Source:http://linkedlifedata.com/resource/pubmed/id/17081192
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
2007-1-15
|
pubmed:abstractText |
In plants, perception of pathogen-associated molecular patterns at the surface is the first line of defence in cellular immunity. This review summarizes recent evidence of the involvement of vesicle trafficking in the plant's immune response against pathogens. I first discuss aspects of ligand-stimulated receptor endocytosis. The best-characterized pattern-recognition receptor (PRR), FLS2, is a transmembrane leucine-rich repeat receptor kinase that recognizes bacterial flagellin. FLS2 was recently shown to undergo internalization upon activation with its cognate ligand. An animal PRR, TLR4 that mediates perception of bacterial-derived lipopolysaccharides, similarly exhibits ligand-stimulated endocytosis. The second focus is N-ethylmaleimide-sensitive factor adaptor protein receptor (SNARE)-mediated immunity involving syntaxins and their cognate partners. One of the genes involved in basal immunity in Arabidopsis, PEN1, encodes a syntaxin that focally accumulates at fungal penetration sites, raising the possibility that induced exocytosis is important for active defence. Pathogen-triggered endocytic and exocytic processes have to be balanced to ensure host cell homeostasis. Thus, understanding how phytopathogens have evolved strategies to exploit host cell vesicle trafficking to manipulate immune responses is currently an area of intense study.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FLS2 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/PEN1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Pattern Recognition,
http://linkedlifedata.com/resource/pubmed/chemical/SNARE Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
1462-5814
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
9
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1-8
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:17081192-Arabidopsis,
pubmed-meshheading:17081192-Arabidopsis Proteins,
pubmed-meshheading:17081192-Endocytosis,
pubmed-meshheading:17081192-Exocytosis,
pubmed-meshheading:17081192-Ligands,
pubmed-meshheading:17081192-Protein Kinases,
pubmed-meshheading:17081192-Protein Transport,
pubmed-meshheading:17081192-Qa-SNARE Proteins,
pubmed-meshheading:17081192-Receptors, Pattern Recognition,
pubmed-meshheading:17081192-SNARE Proteins,
pubmed-meshheading:17081192-Signal Transduction,
pubmed-meshheading:17081192-Transport Vesicles
|
pubmed:year |
2007
|
pubmed:articleTitle |
Vesicle trafficking in plant immune responses.
|
pubmed:affiliation |
Max-Planck-Institut für Züchtungsforschung, Carl-von-Linné-Weg 10, 50829 Köln, Germany. robatzek@mpiz-koeln.mpg.de
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|