The actin-binding domain of spinophilin is necessary and sufficient for targeting to dendritic spines
The actin-binding domain of spinophilin is necessary and sufficient for targeting to dendritic spines
复制标题
DOI：
10.1385/nmm:2:1:61
复制
发表时间：
2002-01-01
影响因子：
3.5
通讯作者：
Greengard, P
中科院分区：
文献类型：
--
作者：
Grossman, SD;Hsieh-Wilson, LC;Greengard, P
嗜刺素在树突棘中富集，树突棘是突触后膜沿着树突长度的小突起，包含大多数兴奋性突触。嗜刺素以高亲和力结合蛋白磷酸酶1，并将其靶向树突棘，因此将其置于附近以调节谷氨酸受体活性。嗜刺素还结合并捆绑f-肌动蛋白（树突棘的主要细胞骨架成分），因此可能有助于调节突触的结构。在这项研究中，我们试图确定的结构基础为靶向的spinophilin树突棘。我们的研究结果表明，肌动蛋白结合结构域的spinophilin是必要的和足够的靶向树突和树突棘的spinophilin。
Spinophilin is enriched in dendritic spines, small protrusions of the postsynaptic membrane along the length of the dendrite that contain the majority of excitatory synapses. Spinophilin binds to protein phosphatase 1 with high affinity and targets it to dendritic spines, therefore placing it in proximity to regulate glutamate receptor activity. Spinophilin also binds to and bundles f-actin, the main cytoskeletal constituent of dendritic spines, and may therefore serve to regulate the structure of the synapse. In this study, we sought to determine the structural basis for the targeting of spinophilin to dendritic spines. Our results show that the actinbinding domain of spinophilin is necessary and sufficient for targeting of spinophilin to dendrites and dendritic spines.