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Spectrin and protein 4.1 as an actin filament capping complex
Author(s) -
Pinder Jennifer C.,
Ohanian V.,
Gratzer W.B.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80310-5
Subject(s) - spectrin , actin , cytoskeleton , protein filament , actin remodeling , chemistry , epb41 , biophysics , actin binding protein , microfilament , cytochalasin d , treadmilling , microbiology and biotechnology , biochemistry , actin cytoskeleton , biology , cell
Spectrin and protein 4.1, when added to G‐ or F‐actin, cause the formation of short filaments, as judged by the appearance of powerful nucleating activity for G‐actin polymerisation. F‐Actin filaments are rapidly fragmented under physiological solvent conditions. The effect of cytochalasin E on the polymerisation reaction and the extent of reduction in the critical monomer concentration of actin when spectrin and 4.1 are added suggest that these proteins form a capping system for the more slowly growing, or ‘pointed’ ends of actin filaments. The interaction is not affected by calcium or by 4.9, the remaining constituent of the purified red cell membrane cytoskeleton.