Functional Contribution of Ca(2+) and Mg (2+) to the Intermolecular Interaction of Visinin-like Proteins.
The interaction of human visinin-like protein 1 (VILIP1) and visinin-like protein 3 (VILIP3) with divalent cations (Mg(2+), Ca(2+), Sr(2+) and Ba(2+)) was explored using circular dichroism and fluorescence measurement. These results showed that the four cations each induced a different subtle change in the conformation of VILIPs. Moreover, VILIP1 and VILIP3 bound with Ca(2+) or Mg(2+) in a cooperative manner. Studies on the truncated mutants showed that the intact EF-3 and EF-4 were essential for the binding of VILIP1 with Ca(2+) and Mg(2+). Pull-down assay revealed that Ca(2+) and Mg(2+) enhanced the intermolecular interaction of VILIPs, and led to the formation of homo- and hetero-oligomer of VILIPs. Together with previous findings that Ca(2+)-dependent localization of VILIPs may be involved in the regulation of distinct cascades and deprivation of Ca(2+)-binding capacity of VILIPs did not completely eliminate their activity, it is likely to reflect that Mg(2+)-bound VILIPs may play a role in regulating the biological function of VILIPs in response to a concentration fluctuation of Ca(2+) in cells.[1]References
- Functional Contribution of Ca(2+) and Mg (2+) to the Intermolecular Interaction of Visinin-like Proteins. Jheng, F.F., Wang, L., Lee, L., Chang, L.S. Protein J. (2006) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
