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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Sun W,Feng R,Hu H,Guo F,Gao Q,Shao D,Yin D,Wang H,Sun X,Zhao M,Minobe E,Sun Y,Jiao G,Kameyama M,Hao L

doi

10.1016/j.febslet.2014.01.019

subject

Has Abstract

pub_date

2014-03-03 00:00:00

pages

665-71

issue

5

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(14)00046-5

journal_volume

588

pub_type

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