Gap junction regulation by calmodulin |
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Institution: | 1. Department of Chemistry, Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, United States;2. Department of Pharmacology, SUNY Upstate Medical University, Syracuse, NY 13210, United States;3. Department of Cell Biology and Neuroscience, University of California, Riverside, CA 92521, United States |
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Abstract: | Intracellular Ca2+ activated calmodulin (CaM) inhibits gap junction channels in the low nanomolar to high micromolar range of Ca2+]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 Ca2+-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. |
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Keywords: | Connexin Gap junction regulation Calmodulin binding |
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