Ca2+ signaling and Target Binding Regulations: Calmodulin and Centrin In Vitroand In VivoJuan Martinez-Sanz1,2,3, Dora Grecu1,2 and Liliane Assairi1,2*
- Corresponding Author:
- Assairi L
Institut Curie, Research Center, INSERM U759
15 Rue Georges Clemenceau, University Center Orsay
Building 112, F-91405 Orsay Cedex, France
E-mail: [email protected]
Received Date: March 28, 2016; Accepted Date: December 22, 2016; Published Date: December 26, 2016
Citation: Martinez-Sanz J, Grecu D, Assairi L (2016) Ca2+ signaling and Target Binding Regulations: Calmodulin and Centrin In Vitro and In Vivo. Bioenergetics 5:144. doi:10.4172/2167-7662.1000144
Copyright: © 2016 Martinez-Sanz J et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Changes in Ca2+ concentrations act as a second messenger to regulate biological processes. Ca2+ sensor proteins transduce these Ca2+ signals upon binding to protein targets that are involved in the cellular process that is being regulated.
Ca2+ sensor proteins such as calmodulin and centrin bind Ca2+ through acidic residues that compose the EFhand motifs and further bind targets via surfaces that recognize specific motifs on targets. However, in some cases, the binding of a Ca2+ sensor protein to a target can occur in the absence of Ca2+. Upon Ca2+ binding, Ca2+-sensor proteins undergo conformational changes, which lead to the exposure of surface that interacts with target. Moreover, Ca2+ binding and the binding of Ca2+ sensors to targets induce conformational changes that drive regulation. Comparisons of the Ca2+-sensor proteins calmodulin and centrin provide information on regulatory processes.