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PMID: 1527214 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

Tightly-bound divalent cation of actin.

Journal of muscle research and cell motility ·Vol. 13 ·No. 3 ·1992-06-00 ·Pages 272-84

Estes JE, Selden LA, Kinosian HJ, Gershman LC

Abstract

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 and in 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 tightly-bound divalent cation per molecule. In vivo the divalent cation is thought to be Mg2+ (Mg-actin) but in 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.

MeSH Terms
Actins/metabolism Adenosine Triphosphate/metabolism Allosteric Regulation Allosteric Site Animals Binding Sites Binding, Competitive Calcium/metabolism Hydrolysis Kinetics Magnesium/metabolism Models, Biological Polymers Protein Binding Protein Conformation
Chemicals
Actins Polymers Adenosine Triphosphate Magnesium Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Estes J E
Research Service, Veterans Administration Medical Centre, Albany, New York 12208.
Selden L A
Kinosian H J
Gershman L C
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Article Info
Journal
Journal of muscle research and cell motility
Abbr.
J Muscle Res Cell Motil
ISSN
0142-4319
DOI
10.1007/BF01766455
Published
1992-06-00
Pages
272-84
Language
English
Region
Netherlands
NLM ID
8006298
Subset
IM
Grants
NIGMS NIH HHS · GM 32007 · United States
External Links
PubMed source DOI: 10.1007/BF01766455 View journal details
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