Linked Life Data

19245862

Source:http://linkedlifedata.com/resource/pubmed/id/19245862

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-4-6
pubmed:abstractText
Phosphorylation is a ubiquitous regulatory mechanism, that governs the activity, subcellular localisation and molecular interactions of proteins. To identify a broad range of nuclear phosphoproteins from Arabidopsis thaliana, we enriched for nuclei from suspension cell cultures and seedlings before extensive fractionation and identification of phosphopeptides by mass spectrometry. We identified 416 phosphopeptides from 345 proteins with high confidence. Our data show that sub-cellular fractionation is an effective strategy for identifying nuclear phosphoproteins, two thirds of our dataset are known or predicted to be nuclear localised and one half of the nuclear localised proteins have novel phosphorylation sites. We identified novel phosphorylation sites on transcription factors, chromatin remodelling proteins, RNA silencing components and the spliceosome. Intriguingly, we also identified phosphorylation sites on several proteins associated with Golgi vesicle trafficking such as the exocyst complex, and speculate that these may be involved in cell plate formation during cytokinesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1876-7737
pubmed:author
pubmed:issnType
Electronic
pubmed:day
13
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
439-51
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana.
pubmed:affiliation
The Sainsbury Laboratory, Norwich Research Park, Colney Lane, Norwich, United Kingdom. alex.jones@tsl.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't