期刊
DEVELOPMENT
卷 143, 期 20, 页码 3806-3816出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/dev.138495
关键词
Actin; Fascin; Singed; IKK epsilon; PKC; Bristle morphogenesis; Drosophila
资金
- MEXT/Japan Society for the Promotion of Science (JSPS) [24770197, 22111007]
- Grants-in-Aid for Scientific Research [24770197, 15KT0086, 16K18544, 16K21629, 15H01501] Funding Source: KAKEN
Signaling molecules have pleiotropic functions and are activated by various extracellular stimuli. Protein kinase C (PKC) is activated by diverse receptors, and its dysregulation is associated with diseases including cancer. However, how the undesired activation of PKC is prevented during development remains poorly understood. We have previously shown that a protein kinase, IKK epsilon, is active at the growing bristle tip and regulates actin bundle organization during Drosophila bristle morphogenesis. Here, we demonstrate that IKK epsilon regulates the actin bundle localization of a dynamic actin cross-linker, Fascin. IKK epsilon inhibits PKC, thereby protecting Fascin from inhibitory phosphorylation. Excess PKC activation is responsible for the actin bundle defects in IKK epsilon-deficient bristles, whereas PKC is dispensable for bristle morphogenesis in wild-type bristles, indicating that PKC is repressed by IKK epsilon in wild-type bristle cells. These results suggest that IKK epsilon prevents excess activation of PKC during bristle morphogenesis.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据