Müller B M, Kistner U, Kindler S, Chung W J, Kuhlendahl S, Fenster S D, Lau L F, Veh R W, Huganir R L, Gundelfinger E D, Garner C C
Center for Molecular Neurobiology, University of Hamburg, Federal Republic of Germany.
Neuron. 1996 Aug;17(2):255-65. doi: 10.1016/s0896-6273(00)80157-9.
Synapse-associated proteins (SAPs) are constituents of the pre- and postsynaptic submembraneous cytomatrix. Here, we present SAP102, a novel 102kDa SAP detected in dendritic shafts and spines of asymmetric type 1 synapses. SAP102 is enriched in preparations of synaptic junctions, where it biochemically behaves as a component of the cortical cytoskeleton. Antibodies directed against NMDA receptors coimmunoprecipitate SAP102 from rat brain synaptosomes. Recombinant proteins containing the carboxy-terminal tail of NMDA receptor subunit NR2B interact with SAP102 from rat brain homogenates. All three PDZ domains in SAP102 bind the cytoplasmic tail of NR2B in vitro. These data represent direct evidence that in vivo SAP102 is involved in linking NMDA receptors to the submembraneous cytomatrix associated with postsynaptic densities at excitatory synapses.
突触相关蛋白（SAPs）是突触前和突触后膜下细胞基质的组成成分。在此，我们介绍SAP102，一种在不对称1型突触的树突干和棘中检测到的新型102kDa的突触相关蛋白。SAP102在突触连接制剂中富集，在生化性质上它表现为皮质细胞骨架的一个组成部分。针对NMDA受体的抗体能从大鼠脑突触体中共免疫沉淀出SAP102。含有NMDA受体亚基NR2B羧基末端尾巴的重组蛋白能与大鼠脑匀浆中的SAP102相互作用。在体外，SAP102的所有三个PDZ结构域都能结合NR2B的胞质尾巴。这些数据直接证明，在体内SAP102参与将NMDA受体与兴奋性突触处与突触后致密物相关的膜下细胞基质相连。
