首页    期刊浏览 2024年11月07日 星期四
登录注册

文章基本信息

  • 标题:D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain
  • 本地全文:下载
  • 作者:Lily Jun-shen Huang ; Kyle Durick ; Joshua A. Weiner
  • 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:21
  • 页码:11184-11189
  • DOI:10.1073/pnas.94.21.11184
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Subcellular localization directed by specific A kinase anchoring proteins (AKAPs) is a mechanism for compartmentalization of cAMP-dependent protein kinase (PKA). Using a two-hybrid screen, a novel AKAP was isolated. Because it interacts with both the type I and type II regulatory subunits, it was defined as a dual specific AKAP or D-AKAP1. Here we report the cloning and characterization of another novel cDNA isolated from that screen. This new member of the D-AKAP family, D-AKAP2, also binds both types of regulatory subunits. A message of 5 kb pairs was detected for D-AKAP2 in all embryonic stages and in all adult tissues tested. In brain, skeletal muscle, kidney, and testis, a 10-kb mRNA was identified. In testis, several small mRNAs were observed. Therefore, D-AKAP2 represents a novel family of proteins. cDNA cloning from a mouse testis library identified the full length D-AKAP2. It is composed of 372 amino acids which includes the R binding fragment, residues 333-372, at its C-terminus. Based on coprecipitation assays, the R binding domain interacts with the N-terminal dimerization domain of RI and RII. A putative RGS domain was identified near the N-terminal region of D-AKAP2. The presence of this domain raises the intriguing possibility that D-AKAP2 may interact with a G protein thus providing a link between the signaling machinery at the plasma membrane and the downstream kinase.
国家哲学社会科学文献中心版权所有