期刊
DEVELOPMENTAL DYNAMICS
卷 232, 期 3, 页码 817-826出版社
WILEY
DOI: 10.1002/dvdy.20346
关键词
GTPase; signaling; Rit; Rin; activation; wing venation; eye development
资金
- NEI NIH HHS [EY08117] Funding Source: Medline
- NINDS NIH HHS [R01 NS045103-02, R01 NS045103, NS-045103] Funding Source: Medline
The mammalian Rit and Rin proteins, along with the Drosophila homologue RIC, comprise a distinct and evolutionarily conserved subfamily of Ras-related small GTP-binding proteins. Unlike other Ras superfamily members, these proteins lack a signal for prenylation, contain a conserved but distinct effector domain, and, in the case of Rin and RIC, contain calmodulin-binding domains. To address the physiological role of this Ras subfamily in vivo, activated forms of the Drosophila Ric gene were introduced into flies. Expression of activated RIC proteins altered the development of well-characterized adult structures, including wing veins and photoreceptors of the compound eye. The effects of activated RIC could be mitigated by a reduction in dosage of several genes in the Drosophila Ras cascade, including Son of sevenless (Sos), Dsor (MEK), rolled (MAPK), and Ras itself. On the other hand, reduction of calmodulin exacerbated the defects caused by activated RIC, thus providing the first functional evidence for interaction of these molecules. We conclude that the activation of the Ras cascade may be an important in vivo requisite to the transduction of signals through RIC and that the binding of calmodulin to RIC may negatively regulate this small GTPase. (C) 2005 Wiley-Liss, Inc.
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