IDENTIFICATION OF THE MAJOR POSTSYNAPTIC DENSITY PROTEIN AS HOMOLOGOUS WITH THE MAJOR CALMODULIN-BINDING SUBUNIT OF A CALMODULIN-DEPENDENT PROTEIN-KINASE
IDENTIFICATION OF THE MAJOR POSTSYNAPTIC DENSITY PROTEIN AS HOMOLOGOUS WITH THE MAJOR CALMODULIN-BINDING SUBUNIT OF A CALMODULIN-DEPENDENT PROTEIN-KINASE
复制标题
DOI：
10.1111/j.1471-4159.1984.tb12713.x
复制
发表时间：
1984-01-01
影响因子：
4.7
通讯作者：
DELORENZO, RJ
中科院分区：
文献类型：
--
作者：
GOLDENRING, JR;MCGUIRE, JS;DELORENZO, RJ
主要突触后密度蛋白（mPSDp），包括> 50%的突触后密度（PSD）蛋白，是钙调蛋白依赖性磷酸化的内源性底物以及PSD制剂中的钙调蛋白结合蛋白。mPSD似乎与主要钙调蛋白结合亚基（ρ）高度同源。的微管蛋白相关钙调蛋白依赖性激酶（TACK），并且PSD级分也含有与σ-β-钙调蛋白依赖性激酶（TACK）同源的蛋白质。TACK的亚基。mPSDp和63，000道尔顿PSD蛋白质之间的同源性和ρ-和σ- TACK的亚基通过以下标准建立：相同的表观MW;相同的钙调蛋白结合特性; Ca 2 +-钙调蛋白刺激的自磷酸化的表现;相同的等电点;在二维凝胶上相同的钙调蛋白结合和自磷酸化模式;同源的二维胰蛋白酶肽图谱;和微管蛋白的相似的磷酸氨基酸特异性磷酸化。显然，mPSDp是一种钙调蛋白结合蛋白，参与调节突触后致密区的蛋白激酶活性，并且与TACK同源的微管蛋白激酶系统以膜结合形式存在于PSD中。
The major postsynaptic density protein (mPSDp), comprising > 50% of postsynaptic density (PSD) protein, is an endogenous substrate for calmodulin-dependent phosphorylation as well as a calmodulin-binding protein in PSD preparations. mPSD seems highly homologous with major calmodulin-binding subunit (.rho.) of [rat brain] tubulin-associated calmodulin-dependent kinase (TACK), and PSD fractions also contain a protein homologous with the .sigma.-subunit of TACK. Homologies between mPSDp and a 63,000 dalton PSD protein and the .rho.- and .sigma.-subunits of TACK were established by the following criteria: identical apparent MW; identical calmodulin-binding properties; manifestation of Ca2+-calmodulin-stimulated autophosphorylation; identical isoelectric points; identical calmodulin binding and autophosphorylation patterns on 2-dimensional gels; homologous 2-dimensional tryptic peptide maps; and similar phosphoamino acid-specific phosphorylation of tubulin. Evidently, mPSDp is a calmodulin-binding protein involved in modulating protein kinase activity in the postsynaptic density and a tubulin kinase system homologous with TACK exists in a membrane-bound form in the PSD.