Glial fibrillary acidic protein: dynamic property and regulation by phosphorylation

Abstract

Glial fibrillary acidic protein (GFAP) is an intermediate filament (IF) protein of astroglia, and belongs to the type III subclass of IF proteins. IF proteins are composed of an amino-terminal HEAD domain, a central ROD domain and a carboxyterminal TAIL domain. GFAP, with a molecular mass of approximately 50 KDa, has the smallest HEAD domain among type III IF proteins. Despite its insolubility, GFAP is in dynamic equilibrium between assembled filaments and unassembled subunits, as demonstrated using fluorescently labeled GFAP molecules. Like other IF proteins, assembly of GFAP is regulated by phosphorylation-dephosphorylation of the HEAD domain by altering its charge. This regulation of GFAP assembly contributes to extensive remodeling of glial frameworks in mitosis. Another type III IF protein, vimentin, colocalizes with GFAP in immature, reactive or radial glia, thereby indicating that vimentin has an important role in the build up of the glial architecture.