The Ca(2+)-dependent interaction of calpastatin domain L with the C-terminal tail of the Cav1.2 channel

FEBS Lett. 2014 Mar 3;588(5):665-71. doi: 10.1016/j.febslet.2014.01.019. Epub 2014 Jan 23.

Abstract

To demonstrate the interaction of calpastatin (CS) domain L (CSL) with Cav1.2 channel, we investigated the binding of CSL with various C-terminus-derived peptides at≈free, 100 nM, 10 μM, and 1mM Ca(2+) by using the GST pull-down assay method. Besides binding with the IQ motif, CSL was also found to bind with the PreIQ motif. With increasing [Ca(2+)], the affinity of the CSL-IQ interaction gradually decreased, and the affinity of the CSL-PreIQ binding gradually increased. The results suggest that CSL may bind with both the IQ and PreIQ motifs of the Cav1.2 channel in different Ca(2+)-dependent manners.

Keywords: Affinity; Binding; Ca(2+); Calpastatin; Cav1.2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Calcium / chemistry*
  • Calcium Channels, L-Type / chemistry*
  • Calcium-Binding Proteins / chemistry*
  • Guinea Pigs
  • Humans
  • Peptide Fragments / chemistry
  • Protein Binding
  • Protein Interaction Domains and Motifs

Substances

  • Calcium Channels, L-Type
  • Calcium-Binding Proteins
  • L-type calcium channel alpha(1C)
  • Peptide Fragments
  • calpastatin
  • Calcium