Retracted Article: Self-association of L-periaxin occurs via its acidic domain and NLS2/NLS3, and affects its trafficking in RSC96 cells

Abstract

Periaxin (PRX) protein was first identified in myelinating Schwann cells through the screening of cytoskeleton-associated proteins in peripheral nerve myelination. PRX plays a significant role in myelin sheath formation and myelin stability, and is closely related to tumor cell metastasis. As described, several loss-of-function mutations were linked to autosomal recessive Dejerine–Sottas neuropathy and demyelinating Charcot–Marie–Tooth disease, type 4F (CMT4F) caused by periaxin mutation. In this study, we report that L-PRX self-association occurs by head-to-tail joining of the nuclear localization signal NLS2 and NLS3 in the tripartite nuclear localization signal and acidic domains. The self-association of L-PRX in RSC96 cells is remarkably weakened by DRP2 and the synthetic NLS3 peptide. In the acidic domain of L-PRX, E1259K mutation weakens the head-to-tail interaction, causing CMT4F disease. The membrane localization of L-PRX in RSC96 was increased by the disruption of self-association by DRP2 and the synthetic NLS3 peptide. The self-association of L-PRX is a possible type of self-regulation of PRX during the localization between the cell membrane and cytoplasm or nucleus.