L-periaxin interacts with S-periaxin through its PDZ domain
L-periaxin interacts with S-periaxin through its PDZ domain
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L-periaxin 通过其 PDZ 结构域与 S-periaxin 相互作用
DOI：
10.1016/j.neulet.2015.10.020
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发表时间：
2015-11
影响因子：
2.5
通讯作者：
Yawei Shi
中科院分区：
文献类型：
--
作者：
Yenan Yang;Yawei Shi
Periaxin was first identified as a protein in myelinating Schwann cells through a screen of novel cytoskeleton-associated proteins in peripheral nerve myelination. Theperiaxingene encodes two isoforms, namely, L- and S-periaxin, which are 1461 and 147 residues in size, respectively. Several loss-of-function mutations linked to autosomal recessive Dejerine–Sottas neuropathy and demyelinating Charcot–Marie–Tooth disease inperiaxinhave been described. In this study, the colocolization of L- and S-periaxin in the cytoplasm of RSC96 cells was found by immunofluorescence assays. The interaction between these two isoforms was confirmed by co-immunoprecipitation, fluorescence complementation experiment, and GST pull-down assay. Results also showed that the twoperiaxinisoforms interacted in the cytoplasm through the PDZ domain, and their interaction prevented the homodimerization of L-periaxin. S-periaxin may regulate the function of L-periaxin in Schwann cells.
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影响因子：
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