Analysis of PDZ-RGS3 function in ephrin-B reverse signaling.
Transmembrane B ephrins and their Eph receptors signal bidirectionally. However, the molecular and cellular mechanisms of the "reverse signaling" by B ephrins are not fully understood. The identification of several B ephrin cytoplasmic domain-interacting proteins has begun to shed light on the signal transduction mechanisms and the cellular effects of B ephrin reverse signaling. This article describes the use of a Transwell migration assay system to characterize the function of a PDZ domain and a regulator of G-protein signaling (RGS) domain-containing protein, PDZ-RGS3, in mediating B ephrin reverse signaling in cultured neurons. The Transwell system discussed here can provide an effective cell-based assay for elucidating RGS protein-mediated signaling interactions in neurons.
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Qiang
Q
Lu
Edna E
EE
Sun
John G
JG
Flanagan
D000818:Animals; D001681:Biological Assay / Q000379:methods; D002465:Cell Movement / Q000502:physiology; D002478:Cells, Cultured; D002531:Cerebellum / Q000166:cytology; D036342:Ephrins / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D020690:GTPase-Activating Proteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D020710:RGS Proteins; D015398:Signal Transduction / Q000502:physiology*; D020798:Two-Hybrid System Techniques
D036342:Ephrins; D020690:GTPase-Activating Proteins; D020710:RGS Proteins; C415085:Rgs3 protein, mouse; D019204:GTP-Binding Proteins