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Submitted on December 7, 2006
Revised on February 7, 2007
Accepted on February 10, 2007

Identification of endosomal EGF-receptor signaling targets by functional organelle proteomics

Taras Stasyk, Natalia Schiefermeier, Sergej Skvortsov, Heinz Zwierzina, Johan Peränen, Guenther K. Bonn, and Lukas A. Huber

Biocenter; Div. Cell Biology, Innsbruck Medical University, Innsbruck A-6020

Corresponding Author: lukas.a.huber{at}i-med.ac.at

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 difference gel electrophoresis (DIGE), fluorescence labelling of phosphoproteins and MALDI-TOF-TOF mass spectrometry was applied. All together 23 EGF-regulated (phospho)proteins have been identified as being differentially associated with endosomal fractions by functional organelle-proteomics, among them proteins known to be involved in endosomal trafficking and cytoskeleton rearrangement (Alix, myosin IX, myosin regulatory light chain, Trap1, moesin, cytokeratin 8, septins 2 and 11, 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 has been 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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