EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane 
microdomains

Brückner, K.; Labrador, J. P.; Scheiffele, P.; Herb, A.; Seeburg, P. H.; Klein, Rüdiger

doi:10.1016/s0896-6273(00)80706-0

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EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains

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Herb, A.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Seeburg, P. H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Brückner, K., Labrador, J. P., Scheiffele, P., Herb, A., Seeburg, P. H., & Klein, R. (1999). EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains. Neuron, 22(3), 511-524. doi:10.1016/s0896-6273(00)80706-0.

Cite as: https://hdl.handle.net/21.11116/0000-0009-BDFD-6

Abstract

Transmembrane ephrinB proteins have important functions during embryonic patterning as ligands for Eph receptor tyrosine kinases and presumably as signal-transducing receptor-like molecules. Consistent with "reverse" signaling, ephrinB1 is localized in sphingo-lipid/cholesterol-enriched raft microdomains, platforms for the localized concentration and activation of signaling molecules. Glutamate receptor-interacting protein (GRIP) and a highly related protein, which we have termed GRIP2, are recruited into these rafts through association with the c-terminal PDZ target site of ephrinB1. Stimulation of ephrinB1 with soluble EphB2 receptor ectodomain causes the formation of large raft patches that also contain GRIP proteins. Moreover, a GRIP-associated serine/threonine kinase activity is recruited into ephrinB1-GRIP complexes. Our findings suggest that GRIP proteins provide a scaffold for the assembly of a multiprotein signaling complex downstream of ephrinB ligands.