The multi-site docking protein Gab1 is constitutively phosphorylated independent from its recruitment to the plasma membrane in Jak2-V617F-positive cells and mediates proliferation of human erythroleukaemia cells

Article ID	Journal	Published Year	Pages	File Type
5509283	Cellular Signalling	2017	31 Pages	PDF

Keywords

KLH MBD EGFR polyvinylidene-difluoride AEBSF SHP2 SH2 PLC FCS ERK PIP3 EPO EpoR Ras-GTPase activating protein HEK HDR PVDF DMEM PI3K RasGAP GRB2 Janus kinase MAPK Dulbecco's modified Eagle's medium PKB/AKT Src-homology 2 STAT erythropoietin essential thrombocythaemia fetal calf serum extracellular signal regulated kinase phosphatidyl-inositol-3-kinase phosphatidylinositol (3,4,5)-trisphosphate phospholipase C Signal transducer and activator of transcription Myeloproliferative neoplasm homology directed repair Pleckstrin Homology Growth factor receptor bound protein 2 protein kinase B mitogen activated protein kinase polycythaemia vera JAK HEL human embryonic kidney Gab1 Erythropoietin Receptor Epidermal growth factor receptor

Related Topics

Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry

Preview

The multi-site docking protein Gab1 is constitutively phosphorylated independent from its recruitment to the plasma membrane in Jak2-V617F-positive cells and mediates proliferation of human erythroleukaemia cells

Authors

Hannes Bongartz, Wiebke Hessenkemper, Christian Müller, Melissa Fensky, Johannes Fritsch, Katharina Mandel, Iris Behrmann, Claude Haan, Thomas Fischer, Stephan M. Feller, Fred Schaper,