Ephrin-B Reverse Signaling Is Mediated by a Novel PDZ-RGS Protein and Selectively Inhibits G Protein–Coupled Chemoattraction
2001; Cell Press; Volume: 105; Issue: 1 Linguagem: Inglês
10.1016/s0092-8674(01)00297-5
ISSN1097-4172
AutoresQiang Lü, Edna E. Sun, Robyn S. Klein, John G. Flanagan,
Tópico(s)Zebrafish Biomedical Research Applications
ResumoTransmembrane B ephrins and their Eph receptors signal bidirectionally. However, neither the cell biological effects nor signal transduction mechanisms of the reverse signal are well understood. We describe a cytoplasmic protein, PDZ-RGS3, which binds B ephrins through a PDZ domain, and has a regulator of heterotrimeric G protein signaling (RGS) domain. PDZ-RGS3 can mediate signaling from the ephrin-B cytoplasmic tail. SDF-1, a chemokine with a G protein–coupled receptor, or BDNF, act as chemoattractants for cerebellar granule cells, with SDF-1 action being selectively inhibited by soluble EphB receptor. This study reveals a pathway that links reverse signaling to cellular guidance, uncovers a novel mode of control for G proteins, and demonstrates a mechanism for selective regulation of responsiveness to neuronal guidance cues.
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