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- W2301910062 abstract "Periaxin is expressed in mammalian Schwann cells and lens fiber cells, and has been identified in a screen for cytoskeleton-associated proteins. Charcot-Marie-Tooth 4F is caused by losses or mutations of theperiaxingene. Theperiaxingene encodes two protein isoforms, namely, L-periaxin and S-periaxin.S-periaxin contains 147 amino acid residues and has an N-terminal PDZ domain. In this paper, S-periaxin was reported to be homodimerized through the formation of intermolecular disulfide bonds with its Cys88 and Cys139 residues under mild oxidation conditions. The covalent dimer of S-periaxin was also observed by western blot analysis and bimolecular fluorescence complementation analyses. S-periaxin dimerization formation could be regulated by cellular redox fluctuations. These results offer a possible mechanism to the formation of periaxin complexes, improvement of complex stability, and establishment of a link between the extracellular matrix and the cytoskeleton." @default.
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- W2301910062 date "2016-04-01" @default.
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- W2301910062 title "Intermolecular disulfide bond in the dimerization of S-periaxin mediated by Cys88 and Cys139" @default.
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- W2301910062 doi "https://doi.org/10.1093/abbs/gmw008" @default.
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