The distribution of cofilin and Dnase I in vivo |
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Authors: | DEEPAK CHHABRA SHISAN BAO CRISTOBAL G DOS REMEDIOS |
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Affiliation: | Muscle Research Unit, Department of Anatomy and Histology, Department of Pathology, Institute for Biomedical Research, F13, University of Sydney, NSW 2006, Australia Muscle Research Unit, Department of Anatomy and Histology, Department of Pathology, Institute for Biomedical Research, F13, University of Sydney, NSW 2006, Australia Muscle Research Unit, Department of Anatomy and Histology, Department of Pathology, Institute for Biomedical Research, F13, University of Sydney, NSW 2006, Australia |
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Abstract: | Actin is the principal component of the cytoskeleton, a structure that can be disassembled and reassem-bled in a matter of seconds in vivo. The state of assembly of actin in vivo is primarily regulated by one ormore actin binding proteins (ABPs). Typically, the actions of ABPs have been studied one by one, however,we propose that multiple ABPs, acting cooperatively, may be involved in the control of actin filament length.Cofilin and DNase I are two ABPs that have previously been demonstrated to form a ternary complex withactin in vitro. This is the first report to demonstrate their co-localisation in vivo, and differences in theirdistributions. Our observations strongly suggest a physiological role for higher order complexes of actin inregulation of cytoskeletal assembly during processes such as cell division. |
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Keywords: | actin cofilin DNase I actin-binding protein ternary complex. |
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