| First Author | Sandilands E | Year | 2004 |
| Journal | Dev Cell | Volume | 7 |
| Issue | 6 | Pages | 855-69 |
| PubMed ID | 15572128 | Mgi Jnum | J:95028 |
| Mgi Id | MGI:3522533 | Doi | 10.1016/j.devcel.2004.09.019 |
| Citation | Sandilands E, et al. (2004) RhoB and actin polymerization coordinate Src activation with endosome-mediated delivery to the membrane. Dev Cell 7(6):855-69 |
| abstractText | We have used a c-Src-GFP fusion protein to address the spatial control of Src activation and the nature of Src-associated intracellular structures during stimulus-induced transit to the membrane. Src is activated during transit, particularly in RhoB-containing cytoplasmic endosomes associated with the perinuclear recycling compartment. Knocking out RhoB or expressing a dominant-interfering Rab11 mutant suppresses both catalytic activation of Src and translocation of active kinase to peripheral membrane structures. In addition, the Src- and RhoB-containing endosomes harbor proteins involved in actin polymerization and filament assembly, for example Scar1, and newly polymerized actin can associate with these endosomes in a Src-dependent manner. This implies that Src may regulate an endosome-associated actin nucleation activity. In keeping with this, Src controls the actin dependence of RhoB endosome movement toward the plasma membrane. This work identifies RhoB as a component of 'outside-in' signaling pathways that coordinate Src activation with translocation to transmembrane receptors. |
