Making the connection - shared molecular machinery and evolutionary links underlie the formation and plasticity of occluding junctions and synapses
Making the connection - shared molecular machinery and evolutionary links underlie the formation and plasticity of occluding junctions and synapses
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DOI：
10.1242/jcs.186627
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发表时间：
2016-08-15
影响因子：
4
通讯作者：
Krieger, Charles
中科院分区：
文献类型：
--
作者：
Harden, Nicholas;Wang, Simon Ji Hau;Krieger, Charles
褶皱分隔结（pSJ）是无脊椎动物上皮细胞中细胞间接触的古老结构，其蛋白质成分存在于三种较新的连接结构中，即神经元突触、有髓鞘轴突的旁节区和脊椎动物上皮紧密连接。这些较新的结构似乎是通过改变祖先的分隔连接而进化而来的。在发育中的动物形成过程中，pSJ表现出可塑性，尽管最终结构非常坚固。与未成熟的pSJ类似，突触和紧密连接都表现出可塑性，我们认为有证据表明这种可塑性至少部分来自免疫球蛋白细胞粘附分子超家族成员与高度调节的膜相关鸟苷酸激酶的相互作用。这种可塑性调节可能是为了调节祖先的pSJ而产生的，并在衍生结构中得到维持；我们建议在研究其中一种结构的可塑性时考虑其他结构的文献是有益的。最后，在连接处之外，我们强调了上皮膜和突触膜之间的相似之处，它们都显示出许多相同蛋白质的极化分布-证据表明上皮中顶基底极性的决定因素也参与突触的模式。
The pleated septate junction (pSJ), an ancient structure for cell-cell contact in invertebrate epithelia, has protein components that are found in three more-recent junctional structures, the neuronal synapse, the paranodal region of the myelinated axon and the vertebrate epithelial tight junction. These more-recent structures appear to have evolved through alterations of the ancestral septate junction. During its formation in the developing animal, the pSJ exhibits plasticity, although the final structure is extremely robust. Similar to the immature pSJ, the synapse and tight junctions both exhibit plasticity, and we consider evidence that this plasticity comes at least in part from the interaction of members of the immunoglobulin cell adhesion molecule superfamily with highly regulated membrane-associated guanylate kinases. This plasticity regulation probably arose in order to modulate the ancestral pSJ and is maintained in the derived structures; we suggest that it would be beneficial when studying plasticity of one of these structures to consider the literature on the others. Finally, looking beyond the junctions, we highlight parallels between epithelial and synaptic membranes, which both show a polarized distribution of many of the same proteins - evidence that determinants of apicobasal polarity in epithelia also participate in patterning of the synapse.