| First Author | Hudson Andrew M | Year | 2010 |
| Journal | J Cell Biol | Volume | 188 |
| Pages | 29-37 | PubMed ID | 20065088 |
| Abstract Text | Drosophila melanogaster Kelch (KEL) is the founding member of a diverse protein family defined by a repeated sequence motif known as the KEL repeat (KREP). Several KREP proteins, including Drosophila KEL, bind filamentous actin (F-actin) and contribute to its organization. Recently, a subset of KREP proteins has been shown to function as substrate adaptor proteins for cullin-RING (really interesting new gene) ubiquitin E3 ligases. In this study, we demonstrate that association of Drosophila KEL with Cullin-3, likely in a cullin-RING ligase, is essential for the growth of Drosophila female germline ring canals. These results suggest a role for protein ubiquitylation in the remodeling of a complex F-actin cytoskeletal structure. | Doi | 10.1083/jcb.200909017 |
| Issue | 1 | Month | Jan |
