Quantitative analysis of HGF and EGF-dependent phosphotyrosine signaling networks

Dean E Hammond, Russell Hyde, Irina Kratchmarova, Robert J Beynon, Blagoy Blagoev, Michael J Clague

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Abstrakt

We have used stable isotope labeling by amino acids in cell culture (SILAC), in combination with high-resolution mass spectrometry, to identify common and discrete components of the respective receptor tyrosine kinase-dependent phosphotyrosine-associated networks induced by acute stimulation of A549 lung adenocarcinoma cells with EGF or HGF. In total, we obtained quantitative information for 274 proteins, which respond to either or both stimuli by >1.5 fold changes in enrichment, following immuno-precipitation with antiphosphotyrosine antibodies. The data reveal a high degree of overlap between the respective signaling networks but also clear points of departure. A small number of HGF specific effectors were identified including myosin-X, galectin-1, ELMO2 and EphrinB1, while a larger set of EGF specific effectors (39 proteins) includes both novel (e.g., MAP4K3) and established components of receptor tyrosine kinase receptor signaling pathways. Using available protein-interaction data the identified proteins have been assembled into a highly connected network that can be visualized using the Cytoscape tool.
OriginalsprogEngelsk
TidsskriftJournal of Proteome Research
Vol/bind9
Udgave nummer5
Sider (fra-til)2734-42
Antal sider8
ISSN1535-3893
DOI
StatusUdgivet - 7. maj 2010

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