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The biological function of protein assemblies was conventionally equated witha unique three-dimensional protein structure and protein-specific interactions.However, in the past 20 years it was found that some assemblies contain longflexible regions that adopt multiple structural conformations. These includeneurofilament (NF) proteins that constitute the stress-responsive supportivenetwork of neurons. Herein, we show that NF networks macroscopic properties aretuned by enzymatic regulation of the charge found on the flexible proteinregions. The results reveal an enzymatic (phosphorylation) regulation ofmacroscopic properties such as orientation, stress-response and expansion inflexible protein assemblies. Together with a model explaining the attractiveelectrostatic interactions induced by enzymatically added charges, wedemonstrate that phosphorylation-regulation is far richer and versatile thanpreviously considered.

Phosphorylation-induced mechanical regulation of intrinsically disordered neurofilament protein assemblies