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Reconstitution of cytoskeletal protein assemblies for large-scale membrane transformation

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons79158

Vogel,  Sven K.
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons15815

Schwille,  Petra
Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Rivas, G., Vogel, S. K., & Schwille, P. (2014). Reconstitution of cytoskeletal protein assemblies for large-scale membrane transformation. CURRENT OPINION IN CHEMICAL BIOLOGY, 22, 18-26. doi:10.1016/j.cbpa.2014.07.018.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-90D1-1
Zusammenfassung
Membranes determine two-dimensional and three-dimensional biochemical reaction spaces in living systems. Defining size and shape of surfaces and volumes encompassed by membrane is of key importance for cellular metabolism and homeostasis, and the maintenance and controlled transformation of membrane shapes are coordinated by a large number of different protein assemblies. The orchestration of spatial elements over distances orders of magnitudes larger than protein molecules, as required for cell division, is a particularly challenging task, requiring large-scale ordered protein filaments and networks. The structure and function of these networks, particularly of cytoskeletal elements, have been characterized extensively in cells and reconstituted systems. However, their co-reconstitution with membranes from the bottom-up under defined conditions, to elucidate their mode of action in detail, is still a relatively new field of research. In this short review, we discuss recent approaches and achievements with regard to the study of cytoskeletal protein assemblies on model membranes, with specific focus on contractile elements as those based on the bacterial division FtsZ protein and eukaryotic actomyosin structures.