Self-association of chicken gizzard filamin and heavy merofilamin.
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Filamin is a high molecular weight (subunit Mr 250 000) actin-binding protein isolated from smooth muscle. The protein forms a gel when mixed with solutions of F-actin. A proteolytic fragment of filamin, heavy merofilamin (subunit Mr 240 000), generated by the action of Ca2+-activated protease binds to actin but does not produce gelation. We have studied the self-association properties of filamin and heavy merofilamin by direct examination in the electron microscope and by equilibrium sedimentation distribution studies in the ultracentrifuge. Filamin self-associates reversibly to form dimers; the free energy of dimerization is approximately 7 kcal/mol. Further association to form tetramer and multimer appears to be irreversible. Warming of filamin solutions accelerates aggregation. Heavy merofilamin does not appear to self-associate but is entirely monomeric. These studies suggest that filamin produces gelation of F-actin by binding to actin and then self-associating to cross-link actin filaments into a gel.
author list (cited authors)
Davies, P. J., Wallach, D., Willingham, M., Pastan, I., & Lewis, M. S.
complete list of authors
Davies, PJ||Wallach, D||Willingham, M||Pastan, I||Lewis, MS