期刊
DEVELOPMENT
卷 146, 期 1, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/dev.169219
关键词
Drosophila oogenesis; Ring canal; Cullin 3; Kelch; Ubiquitin-proteasome system; Actin cytoskeleton
资金
- National Institutes of Health [R01 GM043301, RC1 GM091791, T32 GM007223, T32 GM007499]
During Drosophila oogenesis, specialized actin-based structures called ring canals form and expand to accommodate growth of the oocyte. Previous work demonstrated that Kelch and Cullin 3 function together in a Cullin 3-RING ubiquitin ligase complex (CRL3(Kelch)) to organize the ring canal cytoskeleton, presumably by targeting a substrate for proteolysis. Here, we use tandem affinity purification followed by mass spectrometry to identify HtsRC as the CRL3(Kelch) ring canal substrate. CRISPR-mediated mutagenesis of HtsRC revealed its requirement in the recruitment of the ring canal F-actin cytoskeleton. We present genetic evidence consistent with HtsRC being the CRL3(Kelch) substrate, as well as biochemical evidence indicating that HtsRC is ubiquitylated and degraded by the proteasome. Finally, we identify a short sequence motif in HtsRC that is necessary for Kelch binding. These findings uncover an unusual mechanism during development wherein a specialized cytoskeletal structure is regulated and remodeled by the ubiquitinproteasome system.
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