Document Detail

Phosphatidic acid regulates microtubule organization by interacting with MAP65-1 in response to salt stress in Arabidopsis.
MedLine Citation:
PMID:  23150630     Owner:  NLM     Status:  MEDLINE    
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.
Qun Zhang; Feng Lin; Tonglin Mao; Jianing Nie; Min Yan; Ming Yuan; Wenhua Zhang
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-11-13
Journal Detail:
Title:  The Plant cell     Volume:  24     ISSN:  1532-298X     ISO Abbreviation:  Plant Cell     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2013-01-01     Completed Date:  2013-08-21     Revised Date:  2013-11-05    
Medline Journal Info:
Nlm Unique ID:  9208688     Medline TA:  Plant Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4555-76     Citation Subset:  IM    
College of Life Sciences, State Key Laboratory of Crop Genetics and Germplasm Enhancement, Nanjing Agricultural University, Nanjing 210095, China.
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MeSH Terms
Amino Acid Sequence
Arabidopsis / drug effects,  genetics*,  physiology,  ultrastructure
Arabidopsis Proteins / genetics,  metabolism*
Base Sequence
Cell Membrane / metabolism
Dinitrobenzenes / pharmacology
Gene Expression Regulation, Plant*
Microtubule-Associated Proteins / genetics,  metabolism
Microtubules / metabolism*
Models, Molecular
Molecular Sequence Data
Phosphatidic Acids / metabolism*
Phospholipase D / genetics,  metabolism
Protein Binding
Sequence Alignment
Sequence Analysis, DNA
Signal Transduction
Sodium Chloride / pharmacology*
Stress, Physiological
Sulfanilamides / pharmacology
Tubulin Modulators / pharmacology
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Dinitrobenzenes; 0/MAP65-1 protein, Arabidopsis; 0/Microtubule-Associated Proteins; 0/Phosphatidic Acids; 0/Sulfanilamides; 0/Tubulin Modulators; 19044-88-3/oryzalin; 7647-14-5/Sodium Chloride; EC protein, Arabidopsis; EC D

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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