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Supramolecular cellular filament systems: How and why do they form?
Author(s) -
Popp David,
Robinson Robert C.
Publication year - 2012
Publication title -
cytoskeleton
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.95
H-Index - 86
eISSN - 1949-3592
pISSN - 1949-3584
DOI - 10.1002/cm.21006
Subject(s) - biology , protein filament , actin , cytoskeleton , microtubule , function (biology) , multicellular organism , mreb , microbiology and biotechnology , biophysics , cell , biochemistry
All cells, from simple bacteria to complex human tissues, rely on extensive networks of protein fibers to help maintain their proper form and function. These filament systems usually do not operate as single filaments, but form complex suprastructures, which are essential for specific cellular functions. Here, we describe the progress in determining the architectures of molecular filamentous suprastructures, the principles leading to their formation, and the mechanisms by which they may facilitate function. The complex eukaryotic cytoskeleton is tightly regulated by a large number of actin‐ or microtubule‐associated proteins. In contrast, recently discovered bacterial actins and tubulins have few associated regulatory proteins. Hence, the quest to find basic principles that govern the formation of filamentous suprastructures is simplified in bacteria. Three common principles, which have been probed extensively during evolution, can be identified that lead to suprastructures formation: cationic counterion fluctuations; self‐association into liquid crystals; and molecular crowding. The underlying physics of these processes will be discussed with respect to physiological circumstance. © 2012 Wiley Periodicals, Inc

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