The distribution of cofilin and DNase I in vivo.
Actin is the principal component of the cytoskeleton, a structure that can be disassembled and reassembled in a matter of seconds in vivo. The state of assembly of actin in vivo is primarily regulated by one or more 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 with actin in vitro. This is the first report to demonstrate their co-localisation in vivo, and differences in their distributions. Our observations strongly suggest a physiological role for higher order complexes of actin in regulation of cytoskeletal assembly during processes such as cell division.
Chhabra
Deepak
D
dchhabra@anatomy.usyd.edu.au
Bao
Shisan
S
dos Remedios
Cristobal G
CG
D051339:Actin Depolymerizing Factors; D000818:Animals; D002642:Chick Embryo; D002522:Chlorocebus aethiops; D003850:Deoxyribonuclease I / Q000378:metabolism*; D008840:Microfilament Proteins / Q000302:isolation & purification / Q000378:metabolism*; D015394:Molecular Structure; D018482:Muscle, Skeletal / Q000737:chemistry; D011485:Protein Binding; D014018:Tissue Distribution; D014709:Vero Cells
D051339:Actin Depolymerizing Factors; D008840:Microfilament Proteins; D003850:Deoxyribonuclease I