首页    期刊浏览 2024年11月25日 星期一
登录注册

文章基本信息

  • 标题:RGS4 and GAIP are GTPase-activating proteins for Gqα and block activation of phospholipase Cβ by γ-thio-GTP-Gqα
  • 本地全文:下载
  • 作者:John R. Hepler ; David M. Berman ; Alfred G. Gilman
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1997
  • 卷号:94
  • 期号:2
  • 页码:428-432
  • DOI:10.1073/pnas.94.2.428
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:RGS proteins constitute a newly appreciated and large group of negative regulators of G protein signaling. Four members of the RGS family act as GTPase-activating proteins (GAPs) with apparent specificity for members of the Gi subfamily of G protein subunits. We demonstrate here that two RGS proteins, RGS4 and GAIP, also act as GAPs for Gq, the G protein responsible for activation of phospholipase C{beta}. Furthermore, these RGS proteins block activation of phospholipase C{beta} by guanosine 5'-(3-O-thio)triphosphate-Gq. GAP activity does not explain this effect, which apparently results from occlusion of the binding site on G for effector. Inhibitory effects of RGS proteins on G protein-mediated signaling pathways can be demonstrated by simple mixture of RGS4 or GAIP with plasma membranes.
国家哲学社会科学文献中心版权所有