scholarly journals Dual action of epidermal growth factor: extracellular signal-stimulated nuclear–cytoplasmic export and coordinated translation of selected messenger RNA

2010 ◽  
Vol 188 (3) ◽  
pp. 325-333 ◽  
Author(s):  
Nien-Pei Tsai ◽  
Ya-Lun Lin ◽  
Yao-Chen Tsui ◽  
Li-Na Wei
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Nuclear Export ◽  
Messenger Rna ◽  
Rna Binding ◽  
Tyrosine Phosphatase ◽  
Growth Factor Receptor ◽  
Dual Action ◽  
Epidermal Growth ◽  
Specific Mrna

We report the first example of a coordinated dual action of epidermal growth factor (EGF) in stimulating the nuclear–cytoplasmic export and translation of a select messenger RNA (mRNA). The effect of EGF is mediated by the RNA-binding protein Grb7 (growth factor receptor–bound protein 7), which serves as an adaptor for a specific mRNA–protein export complex and a translational regulator. Using the κ–opioid receptor (OR [KOR]) as a model, we demonstrate that EGF activates nuclear SHP-2 (Src homology region 2–containing tyrosine phosphatase), which dephosphorylates Grb7 in the nucleus. Hypophosphorylated Grb7 binds to the KOR mRNA and recruits the Hu antigen R–exportin-1 (CRM1) complex to form a nuclear–cytoplasmic export complex that exports KOR mRNA. EGF also activates focal adhesion kinase in the cytoplasm to rephosphorylate Grb7, releasing KOR mRNA for active translation. In summary, this study uncovers a coordinated, dual activity of EGF in facilitating nuclear export of a specific mRNA–protein complex as well as translational activation of the exported mRNA.

Processing Temporal Growth Factor Patterns by an Epidermal Growth Factor Receptor Network Dynamically Established in Space

2020 ◽  
Vol 36 (1) ◽  
pp. 359-383 ◽  
Author(s):  
Aneta Koseska ◽  
Philippe I.H. Bastiaens
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Egf Receptor ◽  
Tyrosine Phosphatase ◽  
Operation Mode ◽  
Growth Factor Receptor ◽  
Couple Growth ◽  
Kinetic Mechanisms ◽  
Cellular Context ◽  
Epidermal Growth

The proto-oncogenic epidermal growth factor (EGF) receptor (EGFR) is a tyrosine kinase whose sensitivity and response to growth factor signals that vary over time and space determine cellular behavior within a developing tissue. The molecular reorganization of the receptors on the plasma membrane and the enzyme-kinetic mechanisms of phosphorylation are key determinants that couple growth factor binding to EGFR signaling. To enable signal initiation and termination while simultaneously accounting for suppression of aberrant signaling, a coordinated coupling of EGFR kinase and protein tyrosine phosphatase activity is established through space by vesicular dynamics. The dynamical operation mode of this network enables not only time-varying growth factor sensing but also adaptation of the response depending on cellular context. By connecting spatially coupled enzymatic kinase/phosphatase processes and the corresponding dynamical systems description of the EGFR network, we elaborate on the general principles necessary for processing complex growth factor signals.

scholarly journals The Protein Tyrosine Phosphatase TCPTP Suppresses the Tumorigenicity of Glioblastoma Cells Expressing a Mutant Epidermal Growth Factor Receptor

2001 ◽  
Vol 276 (49) ◽  
pp. 46313-46318 ◽  
Author(s):  
Manuela Klingler-Hoffmann ◽  
Michelle T. Fodero-Tavoletti ◽  
Kazuhiko Mishima ◽  
Yoshitaka Narita ◽  
Webster K. Cavenee ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Growth Factor Receptor ◽  
Glioblastoma Cells ◽  
Protein Tyrosine ◽  
Epidermal Growth
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