| First Author | Zhai J | Year | 2001 |
| Journal | J Biol Chem | Volume | 276 |
| Issue | 44 | Pages | 41318-24 |
| PubMed ID | 11533041 | Mgi Jnum | J:230375 |
| Mgi Id | MGI:5758828 | Doi | 10.1074/jbc.M107709200 |
| Citation | Zhai J, et al. (2001) Identification of a novel interaction of 14-3-3 with p190RhoGEF. J Biol Chem 276(44):41318-24 |
| abstractText | Activation of Rho GTPases by guanine nucleotide exchange factors (GEFs) mediates a broad range of cytoskeletal alterations that determine cell shape. In the nervous system, Rho GTPases are essential for establishing highly asymmetrical neuronal forms and may fine-tune the shape of dendrites in differentiated neurons. p190RhoGEF is a brain-enriched, RhoA-specific GEF whose highly interactive C-terminal domain provides potential linkage to multiple pathways in the cell. In the present study, a yeast two-hybrid screen was used to identify 14-3-3eta and 14-3-3epsilon as additional binding partners of p190RhoGEF. Interactions between p190RhoGEF and 14-3-3eta were confirmed biochemically and by colocalization of the respective proteins when fused to fluorescent markers and transfected in neuronal cells. We also mapped a unique phosphorylation-independent binding site (I(1370)QAIQNL) in p190RhoGEF. Deletion of the binding site abolished interactions in vitro as well as the ability of 14-3-3eta to alter the cytoplasmic aggregation of p190RhoGEF in cotransfected cells. The findings suggest a potential role for 14-3-3 in modulating p190RhoGEF activity or in linking p190RhoGEF to the activities of other pathways in the neuron. |
