Abstract
Neuregulin-1 (NRG1) plays an important role in neural development, synapse formation, and synaptic plasticity by activating ErbB receptor tyrosine kinases. Although ligand-induced endocytosis has been shown to be important for many receptor tyrosine kinases, whether NRG1 signaling depends on ErbB endocytosis remains controversial. Here, we provide evidence that ErbB4, a prominent ErbB protein in the brain, becomes internalized in NRG1-stimulated neurons. The induced ErbB4 endocytosis requires its kinase activity. Remarkably, inhibition of ErbB endocytosis attenuates NRG1-induced activation of Erk and Akt in neurons. These observations indicate a role of ErbB endocytosis in NRG1 signaling in neurons.
Original language | English (US) |
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Pages (from-to) | 505-510 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 354 |
Issue number | 2 |
DOIs | |
State | Published - Mar 9 2007 |
Keywords
- Biotinylation
- Endocytosis
- ErbB4
- Internalization
- Neuregulin
- Neurons
- Schizophrenia
- Tyrosine kinase
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology