Document Detail


Reciprocal phosphorylation and glycosylation recognition motifs control NCAPP1 interaction with pumpkin phloem proteins and their cell-to-cell movement.
MedLine Citation:
PMID:  17601822     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In plants, cell-to-cell trafficking of non-cell-autonomous proteins (NCAPs) involves protein-protein interactions, and a role for posttranslational modification has been implicated. In this study, proteins contained in pumpkin (Cucurbita maxima cv Big Max) phloem sap were used as a source of NCAPs to further explore the molecular basis for selective NCAP trafficking. Protein overlay assays and coimmunoprecipitation experiments established that phosphorylation and glycosylation, on both Nicotiana tabacum NON-CELL-AUTONOMOUS PATHWAY PROTEIN1 (Nt-NCAPP1) and the phloem NCAPs, are essential for their interaction. Detailed molecular analysis of a representative phloem NCAP, Cm-PP16-1, identified the specific residues on which glycosylation and phosphorylation must occur for effective binding to NCAPP1. Microinjection studies confirmed that posttranslational modification on these residues is essential for cell-to-cell movement of Cm-PP16-1. Lastly, a glutathione S-transferase (GST)-Cm-PP16-1 fusion protein system was employed to test whether the peptide region spanning these residues was required for cell-to-cell movement. These studies established that a 36-amino acid peptide was sufficient to impart cell-to-cell movement capacity to GST, a normally cell-autonomous protein. These findings are consistent with the hypothesis that a phosphorylation-glycosylation recognition motif functions to control the binding of a specific subset of phloem NCAPs to NCAPP1 and their subsequent transport through plasmodesmata.
Authors:
Ken-Ichiro Taoka; Byung-Kook Ham; Beatriz Xoconostle-Cázares; Maria R Rojas; William J Lucas
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2007-06-29
Journal Detail:
Title:  The Plant cell     Volume:  19     ISSN:  1040-4651     ISO Abbreviation:  Plant Cell     Publication Date:  2007 Jun 
Date Detail:
Created Date:  2007-08-01     Completed Date:  2007-10-15     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  9208688     Medline TA:  Plant Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1866-84     Citation Subset:  IM    
Affiliation:
Section of Plant Biology, College of Biological Sciences, University of California, Davis, CA 95616, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Motifs
Amino Acid Sequence
Biological Transport
Cucurbita / cytology*,  metabolism*
Glycosylation
Immunoprecipitation
Molecular Sequence Data
Mutation / genetics
Peptides / chemistry
Phloem / cytology*,  metabolism*
Phosphorylation
Plant Proteins / chemistry,  metabolism*
Plasmodesmata / metabolism
Protein Binding
Protein Processing, Post-Translational
Protein Transport
Recombinant Proteins / metabolism
Serine / metabolism
Tobacco / metabolism*
Tyrosine / metabolism
Chemical
Reg. No./Substance:
0/Peptides; 0/Plant Proteins; 0/Recombinant Proteins; 55520-40-6/Tyrosine; 56-45-1/Serine
Comments/Corrections

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