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    myo-Inositol-1-phosphate synthase is required for polar auxin transport and organ development

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    Type
    Article
    Authors
    Chen, Hao
    Xiong, Liming cc
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Desert Agriculture Initiative
    Plant Science
    Plant Stress Genomics Research Lab
    Date
    2010-06-01
    Online Publication Date
    2010-06-01
    Print Publication Date
    2010-07-30
    Permanent link to this record
    http://hdl.handle.net/10754/561497
    
    Metadata
    Show full item record
    Abstract
    myo-Inositol-1-phosphate synthase is a conserved enzyme that catalyzes the first committed and rate-limiting step in inositol biosynthesis. Despite its wide occurrence in all eukaryotes, the role of myo-inositol-1-phosphate synthase and de novo inositol biosynthesis in cell signaling and organism development has been unclear. In this study, we isolated loss-of-function mutants in the Arabidopsis MIPS1 gene from different ecotypes. It was found that all mips1 mutants are defective in embryogenesis, cotyledon venation patterning, root growth, and root cap development. The mutant roots are also agravitropic and have reduced basipetal auxin transport. mips1 mutants have significantly reduced levels of major phosphatidylinositols and exhibit much slower rates of endocytosis. Treatment with brefeldin A induces slower PIN2 protein aggregation in mips1, indicating altered PIN2 trafficking. Our results demonstrate that MIPS1 is critical for maintaining phosphatidylinositol levels and affects pattern formation in plants likely through regulation of auxin distribution. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
    Citation
    Chen, H., & Xiong, L. (2010). myo-Inositol-1-phosphate Synthase Is Required for Polar Auxin Transport and Organ Development. Journal of Biological Chemistry, 285(31), 24238–24247. doi:10.1074/jbc.m110.123661
    Sponsors
    This work was supported by National Science Foundation Grant 0446359 (to L. X.).
    Publisher
    American Society for Biochemistry & Molecular Biology (ASBMB)
    Journal
    Journal of Biological Chemistry
    DOI
    10.1074/jbc.M110.123661
    PubMed ID
    20516080
    PubMed Central ID
    PMC2911297
    Additional Links
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2911297
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.M110.123661
    Scopus Count
    Collections
    Articles; Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Desert Agriculture Initiative

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