Intermolecular disulfide bond in the dimerization of S-periaxin mediated by Cys88 and Cys139

Acta Biochim Biophys Sin (Shanghai). 2016 Apr;48(4):326-33. doi: 10.1093/abbs/gmw008. Epub 2016 Mar 2.


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.

Keywords: S-periaxin; bimolecular fluorescence complementation analyses; cysteine; dimer; intermolecular disulfide bond.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cysteine / chemistry*
  • Dimerization
  • Disulfides / chemistry*
  • HeLa Cells
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Sequence Homology, Amino Acid


  • Disulfides
  • Membrane Proteins
  • periaxin
  • Cysteine