Allen Patrick B, Greenfield Audrey T, Svenningsson Per, Haspeslagh Derek C, Greengard Paul
Department of Psychiatry, Yale University School of Medicine, New Haven, CT 06508, USA.
Proc Natl Acad Sci U S A. 2004 May 4;101(18):7187-92. doi: 10.1073/pnas.0401673101. Epub 2004 Apr 23.
Protein phosphatase 1 (PP1) is a multifunctional enzyme with diverse roles in the nervous system, including regulation of synaptic activity and dendritic morphology. PP1 activity is controlled via association with a family of regulatory subunits that govern subcellular localization and substrate specificity. A previously undescribed class of PP1-binding proteins was detected by interaction cloning. Family members were also found to bind to cytoplasmic actin via Arg, Pro, Glu, and Leu repeat-containing sequences. The prototypical member of this family, phosphatase and actin regulator (phactr) 1 was a potent modulator of PP1 activity in vitro. Phactr-1 protein is selectively expressed in brain, where high levels were found in cortex, hippocampus, and striatum, with enrichment of the protein at synapses. Additional family members displayed highly distinct mRNA transcript expression patterns within rat brain. The current findings present a mechanism by which PP1 may be directed toward neuronal substrates associated with the actin cytoskeleton.
蛋白磷酸酶1(PP1)是一种多功能酶,在神经系统中具有多种作用,包括调节突触活性和树突形态。PP1的活性通过与一类调节亚基结合来控制,这些调节亚基决定亚细胞定位和底物特异性。通过相互作用克隆检测到一类以前未描述的PP1结合蛋白。还发现该家族成员通过含精氨酸、脯氨酸、谷氨酸和亮氨酸重复序列与细胞质肌动蛋白结合。该家族的典型成员,磷酸酶和肌动蛋白调节剂(phactr)1在体外是PP1活性的有效调节剂。Phactr-1蛋白在大脑中选择性表达,在皮质、海马体和纹状体中含量较高,且在突触处该蛋白富集。其他家族成员在大鼠脑内显示出高度不同的mRNA转录表达模式。目前的研究结果提出了一种机制,通过该机制PP1可能被导向与肌动蛋白细胞骨架相关的神经元底物。