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Ion binding to calmodulin

A comparison with other intracellular calcium-binding proteins

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Summary

Over the past few years calcium has emerged as an important bioregulator. Upon external stimulation, the cell generates a transient Ca2+ increase, which is transformed into a cellular event through a molecular cascade. The first step in this cascade is the binding of calcium to proteins present in the cytosol. These proteins capable of binding Ca2+ under physiological conditions all belong to the same evolutionary family that evolved from a common ancestor. However, they strongly differ in the properties of their calcium binding sites. Calmodulin, the ubiquitous calcium binding protein present in all eukaryotic cells, is very close to the ancestor protein, presents four calcium binding sites which bind calcium, magnesium and monovalent ions competitively and is involved in the triggering of cellular processes. Parvalbumin, another member of the family, is more specialized and found mostly in fast-twitch skeletal muscle. It binds calcium and magnesium with high affinity and seems to be involved in muscle relaxation. On the other hand, troponin C which confers Ca2+ sensitivity to acto-myosin interaction exhibits both triggering and relaxing sites. The study of intracellular Ca2− binding proteins has shown that calcium binding proteins have evolved from a simple common structure to fulfill different functions.

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Abbreviations

CaBP:

calcium-binding protein

ICaBP:

the vitamin D-dependent intestinal Cat+binding protein

S-100:

the glial S-100 protein

RLC:

the phosphorylatable myosin regulatory light chain

CaM:

calmodulin

Pa:

parvalbumin

TnC:

troponin C

TnI:

troponin I

Hepes:

N-2-hydroxyethylpipezarine, N′-2-ethane-sulfonic acid

W7:

N-(6-Aminohexyl)-5-chloro-l-Naphtalene sulfonamide

SDS:

sodium dodecyl sulfate

NMR:

nuclear magnetic resonance

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  1. Centre de Recherches de Biochimie macromoléculaire du C. N. R. S., Unite L N. S. E. R. M. 249 and Faculté de Médecine, B. P. 5015, 34033, Montpellier Cedex

    Marie-Claude Kilhoffer, Jacques Haiech & Jacques G. Demaille

  2. Université Louis Pasteur, Faculté de Pharmacie ERA 551, B.P. 10, 67048, Strasbourg Cedex, France

    Marie-Claude Kilhoffer

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  1. Marie-Claude Kilhoffer
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Kilhoffer, MC., Haiech, J. & Demaille, J.G. Ion binding to calmodulin. Mol Cell Biochem 51, 33–54 (1983). https://doi.org/10.1007/BF00215584

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