Phalloidin Binding and Rheological Differences among Actin Isoforms
Actin is a highly conserved protein in eukaryotes, yet different isoforms of this protein can be found within the same cell. To begin to explore whether isoactin sequence diversity leads to functional differences in actin filaments, we have examined the phalloidin binding kinetics and the bulk rheol...
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| Published in | Biochemistry (Easton) Vol. 35; no. 45; pp. 14062 - 14069 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
American Chemical Society
12.11.1996
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| Subjects | |
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| Abstract | Actin is a highly conserved protein in eukaryotes, yet different isoforms of this protein can be found within the same cell. To begin to explore whether isoactin sequence diversity leads to functional differences in actin filaments, we have examined the phalloidin binding kinetics and the bulk rheologic properties of purified actin isoforms from a variety of eukaryotic sources. We observe differences in the phalloidin association kinetics between muscle α- and cytoplasmic actins. Phalloidin dissociates from all mammalian actin isoforms tested at the same slow rate, while dissociation from yeast actin is 1 order of magnitude more rapid. The actin isoforms form viscoelastic gels to varying degrees with skeletal muscle α-actin gels being the most elastic, smooth muscle α- and γ-actins being less elastic, and β-actin not forming elastic structures under our experimental conditions. The sequence variation among isoforms is discussed in light of these biophysical and biochemical differences. |
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| AbstractList | Actin is a highly conserved protein in eukaryotes, yet different isoforms of this protein can be found within the same cell. To begin to explore whether isoactin sequence diversity leads to functional differences in actin filaments, we have examined the phalloidin binding kinetics and the bulk rheologic properties of purified actin isoforms from a variety of eukaryotic sources. We observe differences in the phalloidin association kinetics between muscle α- and cytoplasmic actins. Phalloidin dissociates from all mammalian actin isoforms tested at the same slow rate, while dissociation from yeast actin is 1 order of magnitude more rapid. The actin isoforms form viscoelastic gels to varying degrees with skeletal muscle α-actin gels being the most elastic, smooth muscle α- and γ-actins being less elastic, and β-actin not forming elastic structures under our experimental conditions. The sequence variation among isoforms is discussed in light of these biophysical and biochemical differences. Actin is a highly conserved protein in eukaryotes, yet different isoforms of this protein can be found within the same cell. To begin to explore whether isoactin sequence diversity leads to functional differences in actin filaments, we have examined the phalloidin binding kinetics and the bulk rheologic properties of purified actin isoforms from a variety of eukaryotic sources. We observe differences in the phalloidin association kinetics between muscle alpha- and cytoplasmic actins. Phalloidin dissociates from all mammalian actin isoforms tested at the same slow rate, while dissociation from yeast actin is 1 order of magnitude more rapid. The actin isoforms form viscoelastic gels to varying degrees with skeletal muscle alpha-actin gels being the most elastic, smooth muscle alpha- and gamma-actins being less elastic, and beta-actin not forming elastic structures under our experimental conditions. The sequence variation among isoforms is discussed in light of these biophysical and biochemical differences. |
| Author | Käs, J Herman, I. M Janmey, P. A Allen, P. G Chaponnier, C Shuster, C. B |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/8916891$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1038/345089a0 10.1016/S0006-3495(91)82194-4 10.1016/S0021-9258(17)43188-7 10.1016/S0006-3495(93)81035-X 10.1111/j.1432-1033.1980.tb04397.x 10.1083/jcb.123.5.1185 10.1038/347044a0 10.1083/jcb.130.4.887 10.1016/S0955-0674(05)80007-9 10.1083/jcb.112.4.653 10.1016/0966-7822(93)90020-I 10.1083/jcb.128.5.837 10.1083/jcb.109.1.191 10.1006/jmbi.1993.1628 10.1016/S0021-9258(18)31663-6 10.1016/0014-5793(92)80975-M 10.1002/jcb.240440406 10.1152/ajpcell.1992.262.3.C569 10.1083/jcb.131.6.1759 10.1103/PhysRevLett.75.4425 10.1093/oxfordjournals.jbchem.a123929 |
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| Copyright | Copyright © 1996 American Chemical Society |
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| Notes | Abstract published in Advance ACS Abstracts, October 15, 1996. Supported by a Grant in Aid from the American Heart Association, Massachusetts Affiliate, to P.G.A., by CF Foundation Research Grant G957 to P.A.J., and by Swiss National Science Foundation Grant 31.43582.95 to C.C. istex:3E0009B32417BBB90529C723B3642DEB8159BE43 ark:/67375/TPS-6TWZP59G-2 |
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| SubjectTerms | Actins - chemistry Animals Cattle Cell-Free System Chickens Elasticity Kinetics Models, Molecular Muscle, Skeletal - chemistry Muscle, Smooth - chemistry Phalloidine - chemistry Protein Structure, Tertiary Rabbits Rheology Saccharomyces cerevisiae Structure-Activity Relationship Viscosity |
| Title | Phalloidin Binding and Rheological Differences among Actin Isoforms |
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