Regulatory elements and functional implication for the formation of dimeric visinin-like protein-1

Ku Chung Chen, Li Kuan Wang, Long Sen Chang

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


Size exclusion chromatographic analyses showed that Ca2+-free VILIP-1 contained both monomeric and dimeric forms, while no appreciable dimerization was noted with Ca2+-free VILIP-3. Swapping of EF-hands 3 and 4 of VILIP-1 with those of VILIP-3 caused the inability of the resulting chimeric protein to form dimeric protein. Nonreducing SDS-PAGE analyses revealed that most of the dimeric VILIP-1 was noncovalently bound together. Reduced glutathione (GSH)/oxidized glutathione (GSSG) treatment notably enhanced the formation of disulfide-linked VILIP-1 dimer, while Ca2+ and Mg2+ enhanced disulfide dimerization of VILIP-1 marginally in the presence of thiol compounds. Cys-187 at the C-terminus of VILIP-1 contributed greatly to form S-S-crosslinked dimer as revealed by mutagenesis studies. The ability of GSH/GSSG-treated VILIP-1 to activate guanylyl cyclase B was reduced by substituting Cys-187 with Ala. Together with disulfide dimer of VILIP-1 detected in rat brain extracts, our data may imply the functional contribution of disulfide dimer to the interaction of VILIP-1 with its physiological target(s).

Original languageEnglish
Pages (from-to)89-94
Number of pages6
JournalJournal of Peptide Science
Issue number2
Publication statusPublished - 2009
Externally publishedYes


  • Dimerization
  • Disulfide bond
  • Mutagenesis
  • VILIP-1

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry


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