J. Biochem, 1994, Vol. 116, No. 2 426-434
© 1994 Japanese Biochemical Society
research-article |
Identification of Phosphorylation Sites on Glial Fibrillary Acidic Protein for cdc2 Kinase and Ca2+-Calmodulin-Dependent Protein Kinase II1
*Department of Neurophysiology, Tokyo Metropolitan Institute of Gerontology 35-2 Sakae-cho, Itabashi-ku, Tokyo 173
Department of Thoracic and Cardiovascular Surgery Edobashi, Tsu, Mie 514
|Department of Pathology, Mie University School of MedicineEdobashi Tsu, Mie 514
Biophysics Unit, Aichi Cancer Center Research Institute Chikusa-ku, Nagoya, Aichi 464
Department of Molecular Neurobiology, Tokyo Metropolitan Institute for Neurosciences Fuchu, Tokyo 183
¶Department of Biochemistry, Faculty of Pharmaceutical Sciences, University of Tokushima Shomachi, Tokushima 770
2To whom correspondence should be addressed.
We identified the phosphorylation sites of glial fibrillary acidic protein (GFAP) for cdc2 kinase and Ca2+-calmodulin (CaM)-dependent protein kinase II. GFAP was phosphorylated to 
0.2 mol of phosphate/mol of GFAP by cdc2 kinase, and this phosphorylation did not induce disassembly of the filament structure. On the other hand, GFAP was phosphorylated to 1.9 mol of phosphate/mol of GFAP by Ca2+-CaM-dependent protein kinase II, and this phosphorylation did induce disassembly of the filament. Sequential analysis of the purified phosphopeptides revealed that only Ser8 on GFAP was phosphorylated by cdc2 kinase, whereas Serl3, Serl7, Ser34, and Ser389 on GFAP were phosphorylated by Ca2+-CaM-dependent protein kinase II.
1This research was aupported in part by a Grant-in-Aid for Scientific Research and a Grant for Cancer Research from the Ministry of Education, Science and Culture of Japan, and special coordination funds from the Science and Technology Agency of the Government of Japan; and in part by The Uehara Memorial Foundation.
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