Document Detail

Identification of novel candidate phosphatidic acid-binding proteins involved in the salt-stress response of Arabidopsis thaliana roots.
MedLine Citation:
PMID:  23323832     Owner:  NLM     Status:  MEDLINE    
PA (phosphatidic acid) is a lipid second messenger involved in an array of processes occurring during a plant's life cycle. These include development, metabolism, and both biotic and abiotic stress responses. PA levels increase in response to salt, but little is known about its function in the earliest responses to salt stress. In the present study we have combined an approach to isolate peripheral membrane proteins of Arabidopsis thaliana roots with lipid-affinity purification, to identify putative proteins that interact with PA and are recruited to the membrane in response to salt stress. Of the 42 putative PA-binding proteins identified by MS, a set of eight new candidate PA-binding proteins accumulated at the membrane fraction after 7 min of salt stress. Among these were CHC (clathrin heavy chain) isoforms, ANTH (AP180 N-terminal homology) domain clathrin-assembly proteins, a putative regulator of potassium transport, two ribosomal proteins, GAPDH (glyceraldehyde 3-phosphate dehydrogenase) and a PI (phosphatidylinositol) 4-kinase. PA binding and salt-induced membrane recruitment of GAPDH and CHC were confirmed by Western blot analysis of the cellular fractions. In conclusion, the approach of the present study is an effective way to isolate biologically relevant lipid-binding proteins and provides new leads in the study of PA-mediated salt-stress responses in roots.
Fionn McLoughlin; Steven A Arisz; Henk L Dekker; Gertjan Kramer; Chris G de Koster; Michel A Haring; Teun Munnik; Christa Testerink
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  450     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-02-28     Completed Date:  2013-04-17     Revised Date:  2013-05-06    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  573-81     Citation Subset:  IM    
University of Amsterdam, Swammerdam Institute for Life Sciences, Section Plant Physiology, Postbus 94215, 1090 GE Amsterdam, The Netherlands.
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MeSH Terms
Arabidopsis / chemistry*,  metabolism
Arabidopsis Proteins / isolation & purification*,  metabolism*,  physiology
Carrier Proteins / isolation & purification,  metabolism,  physiology
Membrane Proteins / isolation & purification,  metabolism
Models, Biological
Phosphatidic Acids / metabolism*
Plant Roots / chemistry*,  drug effects,  metabolism
Protein Binding / drug effects
Proteome / analysis,  drug effects,  isolation & purification
Salt-Tolerance* / genetics
Sodium Chloride / pharmacology
Stress, Physiological / drug effects,  physiology
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Carrier Proteins; 0/Membrane Proteins; 0/Phosphatidic Acids; 0/Proteome; 7647-14-5/Sodium Chloride
Erratum In:
Biochem J. 2013 Apr 15;451(2):343

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