دورية أكاديمية
ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments
| العنوان: | ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments |
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| المؤلفون: | Galkin, Vitold E., Orlova, Albina, VanLoock, Margaret S., Shvetsov, Alexander, Reisler, Emil, Egelman, Edward H. |
| المصدر: | The Journal of Cell Biology ; volume 163, issue 5, page 1057-1066 ; ISSN 1540-8140 0021-9525 |
| بيانات النشر: | Rockefeller University Press |
| سنة النشر: | 2003 |
| الوصف: | Proteins in the ADF/cofilin (AC) family are essential for rapid rearrangements of cellular actin structures. They have been shown to be active in both the severing and depolymerization of actin filaments in vitro, but the detailed mechanism of action is not known. Under in vitro conditions, subunits in the actin filament can treadmill; with the hydrolysis of ATP driving the addition of subunits at one end of the filament and loss of subunits from the opposite end. We have used electron microscopy and image analysis to show that AC molecules effectively disrupt one of the longitudinal contacts between protomers within one helical strand of F-actin. We show that in the absence of any AC proteins, this same longitudinal contact between actin protomers is disrupted at the depolymerizing (pointed) end of actin filaments but is prominent at the polymerizing (barbed) end. We suggest that AC proteins use an intrinsic mechanism of F-actin's internal instability to depolymerize/sever actin filaments in the cell. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| DOI: | 10.1083/jcb.200308144 |
| الإتاحة: | https://doi.org/10.1083/jcb.200308144Test https://rupress.org/jcb/article-pdf/163/5/1057/1527372/jcb16351057.pdfTest |
| رقم الانضمام: | edsbas.3FA3E7EE |
| قاعدة البيانات: | BASE |
| DOI: | 10.1083/jcb.200308144 |
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