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Tracking down the different forms of nuclear actin

Jockusch, B. M. and Schoenenberger, C. A. and Stetefeld, J. and Aebi, U.. (2006) Tracking down the different forms of nuclear actin. Trends in cell biology, Vol. 16, H. 8. pp. 391-396.

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Official URL: http://edoc.unibas.ch/dok/A5258877

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Abstract

Actin is a rather uncommitted protein with a high degree of structural plasticity: it can adopt a variety of structural states, depending on the specific ionic conditions or the interaction with ligand proteins. These interactions lock actin into a distinct conformation, which specifies the oligomeric or polymeric form it can assume. The interplay between monomeric, oligomeric and polymeric forms is used by the cell to execute an enormous variety of motility processes, such as lamellipodium formation during locomotion or intracellular transport of vesicles. In these cytoplasmic events, monomeric G-actin and filamentous F-actin are the prevalent forms. However, there might be other structural states of actin in cells that have so far not received the attention they deserve. Here, we propose that specific, "unconventional" actin conformations might contribute especially to the multitude of functions executed by actin in the nucleus. We present evidence for the existence of different forms of nuclear actin, taken from studies with selected antibodies.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Aebi)
05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Schoenenberger)
UniBasel Contributors:Schoenenberger, Cora-Ann and Aebi, Ueli
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Elsevier
ISSN:0962-8924
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:14 Sep 2012 06:50
Deposited On:22 Mar 2012 13:29

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