Phosphorylation-induced mechanical regulation of intrinsically disordered neurofilament protein assemblies
arXiv:1609.05546 · doi:10.1016/j.bpj.2016.12.050
Abstract
The biological function of protein assemblies was conventionally equated with a unique three-dimensional protein structure and protein-specific interactions. However, in the past 20 years it was found that some assemblies contain long flexible regions that adopt multiple structural conformations. These include neurofilament (NF) proteins that constitute the stress-responsive supportive network of neurons. Herein, we show that NF networks macroscopic properties 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. Together with a model explaining the attractive electrostatic interactions induced by enzymatically added charges, we demonstrate that phosphorylation-regulation is far richer and versatile than previously considered.
9 pages, 5 figures
References in corpus (1)
Cited by in corpus (6)
- Glassy dynamics and memory effects in an intrinsically disordered protein construct
- Order from disorder with intrinsically disordered peptide amphiphiles
- Intramolecular Structural Heterogeneity altered by Long-range Contacts in an Intrinsically Disordered Protein
- Nanoparticle mobility over a surface as a probe for weak transient disordered peptide-peptide interactions
- Intrinsically Disordered Proteins at the Nano-scale
- From isolated polyelectrolytes to star-like assemblies: The role of sequence heterogeneity on the statistical structure of the intrinsically disordered Neurofilament-low tail domain