Product Reference
ALK activation induces Shc and FRS2 recruitment: Signaling and phenotypic outcomes in PC12 cells differentiation.
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| Author |
Joffrey Degoutin,Marc Vigny,Jean Y Gouzi |
| Citation Information |
FEBS letters, 581: (2007) |
| Keywords |
Adaptor Proteins, Signal Transducing,Amino Acid Sequence,Animals,Cell Differentiation,Enzyme Activation,Humans,Membrane Proteins,Mitogen-Activated Protein Kinase 1,Mitogen-Activated Protein Kinase 3,Molecular Sequence Data,Neurons,PC12 Cells,Phenotype,Phosphorylation,Phosphotyrosine,Protein Binding,Protein Structure, Tertiary,Protein Transport,Protein-Tyrosine Kinases,Rats,Receptor Protein-Tyrosine Kinases,Shc Signaling Adaptor Proteins,Signal Transduction |
| Related Products |
AB1599 |
| Pub Med ID |
17274988 |
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Abstract
Activation of the neuronal receptor tyrosine kinase ALK (anaplastic lymphoma kinase) promoted the neuron-like differentiation of PC12 cells through specific activation of the ERK MAP-kinase pathway. However, the nature of primary signaling events initiated is still poorly documented. Here, we established that Shc and FRS2 adaptors were recruited and phosphorylated following antibody-based ALK activation. We further demonstrated that Shc was recruited to the consensus phosphotyrosine site NPTpY(1507) and FRS2 was likely recruited to a novel non-orthodox phosphotyrosine site within ALK. Finally, we characterized a functional role for Shc and likely FRS2 in ALK-dependant MAP-kinase activation and neuronal differentiation of PC12 cells. These findings hence open attractive perspectives concerning specific characteristics of ALK in the control of the mechanisms driving neuronal differentiation.
