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Tightly-bound divalent cation of actin

Journal of Muscle Research & Cell Motility volume 13, pages 272–284 (1992)Cite this article

Summary

Actin is known to undergo reversible monomer-polymer transitions that coincide with various cell activities such as cell shape changes, locomotion, endocytosis and exocytosis. This dynamic state of actin filament self-assembly and disassembly is thought to be regulated by the properties of the monomeric actin molecule andin vivo by the influence of actin-associated proteins. Of major importance to the properties of the monomeric actin molecule are the presence of one tightly-bound ATP and one tighly-bound divalent cation per molecule.In vivo the divalent cation is thought to be Mg2+ (Mg-actin) butin vitro standard purification procedures result in the preparation of Ca-actin. The affinity of actin for a divalent cation at the tight binding site is in the nanomolar range, much higher than earlier thought. The binding kinetics of Mg2+ and Ca2+ at the high affinity site on actin are considered in terms of a simple competitive binding mechanism. This model adequately describes the published observations regarding divalent cation exchange on actin. The effects of the tightly-bound cation, Mg2+ or Ca2+, on nucleotide binding and exchange on actin, actin ATP hydrolysis activity and nucleation and polymerization of actin are discussed. From the characteristics that are reviewed, it is apparent that the nature of the bound divalent cation has a significant effect on the properties of actin.

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Abbreviations

I-AEDANS:

N-iodoacetyl-N′-(5-sulpho-1 -naphthyl)ethylenediamine

Quin 2:

2-[(2-bis-[carboxymethyl]amino-5-methylphenoxyl) methyl]-6-methoxy-8-bis[carboxymethyl] aminoquinoline

BAPTA:

1,2-bis(o-aminophenoxy)-ethane-N,N,N′,N′-tetraacetic acid

DCF-actin:

N-(-pyrenyl)iodoacetamide

pyrene:

divalent cation-free actin

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Affiliations

  1. Research Service, Veterans Administration Medical Centre, 12208, Albany, New York, USA

    James E. Estes & Lynn A. Selden

  2. Medical Service, Veterans Administration Medical Centre, 12208, Albany, New York, USA

    Lewis C. Gershman

  3. Department of Physiology and Cell Biology, Albany Medical College, 12208, Albany, New York, USA

    James E. Estes, Henry J. Kinosian & Lewis C. Gershman

  4. Department of Medicine, Albany Medical College, 12208, Albany, New York, USA

    Lewis C. Gershman

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Estes, J.E., Selden, L.A., Kinosian, H.J. et al. Tightly-bound divalent cation of actin. J Muscle Res Cell Motil 13, 272–284 (1992). https://doi.org/10.1007/BF01766455

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  • DOI: https://doi.org/10.1007/BF01766455

Keywords

  • Actin Filament
  • Divalent Cation
  • Shape Change
  • Hydrolysis Activity
  • Purification Procedure