| 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: 2009-11-18 |
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. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| 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 | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Effects of different animal waste treatment technologies on detection and viability of porcine enter...
Next Document: BLADE-ON-PETIOLE 1 and 2 control Arabidopsis lateral organ fate through regulation of LOB domain and...