DYNAMIC PROPERTY OF INTERMEDIATE FILAMENTS - REGULATION BY PHOSPHORYLATION

Site-specific phosphorylation of intermediate filament (IF) proteins o n serine and threonine residues leads to alteration of the filament st ructure, in vitro and in vivo. Protein kinases involved in cell signal ing and those activated in mitosis dynamically control spatial and tem poral organization of intracellular IF phosphorylation. Thus, IF phosp horylation appears to be one of the most predominant strategies in coo rdinating intracellular organization of the IF network.