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Calcium Protein Signaling pp 135–145Cite as

Molecular Analysis of Calmodulin and Smooth Muscle Myosin Light Chain Kinase

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 255))

Abstract

Of all the known members of the superfamily of proteins that utilize the EF-hand helix-loop-helix configuration to bind Ca++, calmodulin is unique. This intracellular receptor is ubiquitous in eukaryotes and is highly conserved at the primary amino acid sequence level. In vertebrates only a single conservative amino acid substitution exists between fish and humans 1. Even between primitive eukaryotes such as yeasts and higher vertebrate species, the proteins show at least 80% amino acid identity. In addition calmodulin serves as the obligatory Ca++-dependent activator of a variety of enzymes, exists in enzyme and organelle complexes in the Ca free state and is associated with several intracellular structural proteins. These characteristics are in sharp contrast to other members of this superfamily such as troponin C, calbindins, S-100, calretinin, calcineurin B and myosin light chains. The function of these proteins, when known, tends to be highly specific. Distribution is largely restricted to vertebrates and even within members of this phylum, is found only in selected cell types. The one exception to this generalization is calcineurin B which enjoys a much broader species distribution. However this breadth may also be related to calmodulin since calcineurin is the only known Ca /calmodulin-dependent protein phosphatase. Indeed some calmodulin-dependent enzymes are more widely distributed among phyla and between cell types of a given organism than are the other members of the calmodulin superfamily 2.

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Author information

Authors and Affiliations

  1. Department of Cell Biology, Baylor College of Medicine, Houston, TX, 77030, USA

    Anthony R. Means, Mark F. A. VanBerkum, Samuel E. George & Indrani C. Bagchi

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  1. Anthony R. Means
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  2. Mark F. A. VanBerkum
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  3. Samuel E. George
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  4. Indrani C. Bagchi
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Editor information

Editors and Affiliations

  1. Nagoya University, Nagoya, Japan

    H. Hidaka

  2. Swiss Federal Institute of Technology, Zurich, Switzerland

    E. Carafoli

  3. Baylor College of Medicine, Houston, Texas, USA

    A. R. Means

  4. Mie University School of Medicine, Mie, Japan

    T. Tanaka

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© 1989 Plenum Press, New York

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Means, A.R., VanBerkum, M.F.A., George, S.E., Bagchi, I.C. (1989). Molecular Analysis of Calmodulin and Smooth Muscle Myosin Light Chain Kinase. In: Hidaka, H., Carafoli, E., Means, A.R., Tanaka, T. (eds) Calcium Protein Signaling. Advances in Experimental Medicine and Biology, vol 255. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5679-0_15

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  • DOI: https://doi.org/10.1007/978-1-4684-5679-0_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5681-3

  • Online ISBN: 978-1-4684-5679-0

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