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Papers In Press, published online ahead of print June 10, 2002
J. Biol. Chem, 10.1074/jbc.M112121200
Submitted on December 19, 2001
Revised on May 29, 2002
Accepted on June 10, 2002

A new splice form of glial fibrillary acidic protein, GFAPe, interacts with the presenilin proteins

Anders L. Nielsen, Ida E. Holm, Marianne Johansen, Bjarne J. Bonven, Poul Jørgensen, and Arne L. Jørgensen

Department of Molecular Biology, University of Aarhus, Aarhus C DK-8000

Corresponding Author: aln{at}mbio.aau.dk

We describe a new human isoform, GFAPe, of the intermediary filament protein GFAP (Glial Fibrillary Acidic Protein). GFAPe mRNA is a result of alternative splicing and a new polyadenylation signal, and thus GFAPe has a new C-terminal protein sequence. This provides GFAPe with a capacity for specific binding of presenilin proteins in yeast and in vitro. Our observations suggest a direct link between the presenilins and the cytoskeleton where GFAPe is incorporated. Mutations in GFAP and presenilins are associated with Alexander disease and Alzheimer's disease, respectively. Accordingly, GFAPe should be taken into consideration when studying neurodegenerative diseases.


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