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
AuthorBuchert, M; Schneider, S; Meskenaite, V; Adams, MT; Canaani, E; Baechi, T; Moelling, K; Hovens, CM
Source TitleThe Journal of Cell Biology
PublisherROCKEFELLER UNIV PRESS
University of Melbourne Author/sHovens, Christopher
Document TypeJournal Article
CitationsBuchert, M., Schneider, S., Meskenaite, V., Adams, M. T., Canaani, E., Baechi, T., Moelling, K. & Hovens, C. M. (1999). 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. JOURNAL OF CELL BIOLOGY, 144 (2), pp.361-371. https://doi.org/10.1083/jcb.144.2.361.
Access StatusOpen Access
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.
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