Fyn tyrosine kinase increases Apolipoprotein E Receptor 2 levels and phosphorylation

Autor: Shailaja D. Divekar, Teal C. Burrell, Edwin J. Weeber, G. William Rebeck
Jazyk: angličtina
Rok vydání: 2014
Předmět:
Long-Term Potentiation
lcsh:Medicine
Proto-Oncogene Proteins c-fyn
Biochemistry
environment and public health
Rats
Sprague-Dawley
Mice
0302 clinical medicine
Cell Signaling
Molecular Cell Biology
Chlorocebus aethiops
Medicine
Reelin
Tyrosine
Phosphorylation
lcsh:Science
Mice
Knockout
Neurons
0303 health sciences
Multidisciplinary
Neuronal Plasticity
biology
Brain
DAB1
Cell biology
F-Spondin
Cell Motility
COS Cells
Signal transduction
Tyrosine kinase
Research Article
Signal Transduction
Protein Binding
Low-density lipoprotein receptor-related protein 8
Transmembrane Receptors
Cell Migration
03 medical and health sciences
FYN
Developmental Neuroscience
Animals
Biotinylation
Neuron Migration
Protein Interactions
LDL-Receptor Related Proteins
030304 developmental biology
business.industry
lcsh:R
Biology and Life Sciences
Proteins
Cell Biology
Phosphoproteins
Rats
Mice
Inbred C57BL
Reelin Protein
enzymes and coenzymes (carbohydrates)
Gene Expression Regulation
nervous system
Protein-Protein Interactions
Cellular Neuroscience
Immunology
biology.protein
lcsh:Q
Molecular Neuroscience
business
030217 neurology & neurosurgery
Developmental Biology
Neuroscience
Synaptic Plasticity
Zdroj: PLoS ONE, Vol 9, Iss 10, p e110845 (2014)
PLoS ONE
ISSN: 1932-6203
Popis: Apolipoprotein E Receptor 2 (ApoER2) and the tyrosine kinase Fyn are both members of the Reelin pathway, a signaling pathway essential for the laminar formation of the cortex during development and proper dendritic spine density and long-term potential (LTP) in the adult brain. In the presence of extracellular Reelin, ApoER2 binds the intracellular protein Dab1, an adaptor protein that is phosphorylated by Fyn. However, direct interactions between ApoER2 and Fyn are not well defined. Here, we show that total levels of ApoER2 and surface levels of ApoER2 are increased by active Fyn. Via a separate mechanism, ApoER2 is also phosphorylated by Fyn, an event that peaks in the postnatal cortex at day 5 and can occur at multiple ApoER2 tyrosine residues. Dab1 is also involved in this phosphorylation, promoting the phosphorylation of ApoER2 by Fyn when it is itself phosphorylated. These results elucidate some of the intracellular mechanisms that give rise to a functional Reelin pathway.
Databáze: OpenAIRE
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