Calmodulin as a protein linker and a regulator of adaptor/scaffold proteins.

Antonio Villalobo, Hiroaki Ishida, Hans J Vogel, Martin W Berchtold

Journal: Biochimica et biophysica acta. Molecular cell research 2018;1865(3):507-521

PMID: 29247668

Abstract

Calmodulin (CaM) is a universal regulator for a huge number of proteins in all eukaryotic cells. Best known is its function as a calcium-dependent modulator of the activity of enzymes, such as protein kinases and phosphatases, as well as other signaling proteins including membrane receptors, channels and structural proteins. However, less well known is the fact that CaM can also function as a Ca-dependent adaptor protein, either by bridging between different domains of the same protein or by linking two identical or different target proteins together. These activities are possible due to the fact that CaM contains two independently-folded Ca binding lobes that are able to interact differentially and to some degree separately with targets proteins. In addition, CaM can interact with and regulates several proteins that function exclusively as adaptors. This review provides an overview over our present knowledge concerning the structural and functional aspects of the role of CaM as an adaptor protein and as a regulator of known adaptor/scaffold proteins.

Copyright © 2017 Elsevier B.V. All rights reserved.

Address: Department of Cancer Biology, Instituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas and Universidad Autónoma de Madrid, Arturo Duperier 4, E-28029 Madrid, Spain. Electronic address: [email protected].; Department of Biological Sciences, University of Calgary, 2500 University Dr. N.W., Calgary, Alberta T2N 1N4, Canada.; Department of Biological Sciences, University of Calgary, 2500 University Dr. N.W., Calgary, Alberta T2N 1N4, Canada. Electronic address: [email protected].; Department of Biology, University of Copenhagen, 13 Universitetsparken, DK-2100 Copenhagen Ø, Denmark. Electronic address: [email protected].
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