Two PDZ domain proteins encoded by the murine periaxin gene are the result of alternative intron retention and are differentially targeted in Schwann cells

Two PDZ domain proteins encoded by the murine periaxin gene are the result of alternative intron retention and are differentially targeted in Schwann cells
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DOI:
10.1074/jbc.273.10.5794
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发表时间:
1998-03-06
影响因子:
4.8
通讯作者:
Brophy, PJ
Brophy, PJ
中科院分区:
生物学2区
文献类型:
--
作者:
Dytrych, L;Sherman, DL;Brophy, PJ

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Periaxin首先被描述为一种147-kDa的蛋白质,基于其丰度、细胞类型特异性、发育表达模式和定位,认为其在外周神经中髓磷脂沉积的起始中具有潜在作用(吉莱斯皮,C.美国,谢尔曼,D. L.,Blair,G. E、还有布罗菲P. J.(1994)Neuron 12,497-508)。在此,我们显示鼠periaxin基因跨越20.6个磷酸酶并编码4.6和5.2个磷酸酶的两种mRNA,所述mRNA编码两种periaxin同种型,分别为147和16 kDa的L-periaxin和S-periaxin。较大的mRNA由保留内含子机制产生,该机制引入终止密码子并产生具有内含子编码的21个氨基酸的C末端的截短蛋白。这两种蛋白质在N末端都具有PDZ结构域;然而,它们在许旺细胞中的靶向不同,与其他含有PDZ结构域的蛋白质一样,L-周蛋白定位于髓鞘形成的许旺细胞的质膜:相反,S-轴周蛋白在细胞质中弥散表达,这表明,含有这种蛋白结合模块的蛋白质也可能参与蛋白质结合。蛋白质相互作用的网站以外的细胞皮质。
Periaxin was first described as a 147-kDa protein that was suggested to have a potential role in the initiation of myelin deposition in peripheral nerves based upon its abundance, cell type specificity, pattern of developmental expression, and localization (Gillespie, C. S., Sherman, D. L., Blair, G. E., and Brophy. P. J. (1994) Neuron 12, 497-508), Here we show that the murine periaxin gene spans 20.6 kilobases and encodes two mRNAs of 4.6 and 5.2 kilobases that encode two periaxin isoforms, L-periaxin and S-periaxin of 147 and 16 kDa respectively. The larger mRNA is produced by a retained intron mechanism that introduces a stop codon and results in a truncated protein with an intron-encoded C terminus of 21 amino acids. Both proteins possess a PDZ domain at the N terminus; nevertheless, they are targeted differently in Schwann cells, Like other proteins that contain PDZ domains, L-periaxin is localized to the plasma membrane of myelinating Schwann cells: in contrast, S-periaxin is expressed diffusely in the cytoplasm, This suggests that proteins that contain this protein-binding module may also participate in protein-protein interactions at sites other than the cell cortex.