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      Phosphatidic acid regulates microtubule organization by interacting with MAP65-1 in response to salt stress in Arabidopsis.

      The Plant cell

      Amino Acid Sequence, Arabidopsis, drug effects, genetics, physiology, ultrastructure, Arabidopsis Proteins, metabolism, Base Sequence, Cell Membrane, Dinitrobenzenes, pharmacology, Gene Expression Regulation, Plant, Microtubule-Associated Proteins, Microtubules, Models, Molecular, Molecular Sequence Data, Mutation, Phosphatidic Acids, Phospholipase D, Protein Binding, Salt-Tolerance, Seedling, Sequence Alignment, Sequence Analysis, DNA, Signal Transduction, Sodium Chloride, Stress, Physiological, Sulfanilamides, Tubulin Modulators

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          Abstract

          Membrane lipids play fundamental structural and regulatory roles in cell metabolism and signaling. Here, we report that phosphatidic acid (PA), a product of phospholipase D (PLD), regulates MAP65-1, a microtubule-associated protein, in response to salt stress. Knockout of the PLDα1 gene resulted in greater NaCl-induced disorganization of microtubules, which could not be recovered during or after removal of the stress. Salt affected the association of MAP65-1 with microtubules, leading to microtubule disorganization in pldα1cells, which was alleviated by exogenous PA. PA bound to MAP65-1, increasing its activity in enhancing microtubule polymerization and bundling. Overexpression of MAP65-1 improved salt tolerance of Arabidopsis thaliana cells. Mutations of eight amino acids in MAP65-1 led to the loss of its binding to PA, microtubule-bundling activity, and promotion of salt tolerance. The pldα1 map65-1 double mutant showed greater sensitivity to salt stress than did either single mutant. These results suggest that PLDα1-derived PA binds to MAP65-1, thus mediating microtubule stabilization and salt tolerance. The identification of MAP65-1 as a target of PA reveals a functional connection between membrane lipids and the cytoskeleton in environmental stress signaling.

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          Author and article information

          Journal
          23150630
          3531852
          10.1105/tpc.112.104182

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