Homeostasis / Q000187:drug effects / Q000502:physiology*; D007210:Indoleacetic Acids / Q000378:metabolism*; D008031:Lignin / Q000096:biosynthesis / Q000235:genetics; D009154:Mutation; D018517:Plant Roots / Q000235:genetics / Q000378:metabolism*; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism; D011767:Pyruvate Decarboxylase / Q000235:genetics / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D001549:Benzamides; D007210:Indoleacetic Acids; C057467:isoxaben; D002482:Cellulose; D008031:Lignin; D011494:Protein Kinases; C488784:IAR4 protein, Arabidopsis; D011767:Pyruvate Decarboxylase