Source:http://linkedlifedata.com/resource/pubmed/id/16930548
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2006-9-11
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pubmed:abstractText |
The low-density lipoprotein receptor-related protein (LRP) is a large, endocytic receptor involved in intracellular signalling. LRP acts as a co-receptor with the PDGF-receptor (PDGF-r) for platelet-derived growth factor (PDGF). PDGF-r and Src-kinases induce tyrosine-phosphorylation of LRP. We used fluorescence lifetime imaging microscopy (FLIM) to specifically detect LRP phosphorylation, measure its extent and localization in intact cells, and assess its effects upon LRP-APP interaction. Robust phosphorylation of LRP throughout the cell was observed after overexpression of Src-kinase. This depended on LRP's distal NPXY domain. By contrast, activation of the PDGF-r resulted in phosphorylation of the subpopulation of LRP at or near the cell surface. PDGF activation triggered phosphorylation of endogenous LRP in primary neurons. LRP is also a trafficking receptor for the Alzheimer-related molecule amyloid-precursor-protein (APP). PDGF stimulation did not affect LRP-APP interactions. This approach allows exquisite subcellular resolution of specific LRP post-translational changes and protein-protein interactions of endogenous proteins in intact cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
349
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
24-30
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:16930548-Amyloid,
pubmed-meshheading:16930548-Animals,
pubmed-meshheading:16930548-Cell Line, Tumor,
pubmed-meshheading:16930548-Cell Membrane,
pubmed-meshheading:16930548-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:16930548-Low Density Lipoprotein Receptor-Related Protein-1,
pubmed-meshheading:16930548-Mice,
pubmed-meshheading:16930548-Microscopy, Fluorescence,
pubmed-meshheading:16930548-Neurons,
pubmed-meshheading:16930548-Phosphorylation,
pubmed-meshheading:16930548-Platelet-Derived Growth Factor,
pubmed-meshheading:16930548-Protein Processing, Post-Translational,
pubmed-meshheading:16930548-Signal Transduction
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pubmed:year |
2006
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pubmed:articleTitle |
Fluorescence lifetime imaging microscopy (FLIM) detects stimulus-dependent phosphorylation of the low density lipoprotein receptor-related protein (LRP) in primary neurons.
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pubmed:affiliation |
Alzheimer's Disease Research Unit, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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