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

Handle URI:
http://hdl.handle.net/10754/561497
Title:
myo-Inositol-1-phosphate synthase is required for polar auxin transport and organ development
Authors:
Chen, Hao; Xiong, Liming ( 0000-0001-8099-0806 )
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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Center for Desert Agriculture; Bioscience Program; Plant Stress Genomics Research Lab
Publisher:
American Society for Biochemistry & Molecular Biology (ASBMB)
Journal:
Journal of Biological Chemistry
Issue Date:
1-Jun-2010
DOI:
10.1074/jbc.M110.123661
PubMed ID:
20516080
PubMed Central ID:
PMC2911297
Type:
Article
ISSN:
00219258
Sponsors:
This work was supported by National Science Foundation Grant 0446359 (to L. X.).
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2911297
Appears in Collections:
Articles; Bioscience Program; Center for Desert Agriculture; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorChen, Haoen
dc.contributor.authorXiong, Limingen
dc.date.accessioned2015-08-02T09:12:49Zen
dc.date.available2015-08-02T09:12:49Zen
dc.date.issued2010-06-01en
dc.identifier.issn00219258en
dc.identifier.pmid20516080en
dc.identifier.doi10.1074/jbc.M110.123661en
dc.identifier.urihttp://hdl.handle.net/10754/561497en
dc.description.abstractmyo-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.en
dc.description.sponsorshipThis work was supported by National Science Foundation Grant 0446359 (to L. X.).en
dc.publisherAmerican Society for Biochemistry & Molecular Biology (ASBMB)en
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2911297en
dc.titlemyo-Inositol-1-phosphate synthase is required for polar auxin transport and organ developmenten
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentCenter for Desert Agricultureen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentPlant Stress Genomics Research Laben
dc.identifier.journalJournal of Biological Chemistryen
dc.identifier.pmcidPMC2911297en
dc.contributor.institutionDonald Danforth Plant Science Center, St. Louis, MO 63132, United Statesen
kaust.authorXiong, Limingen
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