ArticleOncogene2010
SIRPalpha1 receptors interfere with the EGFRvIII signalosome to inhibit glioblastoma cell transformation and migration.
Article in Oncogene, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It carries an expression of concern. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Probabilistic edge inference of gene networks with markov random field-based bayesian learning.Frontiers in genetics · 2022Article
- Sos1 Modulates Extracellular Matrix Synthesis, Proliferation, and Migration in Fibroblasts.Frontiers in physiology · 2021Article
- Molecular functions of SIRPα and its role in cancer.Biomedical reports · 2018Review
- Signal regulatory protein-α protects against cardiac hypertrophy via the disruption of toll-like receptor 4 signaling.Hypertension (Dallas, Tex. : 1979) · 2014Article
- Bayesian methods for expression-based integration of various types of genomics data.EURASIP journal on bioinformatics & systems biology · 2013Article
- Molecular characterization of EGFR and EGFRvIII signaling networks in human glioblastoma tumor xenografts.Molecular & cellular proteomics : MCP · 2012Article
- Prolactin receptor-integrin cross-talk mediated by SIRPα in breast cancer cells.Molecular cancer research : MCR · 2010Article
Corrections and comments
- Expression of concern
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
EGFRvIII, a frequent genetic alteration of the epidermal growth factor receptor (EGFR), has been shown to increase the migratory potential of tumor cells and normal fibroblasts. Previously, we showed that signal regulatory protein alpha1 (SIRPalpha1) receptors interact with SHP-2 to inhibit wild-type (wt) EGFR-mediated tumor migration, survival and cell transformation. However, the effects of SIRPalpha1 inhibitory receptors on EGFRvIII-mediated phenotypes are unclear. The aim of this study was to investigate the effect of SIRPalpha1 receptor on the EGFRvIII signalosome and phenotypes. Overexpression of SIRPalpha1 in U87MG.EGFRvIII cells inhibited transformation and migration in a MAPK-dependent manner, and is independent of the phosphatidylinositol 3-kinase (PI3-K)/Akt pathway. We observed reduced EGFRvIII/SHP-2/Gab1/Grb2/Sos-1 interaction and enhanced SIRP/SHP-2 association in U87MG.EGFRvIII/SIRPalpha1 cells when compared with empty vector control cells. Interestingly, SIRPalpha1 overexpression differentially modulated SHP-2 phosphorylation at tyrosyl 542 and 580 residues, which may regulate Erk1/2 activity and the EGFRvIII phenotype. In addition, SIRPalpha1-expressing cells exhibited reduced focal adhesion kinase (FAK) phosphorylation and its recruitment to the EGFRvIII/Grb2/Sos-1/Gab1/SHP-2 complex. Collectively, our data indicate that SIRPalpha1 specifically affects the SHP-2/FAK/Grb2/Sos-1/MAPK activation loop to downmodulate EGFRvIII-mediated migration and transformation. Further understanding of the molecular interactions between the SIRPalpha1 inhibitory receptor and the EGFRvIII signalosome may facilitate the identification of novel targets to inhibit the EGFRvIII glioblastoma phenotype.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.