Premium
Gap junction regulation by calmodulin
Author(s) -
Zou Juan,
Salarian Mani,
Chen Yanyi,
Veenstra Richard,
Louis Charles F.,
Yang Jenny J.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.01.003
Subject(s) - connexin , calmodulin , gap junction , intracellular , microbiology and biotechnology , binding site , chemistry , biology , biophysics , biochemistry , enzyme
Intracellular Ca 2+ activated calmodulin (CaM) inhibits gap junction channels in the low nanomolar to high micromolar range of [Ca 2+ ] i . This regulation plays an essential role in numerous cellular processes that include hearing, lens transparency, and synchronized contractions of the heart. Previous studies have indicated that gap junction mediated cell‐to‐cell communication was inhibited by CaM antagonists. More recent evidence indicates a direct role of CaM in regulating several members of the connexin family. Since the intracellular loop and carboxyl termini of connexins are largely “invisible” in electron microscopy and X‐ray crystallographic structures due to disorder in these domains, peptide models encompassing the putative CaM binding sites of several intracellular domains of connexins have been used to identify the Ca 2+ ‐dependent CaM binding sites of these proteins. This approach has been used to determine the CaM binding affinities of peptides derived from a number of different connexin‐subfamilies.