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• W87419773 abstract "The completion of the human genome project has marked a new beginning in biomedicalsciences. As human cancer is a genetic disease, the field of oncology has been one of the first to beimpacted by this historic revolution. High-throughput mutational profiling of tumors has providedan unprecedented amount of information on genetic changes leading to cancer and has alreadyrevolutionized the way lung cancers are classified and treated. Fundamental for successfullytranslating the information uncovered by these genetic studies into the clinic is the molecular andfunctional characterization of the identified genetic lesions. As part of these efforts, the goal of mythesis studies was to gain an understanding of how genetic lesions affecting receptor tyrosinekinases (RTKs) contribute to treatment response and survival differences observed in lung tumors.Phosphorylation of tyrosine residues in proteins was first described in 1979 as an activity ofa viral transforming gene product. Soon afterwards RTKs were recognized to play a role intransducing growth factor signals across the plasma membrane. Over the past 50 years, theimportance of RTKs has been demonstrated in multiple studies, and increasing amounts of datahave implicated the deregulation and malfunction of these signaling proteins in a variety ofdiseases including lung cancer. Although highly similar in structure and regulation, different RTKsexert distinct biological functions. The ability of RTKs to function within common pathways, yetinduce diverse phenotypic responses, has largely been attributed to: 1) differences in cellularcontext, as signaling proteins are differentially expressed in distinct cell types; 2) the strength andtemporal properties of signaling; and 3) differences in binding sites for effector molecules.In addition to these mechanisms, we discovered that intrinsic differences in RTK substratespecificity could also play a role in modulating functional differences among RTKs. In particular,we found the SOCS3 residue Y165 to be differentially phosphorylated by certain RTKs such as theplatelet derived growth factor receptor (PDGFR) and the epidermal growth factor receptor (EGFR).The increased phosphorylation leads to ubiquitination and proteasome-dependent degradation ofSOCS3. As SOCS3 is one of the major negative regulators of IL-6 mediated signaling, degradation ofSOCS3 by PDGFR-mediated phosphorylation results in potentiation of IL-6 signaling, andphenotypically in the acquisition of mesenchymal-like features and increased metastatic potentialas well as erlotinib resistance." @default.
• W87419773 created "2016-06-24" @default.
• W87419773 creator A5076045931 @default.
• W87419773 date "2012-09-18" @default.
• W87419773 modified "2023-09-27" @default.
• W87419773 title "Substrate specificity of receptor tyrosine kinases is critical for selective signaling" @default.
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