Crosslinking of actin filaments is caused by caldesmon aggregates, but not by its dimers

A recent report by Bretscher [(1984) J. Biol. Chem. 259, 12873-12880] showed that caldesmon prepared by his method crosslinks actin filaments to form thick bundles. This is in contrast to the results of previous work that caldesmon binds to F-actin but does not cause any gelation [(1981) Proc. Natl....

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Veröffentlicht in:	FEBS letters 1985-03, Vol.182 (1), p.201-204
Hauptverfasser:	Sobue, Kenji, Takahashi, Katsuhito, Tanaka, Toshihiko, Kanda, Keiko, Ashino, Nobuhiko, Kakiuchi, Shiro, Maruyama, Koscak
Format:	Artikel
Sprache:	eng
Schlagworte:	actin Actins - metabolism aggregation Analytical, structural and metabolic biochemistry Animals Biological and medical sciences caldesmon calmodulin Calmodulin-Binding Proteins Chickens Chromatography, Gel Contractile proteins DTT, dithiothreitol Fundamental and applied biological sciences. Psychology Gizzard, Avian - analysis Holoproteins Macromolecular Substances Microscopy, Electron Phosphoprotein Phosphatases - metabolism Proteins
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Zusammenfassung:	A recent report by Bretscher [(1984) J. Biol. Chem. 259, 12873-12880] showed that caldesmon prepared by his method crosslinks actin filaments to form thick bundles. This is in contrast to the results of previous work that caldesmon binds to F-actin but does not cause any gelation [(1981) Proc. Natl. Acad. Sci. USA 78, 5652-5655]. The present work clearly showed that caldesmon purified according to Bretscher does not cause any gelation of F-actin. However, caldesmon aggregates formed by concentration or by freeze-thawing gelated F-actin to form bundles. Caldesmon Actin-associated protein Calmodulin-binding protein Actin-crosslinker Chicken gizzard
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(85)81184-4