| Literature DB >> 8293475 |
E L de Hostos1, B Bradtke, F Lottspeich, G Gerisch.
Abstract
A 17 kDa protein, designated as coactosin, has been purified from an actin-myosin complex reconstituted in vitro from a soluble fraction of Dictyostelium discoideum cells. The protein binds to F-actin in vitro without significantly altering its viscosity. Immunoblots labeled with monoclonal antibodies indicate that part of the protein is associated with the detergent-insoluble cytoskeleton. cDNA clones comprising the entire coding region of coactosin have been isolated from an expression library. The cDNA-derived amino-acid sequence reveals similarities of coactosin to the drebrins identified in neurons and to actin-binding proteins from other organisms, including yeast ABP1p, and yeast and vertebrate cofilins.Entities:
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Year: 1993 PMID: 8293475 DOI: 10.1002/cm.970260302
Source DB: PubMed Journal: Cell Motil Cytoskeleton ISSN: 0886-1544