Phosphorylation sites linked to glial filament disassembly in vitro locate in a non-alpha-helical head domain

Glial fibrillary acidic protein (GFAP), the intermediate filament component of astroglial cells, can serve as an excellent substrate for both cAMP-dependent protein kinase and protein kinase C, in vitro. GFAP phosphorylated by each protein kinase does not polymerize, and the filaments that do polyme...

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Bibliographic Details
Published in:The Journal of biological chemistry 1990-03, Vol.265 (8), p.4722-4729
Main Authors: Inagaki, M, Gonda, Y, Nishizawa, K, Kitamura, S, Sato, C, Ando, S, Tanabe, K, Kikuchi, K, Tsuiki, S, Nishi, Y
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Brain Chemistry
Cattle
Cyclic AMP - pharmacology
Cytoskeleton - metabolism
Desmin - metabolism
glial cells
Glial Fibrillary Acidic Protein - metabolism
Hydrogen-Ion Concentration
Intermediate Filaments - metabolism
Intermediate Filaments - ultrastructure
Kinetics
Microscopy, Electron
Neuroglia - ultrastructure
Phosphates - metabolism
Phosphorylation
Polymers - metabolism
Protein Kinase C - metabolism
Protein Kinases - metabolism
Rats
Swine
Vimentin - metabolism
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Summary:Glial fibrillary acidic protein (GFAP), the intermediate filament component of astroglial cells, can serve as an excellent substrate for both cAMP-dependent protein kinase and protein kinase C, in vitro. GFAP phosphorylated by each protein kinase does not polymerize, and the filaments that do polymerize tend to depolymerize after phosphorylation. Dephosphorylation of phospho-GFAP by phosphatase led to a recovery of the polymerization competence of GFAP. Most of the phosphorylation sites for cAMP-dependent protein kinase and protein kinase C on GFAP are the same, Ser-8, Ser-13, and Ser-34. cAMP-dependent protein kinase has one additional phosphorylation site, Thr-7. All the sites are located within the amino-terminal non-alpha-helical head domain of GFAP. These observations pave the way for in vivo studies on organization of glial filaments.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(19)39622-x