期刊
DEVELOPMENT
卷 139, 期 12, 页码 2170-2176出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/dev.073817
关键词
BMP; Dpp; Gbb; Lipoprotein; Vitellogenin; Wing venation
资金
- National Science Foundation [IBN-0416586, IOS-0818539]
- National Institutes of Health (NIH) [R01-NS028202]
- University of Wisconsin's Department of Genetics through an NIH
- Department of Zoology
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [0818539] Funding Source: National Science Foundation
The sensitivity of the posterior crossvein in the pupal wing of Drosophila to reductions in the levels and range of BMP signaling has been used to isolate and characterize novel regulators of this pathway. We show here that crossveinless d (cv-d) mutations, which disrupt BMP signaling during the development of the posterior crossvein, mutate a lipoprotein that is similar to the vitellogenins that comprise the major constituents of yolk in animal embryos. Cv-d is made in the liver-like fat body and other tissues, and can diffuse into the pupal wing via the hemolymph. Cv-d binds to the BMPs Dpp and Gbb through its Vg domain, and to heparan sulfate proteoglycans, which are well-known for their role in BMP movement and accumulation in the wing. Cv-d acts over a long range in vivo, and does not have BMP co-receptor-like activity in vitro. We suggest that, instead, it affects the range of BMP movement in the pupal wing, probably as part of a lipid-BMP-lipoprotein complex, similar to the role proposed for the apolipophorin lipid transport proteins in Hedgehog and Wnt movement.
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