TY  - JOUR
AU  - Buchert, M
AU  - Schneider, S
AU  - Meskenaite, V
AU  - Adams, MT
AU  - Canaani, E
AU  - Baechi, T
AU  - Moelling, K
AU  - Hovens, CM
Y2  - 2020/12/21
Y1  - 1999/01/25
SN  - 0021-9525
UR  - http://hdl.handle.net/11343/257089
AB  - 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.
LA  - English
PB  - ROCKEFELLER UNIV PRESS
T1  - 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
DO  - 10.1083/jcb.144.2.361
IS  - The Journal of Cell Biology
VL  - 144
IS  - 2
SP  - 361-371
L1  - /bitstream/handle/11343/257089/PMC2132901.pdf?sequence=1&isAllowed=y
ER  -