ArticleThe Journal of cell biology1984
Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia.
Article in The Journal of cell biology, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 25 citations in OpenAlex.
- Phosphorylation facilitates the integrin binding of filamin under force.Biophysical journal · 2009Article
- Molecular mechanics of filamin's rod domain.Biophysical journal · 2008Article
- Regulation by Ca(2+)-calmodulin of the actin-bundling activity of Physarum 210-kDa protein.Journal of muscle research and cell motility · 1992Article
- Control of actin filament length by phosphorylation of fragmin-actin complex.The Journal of cell biology · 1990Article
- Purification of myxamoebal fragmin, and switching of myxamoebal fragmin to plasmodial fragmin during differentiation of Physarum polycephalum.Journal of muscle research and cell motility · 1988Article
- Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins.The Journal of cell biology · 1984Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A high molecular weight actin-binding protein was isolated from the Physarum polycephalum plasmodia. The protein ( HMWP ) shares many properties with other high molecular weight actin-binding proteins such as spectrin, actin-binding protein from macrophages, and filamin. It has a potent activity to cross-link F-actin into a gel-like structure. Its cross-linking activity does not depend on calcium concentrations. Hydrodynamic studies have revealed that the protein is in the monomeric state of a polypeptide chain with molecular weight of approximately 230,000 in a high ionic strength solvent, while it self-associates into a dimer under physiological ionic conditions. Electron microscopic examinations of HMWP have shown that the monomer particle observed in a high ionic strength solvent is rod shaped with the two-stranded morphology very similar to that of spectrin. On the other hand, under physiological ionic conditions, the HMWP dimer shows the dumb-bell shape with two globular domains connected with a thin flexible strand.
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