Journal
BIOPHYSICAL JOURNAL
Volume 112, Issue 5, Pages 892-900Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2016.12.050
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Funding
- Israeli Scientific Foundation [571/11, 550/15]
- Tel Aviv University Center for Nanoscience, Nanotechnology
- Abramson Center for Medical Physics
- Scakler Institute for Biophysics at Tel Aviv University
- BioStruct-X
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The biological function of protein assemblies has been conventionally equated with a unique three-dimensional protein structure and protein-specific interactions. However, in the past 20 years it has been found that some assemblies contain long flexible regions that adopt multiple structural conformations. These include neurofilament proteins that constitute the stress-responsive supportive network of neurons. Herein, we show that the macroscopic properties of neurofilament networks are tuned by enzymatic regulation of the charge found on the flexible protein regions. The results reveal an enzymatic (phosphorylation) regulation of macroscopic properties such as orientation, stress response, and expansion in flexible protein assemblies. Using a model that explains the attractive electrostatic interactions induced by enzymatically added charges, we demonstrate that phosphorylation regulation is far richer and versatile than previously considered.
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