Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton |
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Authors: | Andrew M Hudson Lynn Cooley |
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Institution: | 1.Department of Genetics, and 2.Department of Cell Biology, School of Medicine, and 3.Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520 |
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Abstract: | 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. |
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