Source:http://linkedlifedata.com/resource/pubmed/id/17293594
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2007-5-7
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pubmed:abstractText |
Epidermal growth factor (EGF) receptor (EGFR) signal transduction is organized by scaffold and adaptor proteins, which have specific subcellular distribution. On a way from the plasma membrane to the lysosome EGFRs are still in their active state and can signal from distinct subcellular locations. To identify organelle-specific targets of EGF receptor signaling on endosomes a combination of subcellular fractionation, two-dimensional DIGE, fluorescence labeling of phosphoproteins, and MALDI-TOF/TOF mass spectrometry was applied. All together 23 EGF-regulated (phospho)proteins were identified as being differentially associated with endosomal fractions by functional organelle proteomics; among them were proteins known to be involved in endosomal trafficking and cytoskeleton rearrangement (Alix, myosin-9, myosin regulatory light chain, Trap1, moesin, cytokeratin 8, septins 2 and 11, and CapZbeta). Interestingly R-Ras, a small GTPase of the Ras family that regulates cell survival and integrin activity, was associated with endosomes in a ligand-dependent manner. EGF-dependent association of R-Ras with late endosomes was confirmed by confocal laser scanning immunofluorescence microscopy and Western blotting of endosomal fractions. EGFR tyrosine kinase inhibitor gefitinib was used to confirm EGF-dependent regulation of all identified proteins. EGF-dependent association of signaling molecules, such as R-Ras, with late endosomes suggests signaling specification through intracellular organelles.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Signal-Regulated MAP...,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Quinazolines,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/gefitinib
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1535-9476
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
908-22
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17293594-Cell Culture Techniques,
pubmed-meshheading:17293594-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:17293594-Endosomes,
pubmed-meshheading:17293594-Epidermal Growth Factor,
pubmed-meshheading:17293594-Extracellular Signal-Regulated MAP Kinases,
pubmed-meshheading:17293594-Proteins,
pubmed-meshheading:17293594-Proteomics,
pubmed-meshheading:17293594-Quinazolines,
pubmed-meshheading:17293594-Receptor, Epidermal Growth Factor,
pubmed-meshheading:17293594-Signal Transduction,
pubmed-meshheading:17293594-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2007
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pubmed:articleTitle |
Identification of endosomal epidermal growth factor receptor signaling targets by functional organelle proteomics.
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pubmed:affiliation |
Biocenter, Division of Cell Biology, Innsbruck Medical University, A-6020 Innsbruck, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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