The Junction-associated Protein AF-6 Interacts and Clusters with Specific Eph Receptor Tyrosine Kinases at Specialized Sites of Cell–Cell Contact in the Brain
| Autor: | Karin Moelling, Christopher M. Hovens, Mark Raymond Adams, Michael Buchert, Thomas Baechi, Eli Canaani, Virginia Meskenaite, Stefan Schneider |
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| Jazyk: | angličtina |
| Rok vydání: | 1999 |
| Předmět: |
Receptor
EphB2 Ras-binding protein Recombinant Fusion Proteins Receptor Protein-Tyrosine Kinases PDZ domain Kinesins Biology Myosins Transfection EPH receptor B2 Hippocampus Cell Line Substrate Specificity 03 medical and health sciences 0302 clinical medicine Dogs EPH receptor A3 neuron physiology Animals Humans Receptor 030304 developmental biology postsynaptic clustering Cell Line Transformed 0303 health sciences Binding Sites receptor tyrosine kinases Cell Membrane Erythropoietin-producing hepatocellular (Eph) receptor PDZ domains Brain Cell Biology Receptor EphA7 EPH receptor A2 Precipitin Tests biological factors Cell biology Rats Intercellular Junctions biological phenomena cell phenomena and immunity Postsynaptic density 030217 neurology & neurosurgery Regular Articles |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | The AF-6/afadin protein, which contains a single PDZ domain, forms a peripheral component of cell membranes at specialized sites of cell–cell junctions. To identify potential receptor-binding targets of AF-6 we screened the PDZ domain of AF-6 against a range of COOH-terminal peptides selected from receptors having potential PDZ domain-binding termini. The PDZ domain of AF-6 interacts with a subset of members of the Eph subfamily of RTKs via its COOH terminus both in vitro and in vivo. Cotransfection of a green fluorescent protein-tagged AF-6 fusion protein with full-length Eph receptors into heterologous cells induces a clustering of the Eph receptors and AF-6 at sites of cell–cell contact. Immunohistochemical analysis in the adult rat brain reveals coclustering of AF-6 with Eph receptors at postsynaptic membrane sites of excitatory synapses in the hippocampus. Furthermore, AF-6 is a substrate for a subgroup of Eph receptors and phosphorylation of AF-6 is dependent on a functional kinase domain of the receptor. The physical interaction of endogenous AF-6 with Eph receptors is demonstrated by coimmunoprecipitation from whole rat brain lysates. AF-6 is a candidate for mediating the clustering of Eph receptors at postsynaptic specializations in the adult rat brain. |
| Databáze: | OpenAIRE |
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