Gap junction regulation by calmodulin.
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.
Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Juan
J
Zou
Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Mani
M
Salarian
Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, United States.
Yanyi
Y
Chen
Department of Pharmacology, SUNY Upstate Medical University, Syracuse, NY 13210, United States.
Richard
R
Veenstra
Department of Cell Biology and Neuroscience, University of California, Riverside, CA 92521, United States. Electronic address: charles.louis@ucr.edu.
Charles F
CF
Louis
Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, United States. Electronic address: jenny@gsu.edu.
Jenny J
JJ
Yang
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000378:metabolism*; D017630:Connexins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D011485:Protein Binding
D002147:Calmodulin; D017630:Connexins; D002118:Calcium
Ca(2+); Calmodulin binding; Connexin; Gap junction regulation