Functional Contribution of Ca2+ and Mg2+ to the Intermolecular Interaction of Visinin-like Proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-05-16

AUTHORS

Feng-Fin Jheng, Likuan Wang, Liya Lee, Long-Sen Chang

ABSTRACT

The interaction of human visinin-like protein 1 (VILIP1) and visinin-like protein 3 (VILIP3) with divalent cations (Mg2+, Ca2+, Sr2+ and Ba2+) 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 Ca2+ or Mg2+ 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 Ca2+ and Mg2+. Pull-down assay revealed that Ca2+ and Mg2+ enhanced the intermolecular interaction of VILIPs, and led to the formation of homo- and hetero-oligomer of VILIPs. Together with previous findings that Ca2+-dependent localization of VILIPs may be involved in the regulation of distinct cascades and deprivation of Ca2+-binding capacity of VILIPs did not completely eliminate their activity, it is likely to reflect that Mg2+-bound VILIPs may play a role in regulating the biological function of VILIPs in response to a concentration fluctuation of Ca2+ in cells. More... »

PAGES

250-256

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10930-006-9008-5

DOI

http://dx.doi.org/10.1007/s10930-006-9008-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1023673105

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16703469


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