期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 278, 期 12, 页码 10282-10290出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M212145200
关键词
-
Signal transduction. via protein kinase C (PKC) is closely regulated by its subcellular localization. To map the molecular determinants mediating the C2 domain-dependent translocation of PKCalpha to the plasma membrane, full-length native protein and several point mutants in the Ca2+/phosphatidylserine-binding site were tagged with green fluorescent protein and transiently expressed in rat basophilic leukemia cells (RBL-2H3). Substitution of several aspartate residues by asparagine completely abolished Ca2+-dependent membrane targeting of PKCalpha. Strikingly, these mutations enabled the mutant proteins to translocate in a diacylglycerol-dependent manner, suggesting that neutralization of charges in the Ca2+ binding region enables the C1 domain to bind diacylglycerol. In addition, it was demonstrated that the protein residues involved in direct interactions with acidic phospholipids play differential and pivotal roles in the membrane targeting of the enzyme. These findings provide new information on how the C2 domain-dependent membrane targeting of PKCalpha occurs in the presence of physiological stimuli.
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